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Q13315 (ATM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine-protein kinase ATM

EC=2.7.11.1
Alternative name(s):
Ataxia telangiectasia mutated
Short name=A-T mutated
Gene names
Name:ATM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3056 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.29 Ref.34 Ref.35 Ref.38 Ref.40 Ref.42 Ref.44 Ref.51

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.15 Ref.18

Enzyme regulation

Inhibited by wortmannin. Ref.17

Subunit structure

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. Ref.16 Ref.18 Ref.19 Ref.31 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.41 Ref.43 Ref.46 Ref.48 Ref.49 Ref.52 Ref.53 Ref.54

Subcellular location

Nucleus. Cytoplasmic vesicle. Note: Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin. Ref.13 Ref.14

Tissue specificity

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

Induction

By ionizing radiation. Ref.17

Domain

The FATC domain is required for interaction with KAT5.

Post-translational modification

Phosphorylated by NUAK1/ARK5. Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA damage-mediated activation of the kinase. Ref.12 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.32 Ref.33 Ref.34 Ref.41 Ref.42 Ref.56

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. Ref.41 Ref.44

Involvement in disease

Ataxia telangiectasia (AT) [MIM:208900]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.9 Ref.14 Ref.24 Ref.34 Ref.41 Ref.42 Ref.43 Ref.44 Ref.56 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.66 Ref.67 Ref.68 Ref.69 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.80 Ref.82 Ref.83 Ref.87 Ref.88

Defects in ATM 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.

Defects in ATM contribute to B-cell non-Hodgkin lymphomas (BNHL), including mantle cell lymphoma (MCL). Ref.64

Defects in ATM 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. Ref.78 Ref.79 Ref.84

Sequence similarities

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

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 1 PI3K/PI4K domain.

Sequence caution

The sequence AAA86520.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA86520.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAI37170.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAI37170.1 differs from that shown. Reason: Probable cloning artifact.

The sequence EAW67111.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
   Cellular componentCytoplasmic vesicle
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Neurodegeneration
Tumor suppressor
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage induced protein phosphorylation

Inferred from direct assay Ref.21. Source: BHF-UCL

DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from mutant phenotype PubMed 15149599. Source: BHF-UCL

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

cellular response to gamma radiation

Inferred from direct assay PubMed 9925639. Source: BHF-UCL

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

histone mRNA catabolic process

Inferred from direct assay Ref.40. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

lipoprotein catabolic process

Inferred from electronic annotation. Source: Ensembl

mitotic spindle assembly checkpoint

Inferred from mutant phenotype PubMed 11943150. Source: UniProtKB

negative regulation of B cell proliferation

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

oocyte development

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from direct assay Ref.21. Source: BHF-UCL

phosphatidylinositol-3-phosphate biosynthetic process

Inferred from mutant phenotype Ref.30. Source: GOC

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype Ref.21. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

pre-B cell allelic exclusion

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay PubMed 15790808Ref.21. Source: BHF-UCL

protein phosphorylation

Inferred from direct assay Ref.38. Source: UniProtKB

reciprocal meiotic recombination

Traceable author statement Ref.9. Source: ProtInc

replicative senescence

Inferred from mutant phenotype PubMed 15149599. Source: BHF-UCL

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from direct assay Ref.30. Source: UniProtKB

signal transduction

Traceable author statement Ref.9. Source: ProtInc

signal transduction involved in mitotic G2 DNA damage checkpoint

Inferred from mutant phenotype PubMed 15149599. Source: BHF-UCL

somitogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from mutant phenotype Ref.30. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent protein kinase activity

Inferred from direct assay PubMed 15790808. Source: BHF-UCL

histone serine kinase activity

Inferred from electronic annotation. Source: Ensembl

protein N-terminus binding

Inferred from direct assay Ref.30. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.30PubMed 16452482Ref.49. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 15790808. Source: BHF-UCL

protein dimerization activity

Inferred from direct assay PubMed 15790808. Source: BHF-UCL

protein serine/threonine kinase activity

Inferred from direct assay Ref.30PubMed 20096447. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.57
Chain2 – 30563055Serine-protein kinase ATM
PRO_0000088840

Regions

Domain1960 – 2566607FAT
Domain2712 – 2962251PI3K/PI4K
Domain3024 – 305633FATC
Region1373 – 138210Interaction with ABL1

Amino acid modifications

Modified residue21N-acetylserine Ref.57
Modified residue3671Phosphoserine; by autocatalysis Ref.42
Modified residue18931Phosphoserine; by autocatalysis Ref.42
Modified residue19811Phosphoserine; by autocatalysis Ref.34 Ref.41 Ref.42 Ref.45 Ref.56
Modified residue19831Phosphoserine Ref.45
Modified residue29961Phosphoserine Ref.47 Ref.50
Modified residue30161N6-acetyllysine Ref.44

Natural variations

Natural variant231R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041545
Natural variant451R → W.
Corresponds to variant rs3218684 [ dbSNP | Ensembl ].
VAR_056678
Natural variant491S → C. Ref.2 Ref.60 Ref.81 Ref.82 Ref.90
Corresponds to variant rs1800054 [ dbSNP | Ensembl ].
VAR_010798
Natural variant1261D → E. Ref.73 Ref.90
Corresponds to variant rs2234997 [ dbSNP | Ensembl ].
VAR_010799
Natural variant1401D → H. Ref.90
VAR_041546
Natural variant1821V → L. Ref.81
Corresponds to variant rs3218707 [ dbSNP | Ensembl ].
VAR_010800
Natural variant2241K → E in AT. Ref.87
VAR_010801
Natural variant2501R → Q. Ref.90
VAR_041547
Natural variant2921P → L in AT; associated with lymphoma. Ref.67
VAR_010802
Natural variant3231I → V in AT. Ref.87
VAR_010803
Natural variant3321Y → C in B-cell chronic lymphocytic leukemia. Ref.79
VAR_010804
Natural variant3331S → F. Ref.90
Corresponds to variant rs28904919 [ dbSNP | Ensembl ].
VAR_041548
Natural variant3371R → C in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041549
Natural variant3371R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041550
Natural variant3501A → T in B-cell chronic lymphocytic leukemia. Ref.84
VAR_010805
Natural variant3521I → T in B-cell chronic lymphocytic leukemia. Ref.84
VAR_010806
Natural variant4101V → A. Ref.90
VAR_041551
Natural variant5041N → S. Ref.90
Corresponds to variant rs56365018 [ dbSNP | Ensembl ].
VAR_041552
Natural variant5141G → D. Ref.73 Ref.90
Corresponds to variant rs2235000 [ dbSNP | Ensembl ].
VAR_010807
Natural variant5401C → Y in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041553
Natural variant5461L → V. Ref.90
Corresponds to variant rs2227924 [ dbSNP | Ensembl ].
VAR_041554
Natural variant5701F → S in AT. Ref.82
VAR_010808
Natural variant5821F → L. Ref.90
Corresponds to variant rs2235006 [ dbSNP | Ensembl ].
VAR_041555
Natural variant705 – 7073YSS → FIP in AT; might be associated with susceptibility to cancer.
VAR_010809
Natural variant7071S → P. Ref.81 Ref.90
Corresponds to variant rs4986761 [ dbSNP | Ensembl ].
VAR_010810
Natural variant7611T → S.
Corresponds to variant rs2235011 [ dbSNP | Ensembl ].
VAR_056679
Natural variant7681N → D in AT. Ref.67
VAR_010812
Natural variant7851R → C in AT. Ref.82
VAR_010813
Natural variant7881S → R.
Corresponds to variant rs641252 [ dbSNP | Ensembl ].
VAR_056680
Natural variant8141D → E.
Corresponds to variant rs3218695 [ dbSNP | Ensembl ].
VAR_056681
Natural variant8481E → Q in a lung adenocarcinoma sample; somatic mutation. Ref.90
VAR_041556
Natural variant8581F → L Rare polymorphism. Ref.60 Ref.61 Ref.74 Ref.81 Ref.82 Ref.90
Corresponds to variant rs1800056 [ dbSNP | Ensembl ].
VAR_010814
Natural variant8721P → S. Ref.90
Corresponds to variant rs3218673 [ dbSNP | Ensembl ].
VAR_041557
Natural variant9241R → W. Ref.90
VAR_041558
Natural variant9351T → A. Ref.90
VAR_041559
Natural variant9351T → M.
Corresponds to variant rs3218708 [ dbSNP | Ensembl ].
VAR_056682
Natural variant9421L → F.
Corresponds to variant rs3218688 [ dbSNP | Ensembl ].
VAR_056683
Natural variant9501L → R in AT.
VAR_010815
Natural variant10011L → Q in AT; associated with T-cell acute lymphoblastic leukemia. Ref.67
VAR_010816
Natural variant10401M → V in B-cell non-Hodgkin lymphoma. Ref.64
Corresponds to variant rs3092857 [ dbSNP | Ensembl ].
VAR_010817
Natural variant10541P → R. Ref.2 Ref.60 Ref.61 Ref.74 Ref.82 Ref.84 Ref.85 Ref.90
Corresponds to variant rs1800057 [ dbSNP | Ensembl ].
VAR_010818
Natural variant10821H → L in AT.
VAR_010819
Natural variant10911E → D in AT. Ref.74
VAR_010820
Natural variant11791S → F in a gastric adenocarcinoma sample; somatic mutation. Ref.90
VAR_041560
Natural variant13131E → Q.
Corresponds to variant rs3092841 [ dbSNP | Ensembl ].
VAR_056684
Natural variant13211M → I. Ref.90
VAR_041561
Natural variant13801H → Y. Ref.90
VAR_041562
Natural variant13821P → S. Ref.90
VAR_041563
Natural variant14071I → T in T-prolymphocytic leukemia. Ref.64
VAR_010821
Natural variant14201L → F Rare polymorphism. Ref.2 Ref.60 Ref.81 Ref.90
Corresponds to variant rs1800058 [ dbSNP | Ensembl ].
VAR_010822
Natural variant14201L → P in AT. Ref.87
VAR_010823
Natural variant14271A → T.
Corresponds to variant rs2229021 [ dbSNP | Ensembl ].
VAR_056685
Natural variant14541K → N. Ref.83
VAR_010824
Natural variant14631F → S in B-cell non-Hodgkin lymphoma. Ref.64
VAR_010825
Natural variant14651L → P in AT. Ref.80
VAR_010826
Natural variant14691I → M in a renal papillary cancer sample; somatic mutation. Ref.90
VAR_041564
Natural variant14751Y → C. Ref.90
VAR_041565
Natural variant15411L → F.
Corresponds to variant rs3092849 [ dbSNP | Ensembl ].
VAR_056686
Natural variant15661P → R in AT. Ref.74
VAR_010827
Natural variant15701V → A. Ref.81
Corresponds to variant rs140856217 [ dbSNP | Ensembl ].
VAR_010828
Natural variant16501N → S. Ref.90
Corresponds to variant rs55870064 [ dbSNP | Ensembl ].
VAR_041566
Natural variant16821D → H in T-prolymphocytic leukemia. Ref.64
VAR_010829
Natural variant16911S → R in AT and B-cell chronic lymphocytic leukemia; unknown pathological significance. Ref.60 Ref.67 Ref.79
Corresponds to variant rs1800059 [ dbSNP | Ensembl ].
VAR_010830
Natural variant17291V → L.
Corresponds to variant rs3092907 [ dbSNP | Ensembl ].
VAR_056687
Natural variant17391N → T in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041567
Natural variant17431T → I in AT; associated with preleukemic T-cell proliferation. Ref.67
VAR_010831
Natural variant1812 – 18132AF → V in AT.
VAR_010832
Natural variant18531D → N Common polymorphism. Ref.73 Ref.78 Ref.81 Ref.82 Ref.83 Ref.90
Corresponds to variant rs1801516 [ dbSNP | Ensembl ].
VAR_010833
Natural variant18531D → V Might contribute to B-cell chronic lymphocytic leukemia. Ref.71 Ref.78 Ref.82 Ref.87 Ref.90
Corresponds to variant rs1801673 [ dbSNP | Ensembl ].
VAR_010834
Natural variant19101L → H in T-prolymphocytic leukemia. Ref.64
VAR_010835
Natural variant19131V → G in AT. Ref.82
VAR_010836
Natural variant19161M → I in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.90
VAR_041568
Natural variant19451A → T in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041569
Natural variant19531T → R in B-cell chronic lymphocytic leukemia. Ref.78
VAR_010837
Natural variant19611Y → C. Ref.90
VAR_041570
Natural variant19831S → N. Ref.4
Corresponds to variant rs659243 [ dbSNP | Ensembl ].
VAR_041571
Natural variant19911E → D in a renal clear cell carcinoma sample; somatic mutation. Ref.90
VAR_041572
Natural variant20161D → G in AT. Ref.82
VAR_010838
Natural variant20341R → Q.
Corresponds to variant rs3218670 [ dbSNP | Ensembl ].
VAR_056688
Natural variant20631G → E in AT.
VAR_010839
Natural variant20671A → D in AT. Ref.82
VAR_010840
Natural variant20791V → I. Ref.2
Corresponds to variant rs1800060 [ dbSNP | Ensembl ].
VAR_010841
Natural variant21391E → G in T-prolymphocytic leukemia; somatic mutation. Ref.76
VAR_010842
Natural variant21641E → K in T-prolymphocytic leukemia. Ref.64
VAR_010843
Natural variant22181S → C in AT. Ref.87
VAR_010844
Natural variant2224 – 22274MALR → IS in AT.
VAR_010845
Natural variant22271R → C in AT. Ref.82
VAR_010846
Natural variant2246 – 22527CIKDILT → H in AT.
VAR_010847
Natural variant22741A → T in B-cell chronic lymphocytic leukemia. Ref.84
VAR_010848
Natural variant22871G → A. Ref.2
Corresponds to variant rs1800061 [ dbSNP | Ensembl ].
VAR_010849
Natural variant23071L → F. Ref.90
VAR_041573
Natural variant23321L → P. Ref.90
Corresponds to variant rs4988111 [ dbSNP | Ensembl ].
VAR_041574
Natural variant23351T → K.
Corresponds to variant rs3092831 [ dbSNP | Ensembl ].
VAR_056689
Natural variant23561I → F in a renal clear cell carcinoma sample; somatic mutation. Ref.90
VAR_041575
Natural variant23961T → S in T-prolymphocytic leukemia. Ref.64
VAR_010850
Natural variant24081S → L in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041576
Natural variant24181K → KK in mantle cell lymphoma. Ref.78 Ref.89
VAR_010851
Natural variant24201A → P in B-cell chronic lymphocytic leukemia. Ref.78
VAR_010852
Natural variant24231E → G in mantle cell lymphoma. Ref.78 Ref.89
VAR_010853
Natural variant24241V → G in AT, B-cell chronic lymphocytic leukemia and T-prolymphocytic leukemia; associated with increased risk for breast cancer. Ref.58 Ref.64 Ref.67 Ref.79
VAR_010854
Natural variant2427 – 24282Missing in AT; associated with T-prolymphocytic leukemia.
VAR_010855
Natural variant24381T → I. Ref.59 Ref.87
Corresponds to variant rs147604227 [ dbSNP | Ensembl ].
VAR_010856
Natural variant24421Q → P in T-prolymphocytic leukemia; also in a lung adenocarcinoma sample; somatic mutation. Ref.64 Ref.90
VAR_010857
Natural variant24431R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.90
VAR_041577
Natural variant24641C → R. Ref.90
VAR_041578
Natural variant24701Y → D in AT. Ref.82
VAR_010858
Natural variant24861R → G in T-prolymphocytic leukemia. Ref.70
VAR_010859
Natural variant24911W → R in AT. Ref.75
VAR_010860
Natural variant24921L → R. Ref.90
VAR_041579
Natural variant2546 – 25483Missing in AT, T-prolymphocytic leukemia and T-cell acute lymphoblastic leukemia.
VAR_010861
Natural variant25541H → D in AT. Ref.67
VAR_010862
Natural variant25701E → G.
Corresponds to variant rs28904920 [ dbSNP | Ensembl ].
VAR_056690
Natural variant2625 – 26262DA → EP in AT.
VAR_010864
Natural variant26251D → Q in AT; requires 2 nucleotide substitutions. Ref.87
VAR_010863
Natural variant26401T → I.
Corresponds to variant rs4988125 [ dbSNP | Ensembl ].
VAR_056691
Natural variant26561L → P in AT; partial functional loss. Ref.69
VAR_010865
Natural variant26621Missing in AT. Ref.82
VAR_010866
Natural variant26631Missing in AT.
VAR_010867
Natural variant26661T → A in a lung adenocarcinoma sample; somatic mutation. Ref.90
VAR_041580
Natural variant26681E → G in AT. Ref.67
VAR_010868
Natural variant26951G → A in T-prolymphocytic leukemia and B-cell chronic lymphocytic leukemia. Ref.64 Ref.84
VAR_010869
Natural variant27021I → R in AT.
VAR_010870
Natural variant27091G → S.
Corresponds to variant rs3218680 [ dbSNP | Ensembl ].
VAR_056692
Natural variant27191R → H. Ref.90
VAR_041581
Natural variant27221L → R in T-prolymphocytic leukemia. Ref.64
VAR_010871
Natural variant27251D → G in T-prolymphocytic leukemia. Ref.65
VAR_010872
Natural variant27251D → V in T-prolymphocytic leukemia. Ref.64
VAR_010873
Natural variant27261A → V in AT.
VAR_010874
Natural variant27321F → L in T-prolymphocytic leukemia. Ref.64
VAR_010875
Natural variant27651G → S May contribute to breast cancer. Ref.81
VAR_010876
Natural variant28101Missing in T-prolymphocytic leukemia. Ref.64
VAR_010877
Natural variant28241C → Y in AT. Ref.14
VAR_010878
Natural variant28271F → C in AT; mild. Ref.58 Ref.67
VAR_010879
Natural variant28291P → L in AT. Ref.73
VAR_010880
Natural variant28321R → C in AT and B-cell non-Hodgkin lymphoma. Ref.64 Ref.66 Ref.87
VAR_010881
Natural variant28421P → R in a lung adenocarcinoma sample; somatic mutation. Ref.90
VAR_041582
Natural variant28491R → P in AT. Ref.82
VAR_010882
Natural variant2855 – 28562SV → RI in AT.
VAR_010884
Natural variant28551S → R in AT.
VAR_010883
Natural variant28601Missing in AT. Ref.9 Ref.63
VAR_010885
Natural variant28671G → R in AT. Ref.62 Ref.82
VAR_010886
Natural variant28701D → N. Ref.90
VAR_041583
Natural variant2871 – 28722RH → S in T-prolymphocytic leukemia.
VAR_010887
Natural variant28901L → V in T-prolymphocytic leukemia. Ref.64 Ref.76
VAR_010888
Natural variant29041E → G in AT. Ref.63
VAR_010889
Natural variant29091R → G in AT. Ref.75
VAR_010890
Natural variant30061A → P in T-prolymphocytic leukemia. Ref.65
VAR_010892
Natural variant30081R → C in AT, T-prolymphocytic leukemia and mantle cell lymphoma. Ref.65 Ref.71 Ref.76 Ref.87 Ref.89
VAR_010893
Natural variant30081R → H in B-cell chronic lymphocytic leukemia. Ref.78
VAR_010894
Natural variant30181K → N in B-cell chronic lymphocytic leukemia. Ref.78
VAR_010895

Experimental info

Mutagenesis3671S → 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. Ref.42
Mutagenesis18931S → 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. Ref.42
Mutagenesis19811S → 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. Ref.34 Ref.42
Mutagenesis19811S → D or E: Disrupts the dimer. Ref.34 Ref.42
Mutagenesis28701D → A: Loss of kinase activity. Ref.21
Mutagenesis28751N → K: Loss of kinase activity. Ref.21
Mutagenesis30161K → 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. Ref.44
Mutagenesis30181K → R: Retains DNA damage-inducible acetylation and S-1981 autophosphorylation. Ref.44
Sequence conflict461H → N in CAA62603. Ref.7
Sequence conflict561N → I in CAA62603. Ref.7
Sequence conflict3131Y → N in CAA62603. Ref.7
Sequence conflict4881W → G in CAA62603. Ref.7
Sequence conflict5541T → A in AAC50289. Ref.1
Sequence conflict7501K → N in AAC50289. Ref.1
Sequence conflict7541Q → K in CAA62603. Ref.7
Sequence conflict8871E → G in CAA62603. Ref.7
Sequence conflict10031Q → L in CAA62603. Ref.7
Sequence conflict10491L → W in CAA62603. Ref.7
Sequence conflict10891A → V in CAA62603. Ref.7
Sequence conflict30031N → D in AAC50289. Ref.1
Sequence conflict30031N → D in AAB38309. Ref.2
Sequence conflict30031N → D in AAB38310. Ref.2
Sequence conflict30031N → D in AAA86520. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q13315 [UniParc].

Last modified January 22, 2014. Version 4.
Checksum: C0B4866E1E3199E2

FASTA3,056350,687
        10         20         30         40         50         60 
MSLVLNDLLI CCRQLEHDRA TERKKEVEKF KRLIRDPETI KHLDRHSDSK QGKYLNWDAV 

        70         80         90        100        110        120 
FRFLQKYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL VKYFIKCANR RAPRLKCQEL 

       130        140        150        160        170        180 
LNYIMDTVKD SSNGAIYGAD CSNILLKDIL SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ 

       190        200        210        220        230        240 
DVHRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQCA RQEKSSSGLN HILAALTIFL 

       250        260        270        280        290        300 
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK 

       310        320        330        340        350        360 
GAYESTKWRS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA DICHQVFNED 

       370        380        390        400        410        420 
TRSLEISQSY TTTQRESSDY SVPCKRKKIE LGWEVIKDHL QKSQNDFDLV PWLQIATQLI 

       430        440        450        460        470        480 
SKYPASLPNC ELSPLLMILS QLLPQQRHGE RTPYVLRCLT EVALCQDKRS NLESSQKSDL 

       490        500        510        520        530        540 
LKLWNKIWCI TFRGISSEQI QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACRPSCPAVC 

       550        560        570        580        590        600 
CLTLALTTSI VPGTVKMGIE QNMCEVNRSF SLKESIMKWL LFYQLEGDLE NSTEVPPILH 

       610        620        630        640        650        660 
SNFPHLVLEK ILVSLTMKNC KAAMNFFQSV PECEHHQKDK EELSFSEVEE LFLQTTFDKM 

       670        680        690        700        710        720 
DFLTIVRECG IEKHQSSIGF SVHQNLKESL DRCLLGLSEQ LLNNYSSEIT NSETLVRCSR 

       730        740        750        760        770        780 
LLVGVLGCYC YMGVIAEEEA YKSELFQKAK SLMQCAGESI TLFKNKTNEE FRIGSLRNMM 

       790        800        810        820        830        840 
QLCTRCLSNC TKKSPNKIAS GFFLRLLTSK LMNDIADICK SLASFIKKPF DRGEVESMED 

       850        860        870        880        890        900 
DTNGNLMEVE DQSSMNLFND YPDSSVSDAN EPGESQSTIG AINPLAEEYL SKQDLLFLDM 

       910        920        930        940        950        960 
LKFLCLCVTT AQTNTVSFRA ADIRRKLLML IDSSTLEPTK SLHLHMYLML LKELPGEEYP 

       970        980        990       1000       1010       1020 
LPMEDVLELL KPLSNVCSLY RRDQDVCKTI LNHVLHVVKN LGQSNMDSEN TRDAQGQFLT 

      1030       1040       1050       1060       1070       1080 
VIGAFWHLTK ERKYIFSVRM ALVNCLKTLL EADPYSKWAI LNVMGKDFPV NEVFTQFLAD 

      1090       1100       1110       1120       1130       1140 
NHHQVRMLAA ESINRLFQDT KGDSSRLLKA LPLKLQQTAF ENAYLKAQEG MREMSHSAEN 

      1150       1160       1170       1180       1190       1200 
PETLDEIYNR KSVLLTLIAV VLSCSPICEK QALFALCKSV KENGLEPHLV KKVLEKVSET 

      1210       1220       1230       1240       1250       1260 
FGYRRLEDFM ASHLDYLVLE WLNLQDTEYN LSSFPFILLN YTNIEDFYRS CYKVLIPHLV 

      1270       1280       1290       1300       1310       1320 
IRSHFDEVKS IANQIQEDWK SLLTDCFPKI LVNILPYFAY EGTRDSGMAQ QRETATKVYD 

      1330       1340       1350       1360       1370       1380 
MLKSENLLGK QIDHLFISNL PEIVVELLMT LHEPANSSAS QSTDLCDFSG DLDPAPNPPH 

      1390       1400       1410       1420       1430       1440 
FPSHVIKATF AYISNCHKTK LKSILEILSK SPDSYQKILL AICEQAAETN NVYKKHRILK 

      1450       1460       1470       1480       1490       1500 
IYHLFVSLLL KDIKSGLGGA WAFVLRDVIY TLIHYINQRP SCIMDVSLRS FSLCCDLLSQ 

      1510       1520       1530       1540       1550       1560 
VCQTAVTYCK DALENHLHVI VGTLIPLVYE QVEVQKQVLD LLKYLVIDNK DNENLYITIK 

      1570       1580       1590       1600       1610       1620 
LLDPFPDHVV FKDLRITQQK IKYSRGPFSL LEEINHFLSV SVYDALPLTR LEGLKDLRRQ 

      1630       1640       1650       1660       1670       1680 
LELHKDQMVD IMRASQDNPQ DGIMVKLVVN LLQLSKMAIN HTGEKEVLEA VGSCLGEVGP 

      1690       1700       1710       1720       1730       1740 
IDFSTIAIQH SKDASYTKAL KLFEDKELQW TFIMLTYLNN TLVEDCVKVR SAAVTCLKNI 

      1750       1760       1770       1780       1790       1800 
LATKTGHSFW EIYKMTTDPM LAYLQPFRTS RKKFLEVPRF DKENPFEGLD DINLWIPLSE 

      1810       1820       1830       1840       1850       1860 
NHDIWIKTLT CAFLDSGGTK CEILQLLKPM CEVKTDFCQT VLPYLIHDIL LQDTNESWRN 

      1870       1880       1890       1900       1910       1920 
LLSTHVQGFF TSCLRHFSQT SRSTTPANLD SESEHFFRCC LDKKSQRTML AVVDYMRRQK 

      1930       1940       1950       1960       1970       1980 
RPSSGTIFND AFWLDLNYLE VAKVAQSCAA HFTALLYAEI YADKKSMDDQ EKRSLAFEEG 

      1990       2000       2010       2020       2030       2040 
SQSTTISSLS EKSKEETGIS LQDLLLEIYR SIGEPDSLYG CGGGKMLQPI TRLRTYEHEA 

      2050       2060       2070       2080       2090       2100 
MWGKALVTYD LETAIPSSTR QAGIIQALQN LGLCHILSVY LKGLDYENKD WCPELEELHY 

      2110       2120       2130       2140       2150       2160 
QAAWRNMQWD HCTSVSKEVE GTSYHESLYN ALQSLRDREF STFYESLKYA RVKEVEEMCK 

      2170       2180       2190       2200       2210       2220 
RSLESVYSLY PTLSRLQAIG ELESIGELFS RSVTHRQLSE VYIKWQKHSQ LLKDSDFSFQ 

      2230       2240       2250       2260       2270       2280 
EPIMALRTVI LEILMEKEMD NSQRECIKDI LTKHLVELSI LARTFKNTQL PERAIFQIKQ 

      2290       2300       2310       2320       2330       2340 
YNSVSCGVSE WQLEEAQVFW AKKEQSLALS ILKQMIKKLD ASCAANNPSL KLTYTECLRV 

      2350       2360       2370       2380       2390       2400 
CGNWLAETCL ENPAVIMQTY LEKAVEVAGN YDGESSDELR NGKMKAFLSL ARFSDTQYQR 

      2410       2420       2430       2440       2450       2460 
IENYMKSSEF ENKQALLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEL ALRALKEDRK 

      2470       2480       2490       2500       2510       2520 
RFLCKAVENY INCLLSGEEH DMWVFRLCSL WLENSGVSEV NGMMKRDGMK IPTYKFLPLM 

      2530       2540       2550       2560       2570       2580 
YQLAARMGTK MMGGLGFHEV LNNLISRISM DHPHHTLFII LALANANRDE FLTKPEVARR 

      2590       2600       2610       2620       2630       2640 
SRITKNVPKQ SSQLDEDRTE AANRIICTIR SRRPQMVRSV EALCDAYIIL ANLDATQWKT 

      2650       2660       2670       2680       2690       2700 
QRKGINIPAD QPITKLKNLE DVVVPTMEIK VDHTGEYGNL VTIQSFKAEF RLAGGVNLPK 

      2710       2720       2730       2740       2750       2760 
IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL TICTYKVVPL 

      2770       2780       2790       2800       2810       2820 
SQRSGVLEWC TGTVPIGEFL VNNEDGAHKR YRPNDFSAFQ CQKKMMEVQK KSFEEKYEVF 

      2830       2840       2850       2860       2870       2880 
MDVCQNFQPV FRYFCMEKFL DPAIWFEKRL AYTRSVATSS IVGYILGLGD RHVQNILINE 

      2890       2900       2910       2920       2930       2940 
QSAELVHIDL GVAFEQGKIL PTPETVPFRL TRDIVDGMGI TGVEGVFRRC CEKTMEVMRN 

      2950       2960       2970       2980       2990       3000 
SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDETEL HPTLNADDQE CKRNLSDIDQ 

      3010       3020       3030       3040       3050 
SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAI DPKNLSRLFP GWKAWV 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of the coding region of the ATM gene reveals similarity to cell cycle regulators in different species."
Savitsky K., Sfez S., Tagle D.A., Ziv Y., Sartiel A., Collins F.S., Shiloh Y., Rotman G.
Hum. Mol. Genet. 4:2025-2032(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The ATM gene and susceptibility to breast cancer: analysis of 38 breast tumors reveals no evidence for mutation."
Vorechovsky I., Rasio D., Luo L., Monaco C., Hammarstroem L., Webster A.D.B., Zaloudik J., Barbanti-Brodano G., James M.R., Russo G., Croce C.M., Negrini M.
Cancer Res. 56:2726-2732(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS CYS-49; ARG-1054; PHE-1420; ILE-2079 AND ALA-2287.
[3]"Ataxia-telangiectasia locus: sequence analysis of 184 kb of human genomic DNA containing the entire ATM gene."
Platzer M., Rotman G., Bauer D., Uziel T., Savitsky K., Bar-Shira A., Gilad S., Shiloh Y., Rosenthal A.
Genome Res. 7:592-605(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-1983.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2756.
[7]"Mutations revealed by sequencing the 5' half of the gene for ataxia telangiectasia."
Byrd P.J., McConville C.M., Cooper P., Parkhill J., Stankovic T., McGuire G.M., Thick J.A., Taylor A.M.R.
Hum. Mol. Genet. 5:145-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1369, VARIANT AT 2546-SER--ILE-2548 DEL.
[8]"Ataxia-telangiectasia: structural diversity of untranslated sequences suggests complex post-transcriptional regulation of ATM gene expression."
Savitsky K., Platzer M., Uziel T., Gilad S., Sartiel A., Rosenthal A., Elroy-Stein O., Shiloh Y., Rotman G.
Nucleic Acids Res. 25:1678-1684(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[9]"A single ataxia telangiectasia gene with a product similar to PI-3 kinase."
Savitsky K., Bar-Shira A., Gilad S., Rotman G., Ziv Y., Vanagaite L., Tagle D.A., Smith S., Uziel T., Sfez S., Ashkenazi M., Pecker I., Frydman M., Harnik R., Patanjali S.R., Simmons A., Clines G.A., Sartiel A. expand/collapse author list , Gatti R.A., Chessa L., Sanal O., Lavin M.F., Jaspers N.G.J., Taylor A.M.R., Arlett C.F., Miki T., Weissman S.M., Lovett M., Collins F.S., Shiloh Y.
Science 268:1749-1753(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1332-3056, VARIANTS AT 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL AND SER-2860 DEL.
Tissue: Fibroblast.
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-3056.
Tissue: Brain.
[11]"Genomic organization of the ATM locus involved in ataxia-telangiectasia."
Rasio D., Negrini M., Croce C.M.
Cancer Res. 55:6053-6057(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1349-3056.
[12]"The product of the ATM gene is a 370-kDa nuclear phosphoprotein."
Chen G., Lee E.Y.-H.P.
J. Biol. Chem. 271:33693-33697(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[13]"The ataxia-telangiectasia gene product, a constitutively expressed nuclear protein that is not up-regulated following genome damage."
Brown K.D., Ziv Y., Sadanandan S.N., Chessa L., Collins F.S., Shiloh Y., Tagle D.A.
Proc. Natl. Acad. Sci. U.S.A. 94:1840-1845(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Cellular localisation of the ataxia-telangiectasia (ATM) gene product and discrimination between mutated and normal forms."
Watters D., Khanna K.K., Beamish H., Birrell G., Spring K., Kedar P., Gatei M., Stenzel D., Hobson K., Kozlov S., Zhang N., Farrell A., Ramsay J., Gatti R.A., Lavin M.F.
Oncogene 14:1911-1921(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANTS AT 2546-SER--ILE-2548 DEL AND TYR-2824.
[15]"ATM gene product phosphorylates I kappa B-alpha."
Jung M., Kondratyev A., Lee S.A., Dimtchev A., Dritschilo A.
Cancer Res. 57:24-27(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[16]"Interaction between ATM protein and c-Abl in response to DNA damage."
Shafman T., Khanna K.K., Kedar P., Spring K., Kozlov S., Yen T., Hobson K., Gatei M., Zhang N., Watters D., Egerton M., Shiloh Y., Kharbanda S., Kufe D., Lavin M.F.
Nature 387:520-523(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABL1.
[17]"Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin."
Sarkaria J.N., Tibbetts R.S., Busby E.C., Kennedy A.P., Hill D.E., Abraham R.T.
Cancer Res. 58:4375-4382(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[18]"ATM associates with and phosphorylates p53: mapping the region of interaction."
Khanna K.K., Keating K.E., Kozlov S., Scott S., Gatei M., Hobson K., Taya Y., Gabrielli B., Chan D., Lees-Miller S.P., Lavin M.F.
Nat. Genet. 20:398-400(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53, CATALYTIC ACTIVITY.
[19]"ATM binds to beta-adaptin in cytoplasmic vesicles."
Lim D.-S., Kirsch D.G., Canman C.E., Ahn J.-H., Ziv Y., Newman L.S., Darnell R.B., Shiloh Y., Kastan M.B.
Proc. Natl. Acad. Sci. U.S.A. 95:10146-10151(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BETA-ADAPTIN.
[20]"Enhanced phosphorylation of p53 by ATM in response to DNA damage."
Banin S., Moyal L., Shieh S.-Y., Taya Y., Anderson C.W., Chessa L., Smorodinsky N.I., Prives C., Reiss Y., Shiloh Y., Ziv Y.
Science 281:1674-1677(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF TP53.
[21]"Activation of the ATM kinase by ionizing radiation and phosphorylation of p53."
Canman C.E., Lim D.-S., Cimprich K.A., Taya Y., Tamai K., Sakaguchi K., Appella E., Kastan M.B., Siliciano J.D.
Science 281:1677-1679(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF TP53, MUTAGENESIS OF ASP-2870 AND ASN-2875.
[22]"Purification and DNA binding properties of the ataxia-telangiectasia gene product ATM."
Smith G.C.M., Cary R.B., Lakin N.D., Hann B.C., Teo S.-H., Chen D.J., Jackson S.P.
Proc. Natl. Acad. Sci. U.S.A. 96:11134-11139(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[23]"Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage response to double-strand breaks."
Cortez D., Wang Y., Qin J., Elledge S.J.
Science 286:1162-1166(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF BRCA1.
[24]"BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.
Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF ATM AS MEMBER OF BASC.
[25]"ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway."
Lim D.-S., Kim S.-T., Xu B., Maser R.S., Lin J., Petrini J.H.J., Kastan M.B.
Nature 404:613-617(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF NBN.
[26]"ATM phosphorylation of Nijmegen breakage syndrome protein is required in a DNA damage response."
Wu X., Ranganathan V., Weisman D.S., Heine W.F., Ciccone D.N., O'Neill T.B., Crick K.E., Pierce K.A., Lane W.S., Rathbun G., Livingston D.M., Weaver D.T.
Nature 405:477-482(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF NBN.
[27]"Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response."
Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y., Lee E.Y.-H.P., Lee W.-H.
Nature 406:210-215(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF CTIP.
[28]"ATM-dependent phosphorylation of nibrin in response to radiation exposure."
Gatei M., Young D., Cerosaletti K.M., Desai-Mehta A., Spring K., Kozlov S., Lavin M.F., Gatti R.A., Concannon P., Khanna K.K.
Nat. Genet. 25:115-119(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF NBN.
[29]"Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro."
Matsuoka S., Rotman G., Ogawa A., Shiloh Y., Tamai K., Elledge S.J.
Proc. Natl. Acad. Sci. U.S.A. 97:10389-10394(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CHEK2.
[30]"Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks."
Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.
J. Biol. Chem. 276:29282-29291(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF TERF1.
[31]"ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses."
Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A., Chen S.M., Abraham R.T., Wang X.-F.
Nature 411:969-974(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD17.
[32]"Convergence of the Fanconi anemia and ataxia telangiectasia signaling pathways."
Taniguchi T., Garcia-Higuera I., Xu B., Andreassen P.R., Gregory R.C., Kim S.-T., Lane W.S., Kastan M.B., D'Andrea A.D.
Cell 109:459-472(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION OF FANCD2.
[33]"Identification of a novel protein kinase mediating Akt survival signaling to the ATM protein."
Suzuki A., Kusakai G., Kishimoto A., Lu J., Ogura T., Lavin M.F., Esumi H.
J. Biol. Chem. 278:48-53(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY NUAK1.
[34]"DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation."
Bakkenist C.J., Kastan M.B.
Nature 421:499-506(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT SER-1981, SUBUNIT, FUNCTION, MUTAGENESIS OF SER-1981.
[35]"Requirement of protein phosphatase 5 in DNA-damage-induced ATM activation."
Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M., Abraham R.T., Wang X.F.
Genes Dev. 18:249-254(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE RESPONSE, INTERACTION WITH PPP5C.
[36]"Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response."
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.
Mol. Cell. Biol. 24:9207-9220(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1C.
[37]"The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR."
Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H., Choi Y.H., Choi D., Lee K.S., Kim S.
Cell 120:209-221(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EEF1E1.
[38]"ATM-dependent phosphorylation of ATF2 is required for the DNA damage response."
Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., Ronai Z.
Mol. Cell 18:577-587(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[39]"Involvement of human MOF in ATM function."
Gupta A., Sharma G.G., Young C.S.H., Agarwal M., Smith E.R., Paull T.T., Lucchesi J.C., Khanna K.K., Ludwig T., Pandita T.K.
Mol. Cell. Biol. 25:5292-5305(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT8.
[40]"Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1."
Kaygun H., Marzluff W.F.
Nat. Struct. Mol. Biol. 12:794-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
[41]"A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM."
Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.
Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTATIP, AUTOPHOSPHORYLATION AT SER-1981, ACETYLATION.
[42]"Involvement of novel autophosphorylation sites in ATM activation."
Kozlov S.V., Graham M.E., Peng C., Chen P., Robinson P.J., Lavin M.F.
EMBO J. 25:3504-3514(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT SER-367; SER-1893 AND SER-1981, FUNCTION, MUTAGENESIS OF SER-367; SER-1893 AND SER-1981, IDENTIFICATION BY MASS SPECTROMETRY.
[43]"ATMIN defines an NBS1-independent pathway of ATM signalling."
Kanu N., Behrens A.
EMBO J. 26:2933-2941(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATMIN.
[44]"DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity."
Sun Y., Xu Y., Roy K., Price B.D.
Mol. Cell. Biol. 27:8502-8509(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-3016, FUNCTION, MUTAGENESIS OF LYS-3016 AND LYS-3018.
[45]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1981 AND SER-1983, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[46]"Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1."
Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.
Genes Dev. 22:587-600(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP164.
[47]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[48]"Single-stranded DNA-binding protein hSSB1 is critical for genomic stability."
Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K., Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J., Pandita R.K., Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T., Pandita T.K., White M.F., Khanna K.K.
Nature 453:677-681(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NABP2.
[49]"A role for DEAD box 1 at DNA double-strand breaks."
Li L., Monckton E.A., Godbout R.
Mol. Cell. Biol. 28:6413-6425(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX1.
[50]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[51]"ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the apoptotic response to DNA damage."
Taira N., Yamamoto H., Yamaguchi T., Miki Y., Yoshida K.
J. Biol. Chem. 285:4909-4919(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS DYRK2 KINASE.
[52]"A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability."
Hurov K.E., Cotta-Ramusino C., Elledge S.J.
Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTI1.
[53]"Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
Takai H., Xie Y., de Lange T., Pavletich N.P.
Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TELO2.
[54]"Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly."
Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N.
J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TELO2 AND TTI1.
[55]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]"Protein phosphatase 5 is necessary for ATR-mediated DNA repair."
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y., You H.J.
Biochem. Biophys. Res. Commun. 404:476-481(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1981.
[57]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[58]"Mutations associated with variant phenotypes in ataxia-telangiectasia."
McConville C.M., Stankovic T., Byrd P.J., McGuire G.M., Yao Q.-Y., Lennox G.G., Taylor A.M.R.
Am. J. Hum. Genet. 59:320-330(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT GLY-2424; 2546-SER--ILE-2548 DEL AND CYS-2827.
[59]"A high frequency of distinct ATM gene mutations in ataxia-telangiectasia."
Wright J., Teraoka S., Onengut S., Tolun A., Gatti R.A., Ochs H.D., Concannon P.
Am. J. Hum. Genet. 59:839-846(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT 2546-SER--ILE-2548 DEL, VARIANT ILE-2438.
[60]"ATM mutations in cancer families."
Vorechovsky I., Luo L., Lindblom A., Negrini M., Webster A.D.B., Croce C.M., Hammarstroem L.
Cancer Res. 56:4130-4133(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT 705-PHE--PRO-707 AND 2546-SER--ILE-2548 DEL, VARIANTS CYS-49; LEU-858; ARG-1054; PHE-1420 AND ARG-1691.
[61]"Exon-scanning mutation analysis of the ATM gene in patients with ataxia-telangiectasia."
Vorechovsky I., Luo L., Prudente S., Chessa L., Russo G., Kanariou M., James M.R., Negrini M., Webster A.D.B., Hammarstroem L.
Eur. J. Hum. Genet. 4:352-355(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT 705-PHE--PRO-707, VARIANTS LEU-858 AND ARG-1054.
[62]"New mutations in the ataxia telangiectasia gene."
Baumer A., Bernthaler U., Wolz W., Hoehn H., Schindler D.
Hum. Genet. 98:246-249(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT ARG-2867.
[63]"Predominance of null mutations in ataxia-telangiectasia."
Gilad S., Khosravi R., Shkedy D., Uziel T., Ziv Y., Savitsky K., Rotman G., Smith S., Chessa L., Jorgensen T.J., Harnik R., Frydman M., Sanal O., Portnoi S., Goldwicz Z., Jaspers N.G.J., Gatti R.A., Lenoir G. expand/collapse author list , Lavin M.F., Tatsumi K., Wegner R.-D., Shiloh Y., Bar-Shira A.
Hum. Mol. Genet. 5:433-439(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860 DEL AND GLY-2904.
[64]"Clustering of missense mutations in the ataxia-telangiectasia gene in a sporadic T-cell leukaemia."
Vorechovsky I., Luo L., Dyer M.J.S., Catovsky D., Amlot P.L., Yaxley J.C., Foroni L., Hammarstroem L., Webster A.D.B., Yuille M.A.R.
Nat. Genet. 17:96-99(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TPLL THR-1407; HIS-1682; HIS-1910; LYS-2164; SER-2396; GLY-2424; PRO-2442; 2546-SER--ILE-2548 DEL; ALA-2695; ARG-2722; VAL-2725; LEU-2732; LYS-2810 DEL; 2871-ARG-HIS-2872 DELINS SER AND VAL-2890, VARIANTS BNHL VAL-1040; SER-1463 AND CYS-2832.
[65]"Biallelic mutations in the ATM gene in T-prolymphocytic leukemia."
Stilgenbauer S., Schaffner C., Litterst A., Liebisch P., Gilad S., Bar-Shira A., James M.R., Lichter P., Doehner H.
Nat. Med. 3:1155-1159(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TPLL GLY-2725; PRO-3006 AND CYS-3008.
[66]"Ataxia-telangiectasia: identification and detection of founder-effect mutations in the ATM gene in ethnic populations."
Telatar M., Teraoka S., Wang Z., Chun H.H., Liang T., Castellvi-Bel S., Udar N., Boerresen-Dale A.-L., Chessa L., Bernatowska-Matuszkiewicz E., Porras O., Watanabe M., Junker A., Concannon P., Gatti R.A.
Am. J. Hum. Genet. 62:86-97(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT CYS-2832.
[67]"ATM mutations and phenotypes in ataxia-telangiectasia families in the British Isles: expression of mutant ATM and the risk of leukemia, lymphoma, and breast cancer."
Stankovic T., Kidd A.M.J., Sutcliffe A., McGuire G.M., Robinson P., Weber P., Bedenham T., Bradwell A.R., Easton D.F., Lennox G.G., Haites N., Byrd P.J., Taylor A.M.R.
Am. J. Hum. Genet. 62:334-345(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT LEU-292; ASP-768; GLN-1001; ARG-1691; ILE-1743; GLY-2424; 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; ASP-2554; GLY-2668 AND CYS-2827.
[68]"Genotype-phenotype relationships in ataxia-telangiectasia and variants."
Gilad S., Chessa L., Khosravi R., Russell P., Galanty Y., Piane M., Gatti R.A., Jorgensen T.J., Shiloh Y., Bar-Shira A.
Am. J. Hum. Genet. 62:551-561(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT 1812-ALA-PHE-1813 DELINS VAL.
[69]"Ataxia-telangiectasia without immunodeficiency: novel point mutations within and adjacent to the phosphatidylinositol 3-kinase-like domain."
Toyoshima M., Hara T., Zhang H., Yamamoto T., Akaboshi S., Nanba E., Ohno K., Hori N., Sato K., Takeshita K.
Am. J. Med. Genet. 75:141-144(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT PRO-2656.
[70]"Inactivation of the ATM gene in T-cell prolymphocytic leukemias."
Stoppa-Lyonnet D., Soulier J., Lauge A., Dastot H., Garand R., Sigaux F., Stern M.-H.
Blood 91:3920-3926(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TPLL GLY-2486.
[71]"Strategies for mutational analysis of the large multiexon ATM gene using high-density oligonucleotide arrays."
Hacia J.G., Sun B., Hunt N., Edgemon K., Mosbrook D., Robbins C., Fodor S.P.A., Tagle D.A., Collins F.S.
Genome Res. 8:1245-1258(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT 2855-ARG-ILE-2856 AND CYS-3008, VARIANT VAL-1853.
[72]"A double missense mutation in the ATM gene of a Dutch family with ataxia telangiectasia."
van Belzen M.J., Hiel J.A.P., Weemaes C.M.R., Gabreeels F.J.M., van Engelen B.G.M., Smeets D.F.C.M., van den Heuvel L.P.W.J.
Hum. Genet. 102:187-191(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT 2625-GLU-PRO-2626.
[73]"ATM mutations in patients with ataxia telangiectasia screened by a hierarchical strategy."
Sasaki T., Tian H., Kukita Y., Inazuka M., Tahira T., Imai T., Yamauchi M., Saito T., Hori T., Hashimoto-Tamaoki T., Komatsu K., Nikaido O., Hayashi K.
Hum. Mutat. 12:186-195(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT LEU-2829, VARIANTS GLU-126; ASP-514 AND ASN-1853.
[74]"ATM germline mutations in classical ataxia-telangiectasia patients in the Dutch population."
Broeks A., de Klein A., Floore A.N., Muijtjens M., Kleijer W.J., Jaspers N.G.J., van 't Veer L.J.
Hum. Mutat. 12:330-337(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT ASP-1091 AND ARG-1566, VARIANTS LEU-858 AND ARG-1054.
[75]"Ataxia-telangiectasia in the Japanese population: identification of R1917X, W2491R, R2909G, IVS33+2T-->A, and 7883del5, the latter two being relatively common mutations."
Fukao T., Song X.-Q., Yoshida T., Tashita H., Kaneko H., Teramoto T., Inoue R., Katamura K., Mayumi M., Hiratani M., Taniguchi N., Arai J., Wakiguchi H., Bar-Shira A., Shiloh Y., Kondo N.
Hum. Mutat. 12:338-343(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT ARG-2491 AND GLY-2909.
[76]"ATM is usually rearranged in T-cell prolymphocytic leukaemia."
Yuille M.A.R., Coignet L.J.A., Abraham S.M., Yaqub F., Luo L., Matutes E., Brito-Babapulle V., Vorechovsky I., Dyer M.J.S., Catovsky D.
Oncogene 16:789-796(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TPLL GLY-2139; VAL-2890 AND CYS-3008.
[77]Erratum
Yuille M.A.R., Coignet L.J.A., Abraham S.M., Yaqub F., Luo L., Matutes E., Brito-Babapulle V., Vorechovsky I., Dyer M.J.S., Catovsky D.
Oncogene 16:2955-2955(1998)
[78]"Somatic ATM mutations indicate a pathogenic role of ATM in B-cell chronic lymphocytic leukemia."
Schaffner C., Stilgenbauer S., Rappold G.A., Doehner H., Lichter P.
Blood 94:748-753(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BCLL VAL-1853; ARG-1953; PRO-2420; HIS-3008 AND ASN-3018, VARIANTS MCL LYS-2418 INS AND GLY-2423, VARIANT ASN-1853.
[79]"ATM mutations in B-cell chronic lymphocytic leukemia."
Bullrich F., Rasio D., Kitada S., Starostik P., Kipps T., Keating M., Albitar M., Reed J.C., Croce C.M.
Cancer Res. 59:24-27(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BCLL CYS-332; ARG-1691 AND GLY-2424.
[80]"Rapid and efficient ATM mutation detection by fluorescent chemical cleavage of mismatch: identification of four novel mutations."
Izatt L., Vessey C., Hodgson S.V., Solomon E.
Eur. J. Hum. Genet. 7:310-320(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AT PRO-1465.
[81]"Identification of germline missense mutations and rare allelic variants in the ATM gene in early-onset breast cancer."
Izatt L., Greenman J., Hodgson S.V., Ellis D., Watts S., Scott G., Jacobs C., Liebmann R., Zvelebil M.J., Mathew C., Solomon E.
Genes Chromosomes Cancer 26:286-294(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-49; LEU-182; PRO-707; LEU-858; PHE-1420; ALA-1570; ASN-1853 AND SER-2765.
[82]"Characterization of ATM gene mutations in 66 ataxia telangiectasia families."
Sandoval N., Platzer M., Rosenthal A., Doerk T., Bendix R., Skawran B., Stuhrmann M., Wegner R.-D., Sperling K., Banin S., Shiloh Y., Baumer A., Bernthaler U., Sennefelder H., Brohm M., Weber B.H.F., Schindler D.
Hum. Mol. Genet. 8:69-79(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT SER-570; CYS-785; GLY-1913; GLY-2016; ASP-2067; CYS-2227; ASP-2470; VAL-2662 DEL; PRO-2849 AND ARG-2867, VARIANTS CYS-49; LEU-858; ARG-1054; ASN-1853 AND VAL-1853.
[83]"New mutations, polymorphisms, and rare variants in the ATM gene detected by a novel SSCP strategy."
Castellvi-Bel S., Sheikhavandi S., Telatar M., Tai L.-Q., Hwang M.J., Wang Z., Yang Z., Cheng R., Gatti R.A.
Hum. Mutat. 14:156-162(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT, VARIANTS ASN-1454 AND ASN-1853.
[84]"Inactivation of ataxia telangiectasia mutated gene in B-cell chronic lymphocytic leukaemia."
Stankovic T., Weber P., Stewart G., Bedenham T., Murray J., Byrd P.J., Moss P.A.H., Taylor A.M.R.
Lancet 353:26-29(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BCLL THR-350; THR-352; ARG-1054; THR-2274 AND ALA-2695.
[85]"Missense mutations at ATM gene and cancer risk."
Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.
Lancet 353:1276-1276(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-1054.
[86]Erratum
Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.
Lancet 354:780-780(1999)
[87]"Mutations at the ataxia-telangiectasia locus and clinical phenotypes of A-T patients."
Li A., Swift M.
Am. J. Med. Genet. 92:170-177(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT GLU-224; VAL-323; PRO-1420; CYS-2218; 2546-SER--ILE-2548 DEL; GLN-2625; CYS-2832; 2855-ARG-ILE-2856 AND CYS-3008, VARIANTS VAL-1853 AND ILE-2438.
[88]"Ataxia-telangiectasia: phenotype/genotype studies of ATM protein expression, mutations, and radiosensitivity."
Becker-Catania S.G., Chen G., Hwang M.J., Wang Z., Sun X., Sanal O., Bernatowska-Matuszkiewicz E., Chessa L., Lee E.Y.-H.P., Gatti R.A.
Mol. Genet. Metab. 70:122-133(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AT.
[89]"Mantle cell lymphoma is characterized by inactivation of the ATM gene."
Schaffner C., Idler I., Stilgenbauer S., Doehner H., Lichter P.
Proc. Natl. Acad. Sci. U.S.A. 97:2773-2778(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MCL LYS-2418 INS; GLY-2423 AND CYS-3008.
[90]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-23; CYS-49; GLU-126; HIS-140; GLN-250; PHE-333; CYS-337; HIS-337; ALA-410; SER-504; ASP-514; TYR-540; VAL-546; LEU-582; PRO-707; GLN-848; LEU-858; SER-872; TRP-924; ALA-935; ARG-1054; PHE-1179; ILE-1321; TYR-1380; SER-1382; PHE-1420; MET-1469; CYS-1475; SER-1650; THR-1739; ASN-1853; VAL-1853; ILE-1916; THR-1945; CYS-1961; ASP-1991; PHE-2307; PRO-2332; PHE-2356; LEU-2408; PRO-2442; GLN-2443; ARG-2464; ARG-2492; ALA-2666; HIS-2719; ARG-2842 AND ASN-2870.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33841 mRNA. Translation: AAC50289.1.
U55757 expand/collapse EMBL AC list , U55704, U55705, U55707, U55708, U55709, U55710, U55711, U55712, U55713, U55714, U55715, U55716, U55717, U55718, U55719, U55720, U55721, U55722, U55723, U55724, U55725, U55726, U55727, U55728, U55729, U55730, U55731, U55732, U55733, U55734, U55735, U55736, U55737, U55738, U55739, U55740, U55741, U55742, U55743, U55744, U55745, U55746, U55747, U55748, U55749, U55750, U55751, U55752, U55753, U55754, U55755, U55756 Genomic DNA. Translation: AAB38309.1.
U55757 expand/collapse EMBL AC list , U55726, U55727, U55728, U55729, U55730, U55731, U55732, U55733, U55734, U55735, U55736, U55737, U55738, U55739, U55740, U55741, U55742, U55743, U55744, U55745, U55746, U55747, U55748, U55749, U55750, U55751, U55752, U55753, U55754, U55755, U55756 Genomic DNA. Translation: AAB38310.1.
U82828 Genomic DNA. Translation: AAB65827.1.
AP001925 Genomic DNA. No translation available.
AP005718 Genomic DNA. No translation available.
KF455499 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67111.1. Sequence problems.
X91196 mRNA. Translation: CAA62603.1.
U67092 Genomic DNA. Translation: AAC51298.1.
AY220758 Genomic DNA. Translation: AAO26044.1.
U26455 mRNA. Translation: AAA86520.1. Sequence problems.
BC137169 mRNA. Translation: AAI37170.1. Sequence problems.
CCDSCCDS31669.1.
PIRA43100.
RefSeqNP_000042.3. NM_000051.3.
XP_005271618.2. XM_005271561.2.
XP_005271619.2. XM_005271562.2.
XP_006718906.1. XM_006718843.1.
XP_006718908.1. XM_006718845.1.
UniGeneHs.367437.

3D structure databases

ProteinModelPortalQ13315.
SMRQ13315. Positions 3025-3055.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106962. 117 interactions.
DIPDIP-182N.
IntActQ13315. 33 interactions.
MINTMINT-194471.
STRING9606.ENSP00000278616.

Chemistry

BindingDBQ13315.
ChEMBLCHEMBL3797.

PTM databases

PhosphoSiteQ13315.

Polymorphism databases

DMDM317373479.

Proteomic databases

PaxDbQ13315.
PRIDEQ13315.

Protocols and materials databases

DNASU472.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278616; ENSP00000278616; ENSG00000149311.
ENST00000452508; ENSP00000388058; ENSG00000149311.
GeneID472.
KEGGhsa:472.
UCSCuc001pkb.1. human.

Organism-specific databases

CTD472.
GeneCardsGC11P108093.
GeneReviewsATM.
H-InvDBHIX0010089.
HIX0201637.
HGNCHGNC:795. ATM.
HPACAB000102.
MIM208900. phenotype.
607585. gene.
neXtProtNX_Q13315.
Orphanet100. Ataxia-telangiectasia.
370109. Ataxia-telangiectasia variant.
67038. B-cell chronic lymphocytic leukemia.
370114. Combined cervical dystonia.
52416. Mantle cell lymphoma.
PharmGKBPA61.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOVERGENHBG004304.
InParanoidQ13315.
KOK04728.
PhylomeDBQ13315.
TreeFamTF101182.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_216. DNA Repair.
SignaLinkQ13315.

Gene expression databases

ArrayExpressQ13315.
BgeeQ13315.
CleanExHS_ATM.
GenevestigatorQ13315.

Family and domain databases

Gene3D1.10.1070.11. 3 hits.
InterProIPR016024. ARM-type_fold.
IPR015519. ATM.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR021668. TAN.
[Graphical view]
PANTHERPTHR11139:SF66. PTHR11139:SF66. 1 hit.
PfamPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATM. human.
GeneWikiAtaxia_telangiectasia_mutated.
GenomeRNAi472.
NextBio1949.
PROQ13315.
SOURCESearch...

Entry information

Entry nameATM_HUMAN
AccessionPrimary (citable) accession number: Q13315
Secondary accession number(s): B2RNX5 expand/collapse secondary AC list , O15429, Q12758, Q16551, Q93007, Q9NP02, Q9UCX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 22, 2014
Last modified: July 9, 2014
This is version 180 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM