Q13315 (ATM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3056 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.29 Ref.34 Ref.38 Ref.40 Ref.42 Ref.49
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.44 Ref.46 Ref.47 Ref.50 Ref.51 Ref.52
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.39 Ref.40 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.
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.39 Ref.40 Ref.41 Ref.42 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.62 Ref.63 Ref.64 Ref.65 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.76 Ref.78 Ref.79 Ref.83 Ref.84 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.60 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.74 Ref.75 Ref.80
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 process	Cell cycle DNA damage DNA repair
Cellular component	Cytoplasmic vesicle Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Neurodegeneration Tumor suppressor
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 G2 DNA damage checkpoint Inferred from mutant phenotype PubMed 15149599. Source: BHF-UCL brain development Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from mutant phenotype PubMed 15149599. Source: BHF-UCL cellular response to gamma radiation Inferred from direct assay PubMed 9925639. Source: BHF-UCL double-strand break repair via homologous recombination Traceable author statement. Source: Reactome female gamete generation Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara histone mRNA catabolic process Inferred from direct assay Ref.38. Source: UniProtKB intrinsic apoptotic signaling pathway in response to DNA damage Inferred from electronic annotation. Source: Compara lipoprotein catabolic process Inferred from electronic annotation. Source: Compara 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 negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara neuron apoptotic process Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from direct assay Ref.21. Source: BHF-UCL 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: Compara 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 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: Compara somitogenesis Inferred from electronic annotation. Source: Compara telomere maintenance Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome spindle Inferred from electronic annotation. Source: Compara
Molecular_function	1-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: Compara protein N-terminus binding Inferred from direct assay Ref.30. 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AATF	Q9NY61	3	EBI-495465,EBI-372428
MDC1	Q14676	2	EBI-495465,EBI-495644
NABP2	Q9BQ15	4	EBI-495465,EBI-2120336
TELO2	Q9Y4R8	4	EBI-495465,EBI-1043674
TERF1	P54274	2	EBI-495465,EBI-710997
TERF1	P54274-2	5	EBI-495465,EBI-711018
TTI1	O43156	5	EBI-495465,EBI-1055680

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3056	3056	Serine-protein kinase ATM		PRO_0000088840
Regions
	Domain	1960 – 2566	607	FAT
	Domain	2712 – 2962	251	PI3K/PI4K
	Domain	3024 – 3056	33	FATC
	Region	1373 – 1382	10	Interaction with ABL1
Amino acid modifications
	Modified residue	367	1	Phosphoserine; by autocatalysis Ref.40
	Modified residue	1893	1	Phosphoserine; by autocatalysis Ref.40
	Modified residue	1981	1	Phosphoserine; by autocatalysis Ref.34 Ref.39 Ref.40 Ref.43
	Modified residue	1983	1	Phosphoserine; in variant Ser-1983 Ref.43
	Modified residue	2996	1	Phosphoserine Ref.45 Ref.48
	Modified residue	3016	1	N6-acetyllysine Ref.42
Natural variations
	Natural variant	23	1	R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041545
	Natural variant	45	1	R → W. Corresponds to variant rs3218684 [ dbSNP | Ensembl ].		VAR_056678
	Natural variant	49	1	S → C. Ref.2 Ref.56 Ref.77 Ref.78 Ref.86 Corresponds to variant rs1800054 [ dbSNP | Ensembl ].		VAR_010798
	Natural variant	126	1	D → E. Ref.69 Ref.86 Corresponds to variant rs2234997 [ dbSNP | Ensembl ].		VAR_010799
	Natural variant	140	1	D → H. Ref.86		VAR_041546
	Natural variant	182	1	V → L. Ref.77 Corresponds to variant rs3218707 [ dbSNP | Ensembl ].		VAR_010800
	Natural variant	224	1	K → E in AT. Ref.83		VAR_010801
	Natural variant	250	1	R → Q. Ref.86		VAR_041547
	Natural variant	292	1	P → L in AT; associated with lymphoma. Ref.63		VAR_010802
	Natural variant	323	1	I → V in AT. Ref.83		VAR_010803
	Natural variant	332	1	Y → C in B-cell chronic lymphocytic leukemia. Ref.75		VAR_010804
	Natural variant	333	1	S → F. Ref.86		VAR_041548
	Natural variant	337	1	R → C in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041549
	Natural variant	337	1	R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041550
	Natural variant	350	1	A → T in B-cell chronic lymphocytic leukemia. Ref.80		VAR_010805
	Natural variant	352	1	I → T in B-cell chronic lymphocytic leukemia. Ref.80		VAR_010806
	Natural variant	410	1	V → A. Ref.86		VAR_041551
	Natural variant	504	1	N → S. Ref.86		VAR_041552
	Natural variant	514	1	G → D. Ref.69 Ref.86 Corresponds to variant rs2235000 [ dbSNP | Ensembl ].		VAR_010807
	Natural variant	540	1	C → Y in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041553
	Natural variant	546	1	L → V. Ref.86 Corresponds to variant rs2227924 [ dbSNP | Ensembl ].		VAR_041554
	Natural variant	570	1	F → S in AT. Ref.78		VAR_010808
	Natural variant	582	1	F → L. Ref.86 Corresponds to variant rs2235006 [ dbSNP | Ensembl ].		VAR_041555
	Natural variant	705 – 707	3	YSS → FIP in AT; might be associated with susceptibility to cancer.		VAR_010809
	Natural variant	707	1	S → P. Ref.77 Ref.86 Corresponds to variant rs4986761 [ dbSNP | Ensembl ].		VAR_010810
	Natural variant	761	1	T → S. Corresponds to variant rs2235011 [ dbSNP | Ensembl ].		VAR_056679
	Natural variant	768	1	N → D in AT. Ref.63		VAR_010812
	Natural variant	785	1	R → C in AT. Ref.78		VAR_010813
	Natural variant	788	1	S → R. Corresponds to variant rs641252 [ dbSNP | Ensembl ].		VAR_056680
	Natural variant	814	1	D → E. Corresponds to variant rs3218695 [ dbSNP | Ensembl ].		VAR_056681
	Natural variant	848	1	E → Q in a lung adenocarcinoma sample; somatic mutation. Ref.86		VAR_041556
	Natural variant	858	1	F → L Rare polymorphism. Ref.56 Ref.57 Ref.70 Ref.77 Ref.78 Ref.86 Corresponds to variant rs1800056 [ dbSNP | Ensembl ].		VAR_010814
	Natural variant	872	1	P → S. Ref.86		VAR_041557
	Natural variant	924	1	R → W. Ref.86		VAR_041558
	Natural variant	935	1	T → A. Ref.86		VAR_041559
	Natural variant	935	1	T → M. Corresponds to variant rs3218708 [ dbSNP | Ensembl ].		VAR_056682
	Natural variant	942	1	L → F. Corresponds to variant rs3218688 [ dbSNP | Ensembl ].		VAR_056683
	Natural variant	950	1	L → R in AT.		VAR_010815
	Natural variant	1001	1	L → Q in AT; associated with T-cell acute lymphoblastic leukemia. Ref.63		VAR_010816
	Natural variant	1040	1	M → V in B-cell non-Hodgkin lymphoma. Ref.60 Corresponds to variant rs3092857 [ dbSNP | Ensembl ].		VAR_010817
	Natural variant	1054	1	P → R. Ref.2 Ref.56 Ref.57 Ref.70 Ref.78 Ref.80 Ref.81 Ref.86 Corresponds to variant rs1800057 [ dbSNP | Ensembl ].		VAR_010818
	Natural variant	1082	1	H → L in AT.		VAR_010819
	Natural variant	1091	1	E → D in AT. Ref.70		VAR_010820
	Natural variant	1179	1	S → F in a gastric adenocarcinoma sample; somatic mutation. Ref.86		VAR_041560
	Natural variant	1313	1	E → Q. Corresponds to variant rs3092841 [ dbSNP | Ensembl ].		VAR_056684
	Natural variant	1321	1	M → I. Ref.86		VAR_041561
	Natural variant	1380	1	H → Y. Ref.86		VAR_041562
	Natural variant	1382	1	P → S. Ref.86		VAR_041563
	Natural variant	1407	1	I → T in T-prolymphocytic leukemia. Ref.60		VAR_010821
	Natural variant	1420	1	L → F Rare polymorphism. Ref.2 Ref.56 Ref.77 Ref.86 Corresponds to variant rs1800058 [ dbSNP | Ensembl ].		VAR_010822
	Natural variant	1420	1	L → P in AT. Ref.83		VAR_010823
	Natural variant	1427	1	A → T. Corresponds to variant rs2229021 [ dbSNP | Ensembl ].		VAR_056685
	Natural variant	1454	1	K → N. Ref.79		VAR_010824
	Natural variant	1463	1	F → S in B-cell non-Hodgkin lymphoma. Ref.60		VAR_010825
	Natural variant	1465	1	L → P in AT. Ref.76		VAR_010826
	Natural variant	1469	1	I → M in a renal papillary cancer sample; somatic mutation. Ref.86		VAR_041564
	Natural variant	1475	1	Y → C. Ref.86		VAR_041565
	Natural variant	1541	1	L → F. Corresponds to variant rs3092849 [ dbSNP | Ensembl ].		VAR_056686
	Natural variant	1566	1	P → R in AT. Ref.70		VAR_010827
	Natural variant	1570	1	V → A. Ref.77		VAR_010828
	Natural variant	1650	1	N → S. Ref.86		VAR_041566
	Natural variant	1682	1	D → H in T-prolymphocytic leukemia. Ref.60		VAR_010829
	Natural variant	1691	1	S → R in AT and B-cell chronic lymphocytic leukemia; could be a rare polymorphism. Ref.56 Ref.63 Ref.75 Corresponds to variant rs1800059 [ dbSNP | Ensembl ].		VAR_010830
	Natural variant	1729	1	V → L. Corresponds to variant rs3092907 [ dbSNP | Ensembl ].		VAR_056687
	Natural variant	1739	1	N → T in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041567
	Natural variant	1743	1	T → I in AT; associated with preleukemic T-cell proliferation. Ref.63		VAR_010831
	Natural variant	1812 – 1813	2	AF → V in AT.		VAR_010832
	Natural variant	1853	1	D → N Common polymorphism. Ref.69 Ref.74 Ref.77 Ref.78 Ref.79 Ref.86 Corresponds to variant rs1801516 [ dbSNP | Ensembl ].		VAR_010833
	Natural variant	1853	1	D → V Might contribute to B-cell chronic lymphocytic leukemia. Ref.67 Ref.74 Ref.78 Ref.83 Ref.86 Corresponds to variant rs1801673 [ dbSNP | Ensembl ].		VAR_010834
	Natural variant	1910	1	L → H in T-prolymphocytic leukemia. Ref.60		VAR_010835
	Natural variant	1913	1	V → G in AT. Ref.78		VAR_010836
	Natural variant	1916	1	M → I in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.86		VAR_041568
	Natural variant	1945	1	A → T in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041569
	Natural variant	1953	1	T → R in B-cell chronic lymphocytic leukemia. Ref.74		VAR_010837
	Natural variant	1961	1	Y → C. Ref.86		VAR_041570
	Natural variant	1983	1	N → S. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.43 Ref.45 Ref.48 Ref.86		VAR_041571
	Natural variant	1991	1	E → D in a renal clear cell carcinoma sample; somatic mutation. Ref.86		VAR_041572
	Natural variant	2016	1	D → G in AT. Ref.78		VAR_010838
	Natural variant	2034	1	R → Q. Corresponds to variant rs3218670 [ dbSNP | Ensembl ].		VAR_056688
	Natural variant	2063	1	G → E in AT.		VAR_010839
	Natural variant	2067	1	A → D in AT. Ref.78		VAR_010840
	Natural variant	2079	1	V → I. Ref.2 Corresponds to variant rs1800060 [ dbSNP | Ensembl ].		VAR_010841
	Natural variant	2139	1	E → G in T-prolymphocytic leukemia; somatic mutation. Ref.72		VAR_010842
	Natural variant	2164	1	E → K in T-prolymphocytic leukemia. Ref.60		VAR_010843
	Natural variant	2218	1	S → C in AT. Ref.83		VAR_010844
	Natural variant	2224 – 2227	4	MALR → IS in AT.		VAR_010845
	Natural variant	2227	1	R → C in AT. Ref.78		VAR_010846
	Natural variant	2246 – 2252	7	CIKDILT → H in AT.		VAR_010847
	Natural variant	2274	1	A → T in B-cell chronic lymphocytic leukemia. Ref.80		VAR_010848
	Natural variant	2287	1	G → A. Ref.2 Corresponds to variant rs1800061 [ dbSNP | Ensembl ].		VAR_010849
	Natural variant	2307	1	L → F. Ref.86		VAR_041573
	Natural variant	2332	1	L → P. Ref.86		VAR_041574
	Natural variant	2335	1	T → K. Corresponds to variant rs3092831 [ dbSNP | Ensembl ].		VAR_056689
	Natural variant	2356	1	I → F in a renal clear cell carcinoma sample; somatic mutation. Ref.86		VAR_041575
	Natural variant	2396	1	T → S in T-prolymphocytic leukemia. Ref.60		VAR_010850
	Natural variant	2408	1	S → L in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041576
	Natural variant	2418	1	K → KK in mantle cell lymphoma. Ref.74 Ref.85		VAR_010851
	Natural variant	2420	1	A → P in B-cell chronic lymphocytic leukemia. Ref.74		VAR_010852
	Natural variant	2423	1	E → G in mantle cell lymphoma. Ref.74 Ref.85		VAR_010853
	Natural variant	2424	1	V → G in AT, B-cell chronic lymphocytic leukemia and T-prolymphocytic leukemia; associated with increased risk for breast cancer. Ref.54 Ref.60 Ref.63 Ref.75		VAR_010854
	Natural variant	2427 – 2428	2	Missing in AT; associated with T-prolymphocytic leukemia.		VAR_010855
	Natural variant	2438	1	T → I. Ref.55 Ref.83		VAR_010856
	Natural variant	2442	1	Q → P in T-prolymphocytic leukemia; also in a lung adenocarcinoma sample; somatic mutation. Ref.60 Ref.86		VAR_010857
	Natural variant	2443	1	R → Q in a colorectal adenocarcinoma sample; somatic mutation. Ref.86		VAR_041577
	Natural variant	2464	1	C → R. Ref.86		VAR_041578
	Natural variant	2470	1	Y → D in AT. Ref.78		VAR_010858
	Natural variant	2486	1	R → G in T-prolymphocytic leukemia. Ref.66		VAR_010859
	Natural variant	2491	1	W → R in AT. Ref.71		VAR_010860
	Natural variant	2492	1	L → R. Ref.86		VAR_041579
	Natural variant	2546 – 2548	3	Missing in AT, T-prolymphocytic leukemia and T-cell acute lymphoblastic leukemia.		VAR_010861
	Natural variant	2554	1	H → D in AT. Ref.63		VAR_010862
	Natural variant	2570	1	E → G. Corresponds to variant rs28904920 [ dbSNP | Ensembl ].		VAR_056690
	Natural variant	2625 – 2626	2	DA → EP in AT.		VAR_010864
	Natural variant	2625	1	D → Q in AT; requires 2 nucleotide substitutions. Ref.83		VAR_010863
	Natural variant	2640	1	T → I. Corresponds to variant rs4988125 [ dbSNP | Ensembl ].		VAR_056691
	Natural variant	2656	1	L → P in AT; partial functional loss. Ref.65		VAR_010865
	Natural variant	2662	1	Missing in AT. Ref.78		VAR_010866
	Natural variant	2663	1	Missing in AT.		VAR_010867
	Natural variant	2666	1	T → A in a lung adenocarcinoma sample; somatic mutation. Ref.86		VAR_041580
	Natural variant	2668	1	E → G in AT. Ref.63		VAR_010868
	Natural variant	2695	1	G → A in T-prolymphocytic leukemia and B-cell chronic lymphocytic leukemia. Ref.60 Ref.80		VAR_010869
	Natural variant	2702	1	I → R in AT.		VAR_010870
	Natural variant	2709	1	G → S. Corresponds to variant rs3218680 [ dbSNP | Ensembl ].		VAR_056692
	Natural variant	2719	1	R → H. Ref.86		VAR_041581
	Natural variant	2722	1	L → R in T-prolymphocytic leukemia. Ref.60		VAR_010871
	Natural variant	2725	1	D → G in T-prolymphocytic leukemia. Ref.61		VAR_010872
	Natural variant	2725	1	D → V in T-prolymphocytic leukemia. Ref.60		VAR_010873
	Natural variant	2726	1	A → V in AT.		VAR_010874
	Natural variant	2732	1	F → L in T-prolymphocytic leukemia. Ref.60		VAR_010875
	Natural variant	2765	1	G → S May contribute to breast cancer. Ref.77		VAR_010876
	Natural variant	2810	1	Missing in T-prolymphocytic leukemia. Ref.60		VAR_010877
	Natural variant	2824	1	C → Y in AT. Ref.14		VAR_010878
	Natural variant	2827	1	F → C in AT; mild. Ref.54 Ref.63		VAR_010879
	Natural variant	2829	1	P → L in AT. Ref.69		VAR_010880
	Natural variant	2832	1	R → C in AT and B-cell non-Hodgkin lymphoma. Ref.60 Ref.62 Ref.83		VAR_010881
	Natural variant	2842	1	P → R in a lung adenocarcinoma sample; somatic mutation. Ref.86		VAR_041582
	Natural variant	2849	1	R → P in AT. Ref.78		VAR_010882
	Natural variant	2855 – 2856	2	SV → RI in AT.		VAR_010884
	Natural variant	2855	1	S → R in AT.		VAR_010883
	Natural variant	2860	1	Missing in AT. Ref.9 Ref.59		VAR_010885
	Natural variant	2867	1	G → R in AT. Ref.58 Ref.78		VAR_010886
	Natural variant	2870	1	D → N. Ref.86		VAR_041583
	Natural variant	2871 – 2872	2	RH → S in T-prolymphocytic leukemia.		VAR_010887
	Natural variant	2890	1	L → V in T-prolymphocytic leukemia. Ref.60 Ref.72		VAR_010888
	Natural variant	2904	1	E → G in AT. Ref.59		VAR_010889
	Natural variant	2909	1	R → G in AT. Ref.71		VAR_010890
	Natural variant	3006	1	A → P in T-prolymphocytic leukemia. Ref.61		VAR_010892
	Natural variant	3008	1	R → C in AT, T-prolymphocytic leukemia and mantle cell lymphoma. Ref.61 Ref.67 Ref.72 Ref.83 Ref.85		VAR_010893
	Natural variant	3008	1	R → H in B-cell chronic lymphocytic leukemia. Ref.74		VAR_010894
	Natural variant	3018	1	K → N in B-cell chronic lymphocytic leukemia. Ref.74		VAR_010895
Experimental info
	Mutagenesis	367	1	S → 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.40
	Mutagenesis	1893	1	S → 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.40
	Mutagenesis	1981	1	S → 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.40
	Mutagenesis	1981	1	S → D or E: Disrupts the dimer. Ref.34 Ref.40
	Mutagenesis	2870	1	D → A: Loss of kinase activity. Ref.21
	Mutagenesis	2875	1	N → K: Loss of kinase activity. Ref.21
	Mutagenesis	3016	1	K → 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.42
	Mutagenesis	3018	1	K → R: Retains DNA damage-inducible acetylation and S-1981 autophosphorylation. Ref.42
	Sequence conflict	46	1	H → N in CAA62603. Ref.7
	Sequence conflict	56	1	N → I in CAA62603. Ref.7
	Sequence conflict	313	1	Y → N in CAA62603. Ref.7
	Sequence conflict	488	1	W → G in CAA62603. Ref.7
	Sequence conflict	554	1	T → A in AAC50289. Ref.1
	Sequence conflict	750	1	K → N in AAC50289. Ref.1
	Sequence conflict	754	1	Q → K in CAA62603. Ref.7
	Sequence conflict	887	1	E → G in CAA62603. Ref.7
	Sequence conflict	1003	1	Q → L in CAA62603. Ref.7
	Sequence conflict	1049	1	L → W in CAA62603. Ref.7
	Sequence conflict	1089	1	A → V in CAA62603. Ref.7
	Sequence conflict	3003	1	N → D in AAC50289. Ref.1
	Sequence conflict	3003	1	N → D in AAB38309. Ref.2
	Sequence conflict	3003	1	N → D in AAB38310. Ref.2
	Sequence conflict	3003	1	N → D in AAA86520. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q13315 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 39A88DF82E35E4BE	FASTA	3,056	350,714
	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 SQNTTISSLS 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

References

	« Hide 'large scale' referencesShow '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], VARIANT SER-1983.
[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; SER-1983; 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], VARIANT SER-1983.
[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. , 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].
[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. , 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], VARIANT SER-1983.
[6]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2756, VARIANT SER-1983.
[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. , 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, VARIANT SER-1983. 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, VARIANT SER-1983. 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, VARIANT SER-1983.
[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]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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, MASS SPECTROMETRY, MUTAGENESIS OF SER-367; SER-1893 AND SER-1981.
[41]	"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.
[42]	"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.
[43]	"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, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1983 (VARIANT SER-1983), VARIANT [LARGE SCALE ANALYSIS] SER-1983, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[44]	"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.
[45]	"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, VARIANT [LARGE SCALE ANALYSIS] SER-1983, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[46]	"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.
[47]	"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.
[48]	"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, VARIANT [LARGE SCALE ANALYSIS] SER-1983, MASS SPECTROMETRY.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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].
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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. , 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.
[60]	"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.
[61]	"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.
[62]	"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.
[63]	"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.
[64]	"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.
[65]	"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.
[66]	"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.
[67]	"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.
[68]	"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.
[69]	"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.
[70]	"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.
[71]	"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.
[72]	"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.
[73]	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)
[74]	"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.
[75]	"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.
[76]	"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.
[77]	"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.
[78]	"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.
[79]	"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.
[80]	"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.
[81]	"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.
[82]	Erratum Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T. Lancet 354:780-780(1999)
[83]	"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.
[84]	"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.
[85]	"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.
[86]	"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. , 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; SER-1983; 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Wikipedia

Ataxia telangiectasia mutated entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	U33841 mRNA. Translation: AAC50289.1. U55757 , 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 , 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. 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.
IPI	IPI00298306.
PIR	A43100.
RefSeq	NP_000042.3. NM_000051.3.
UniGene	Hs.367437.
3D structure databases
ProteinModelPortal	Q13315.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-182N.
IntAct	Q13315. 25 interactions.
MINT	MINT-194471.
STRING	9606.ENSP00000278616.
PTM databases
PhosphoSite	Q13315.
Polymorphism databases
DMDM	254763251.
Proteomic databases
PaxDb	Q13315.
PRIDE	Q13315.
Protocols and materials databases
DNASU	472.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278616; ENSP00000278616; ENSG00000149311. ENST00000452508; ENSP00000388058; ENSG00000149311.
GeneID	472.
KEGG	hsa:472.
UCSC	uc001pkb.1. human.
Organism-specific databases
CTD	472.
GeneCards	GC11P108093.
H-InvDB	HIX0010089. HIX0201637.
HGNC	HGNC:795. ATM.
HPA	CAB000102.
MIM	208900. phenotype. 607585. gene.
neXtProt	NX_Q13315.
Orphanet	100. Ataxia-telangiectasia. 67038. Chronic B-cell lymphocytic leukemia. 52416. Mantle cell lymphoma.
PharmGKB	PA61.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5032.
HOVERGEN	HBG004304.
InParanoid	Q13315.
KO	K04728.
OMA	GVLGCYC.
OrthoDB	EOG4X97G7.
Enzyme and pathway databases
Pathway_Interaction_DB	bard1pathway. BARD1 signaling events. nfkappabcanonicalpathway. Canonical NF-kappaB pathway. p38_mkk3_6pathway. p38 MAPK signaling pathway. telomerasepathway. Regulation of Telomerase.
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q13315.
Bgee	Q13315.
CleanEx	HS_ATM.
Genevestigator	Q13315.
GermOnline	ENSG00000149311. Homo sapiens.
Family and domain databases
Gene3D	1.10.1070.11. 3 hits.
InterPro	IPR016024. ARM-type_fold. IPR015519. ATM/Tel1. 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]
PANTHER	PTHR11139:SF3. PTHR11139:SF3. 1 hit.
Pfam	PF02259. FAT. 1 hit. PF02260. FATC. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. PF11640. TAN. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF56112. Kinase_like. 1 hit.
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. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q13315.
ChEMBL	CHEMBL3797.
ChiTaRS	ATM. human.
GenomeRNAi	472.
NextBio	1949.
SOURCE	Search...

Entry information

Entry name

ATM_HUMAN

Accession

Primary (citable) accession number: Q13315
Secondary accession number(s): B2RNX5 , O15429, Q12758, Q16551, Q93007, Q9NP02, Q9UCX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 166 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.