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UniProtKB - Q13315 (ATM_HUMAN)

Entry version 250 (23 Feb 2022)
Sequence version 4 (22 Jan 2014)
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Protein

Serine-protein kinase ATM

Gene

ATM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX 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, FBXW7, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed:9843217, PubMed:9733515, PubMed:10550055, PubMed:10766245, PubMed:10839545, PubMed:10910365, PubMed:10802669, PubMed:10973490, PubMed:11375976, PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:30612738, PubMed:30886146, PubMed:26774286).

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. Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878).

Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed:15448695).

25 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by wortmannin.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.1, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q13315

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2559586, DNA Damage/Telomere Stress Induced Senescence
R-HSA-3371453, Regulation of HSF1-mediated heat shock response
R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-5685938, HDR through Single Strand Annealing (SSA)
R-HSA-5685942, HDR through Homologous Recombination (HRR)
R-HSA-5693548, Sensing of DNA Double Strand Breaks
R-HSA-5693554, Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
R-HSA-5693579, Homologous DNA Pairing and Strand Exchange
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6796648, TP53 Regulates Transcription of DNA Repair Genes
R-HSA-6803204, TP53 Regulates Transcription of Genes Involved in Cytochrome C Release
R-HSA-6803207, TP53 Regulates Transcription of Caspase Activators and Caspases
R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-6804760, Regulation of TP53 Activity through Methylation
R-HSA-69473, G2/M DNA damage checkpoint
R-HSA-69541, Stabilization of p53
R-HSA-912446, Meiotic recombination
R-HSA-9664873, Pexophagy
R-HSA-9701192, Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function
R-HSA-9704331, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function
R-HSA-9704646, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q13315

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13315

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine-protein kinase ATM (EC:2.7.11.16 Publications)
Alternative name(s):
Ataxia telangiectasia mutated
Short name:
A-T mutated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATM
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:795, ATM

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		607585, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13315

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000149311

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Ataxia telangiectasia (AT)27 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA rare recessive disorder characterized by progressive cerebellar ataxia, dilation of the blood vessels in the conjunctiva and eyeballs, immunodeficiency, growth retardation and sexual immaturity. Patients have a strong predisposition to cancer; about 30% of patients develop tumors, particularly lymphomas and leukemias. Cells from affected individuals are highly sensitive to damage by ionizing radiation and resistant to inhibition of DNA synthesis following irradiation.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08506035 – 3056Missing in AT. 1 PublicationCorresponds to variant dbSNP:rs55861249Add BLAST3022
Natural variantiVAR_01079849S → C in AT; increases protein abundance. 9 PublicationsCorresponds to variant dbSNP:rs1800054EnsemblClinVar.1
Natural variantiVAR_010801224K → E in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs145053092EnsemblClinVar.1
Natural variantiVAR_010802292P → L in AT; associated with lymphoma; decrease phosphorylation of target proteins; increases protein abundance. 3 PublicationsCorresponds to variant dbSNP:rs747727055EnsemblClinVar.1
Natural variantiVAR_010803323I → V in AT; loss of protein expression. 2 PublicationsCorresponds to variant dbSNP:rs587781511EnsemblClinVar.1
Natural variantiVAR_085061374 – 3056Missing in AT; unknown pathological significance. 1 PublicationAdd BLAST2683
Natural variantiVAR_085062393 – 3056Missing in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587776547Add BLAST2664
Natural variantiVAR_010808570F → S in AT. 1 PublicationCorresponds to variant dbSNP:rs777301065EnsemblClinVar.1
Natural variantiVAR_010809705 – 707YSS → FIP in AT; might be associated with susceptibility to cancer. 3
Natural variantiVAR_010812768N → D in AT. 1 Publication1
Natural variantiVAR_010813785R → C in AT. 1 PublicationCorresponds to variant dbSNP:rs587778065EnsemblClinVar.1
Natural variantiVAR_010815950L → R in AT. Corresponds to variant dbSNP:rs786203054EnsemblClinVar.1
Natural variantiVAR_0108161001L → Q in AT; associated with T-cell acute lymphoblastic leukemia. 1 Publication1
Natural variantiVAR_0772371046L → P in AT; loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs568461905EnsemblClinVar.1
Natural variantiVAR_0108181054P → R in AT, B-cell chronic lymphocytic leukemia, breast cancer patients and familial cancer patients; no effect on phosphorylation of target proteins. 11 PublicationsCorresponds to variant dbSNP:rs1800057EnsemblClinVar.1
Natural variantiVAR_0108191082H → L in AT; unknown pathological significance. 1 Publication1
Natural variantiVAR_0108201091E → D in AT. 1 Publication1
Natural variantiVAR_0850631171 – 3056Missing in AT; unknown pathological significance; increases protein abundance. 1 PublicationAdd BLAST1886
Natural variantiVAR_0108231420L → P in AT. 1 Publication1
Natural variantiVAR_0108261465L → P in AT; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs730881391EnsemblClinVar.1
Natural variantiVAR_0850641466 – 3056Missing in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs730881369Add BLAST1591
Natural variantiVAR_0108271566P → R in AT. 1 Publication1
Natural variantiVAR_0108301691S → R in AT, B-cell chronic lymphocytic leukemia and familial cancer patients; no effect on phosphorylation of target proteins. 5 PublicationsCorresponds to variant dbSNP:rs1800059EnsemblClinVar.1
Natural variantiVAR_0850651730 – 3056Missing in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs764389018Add BLAST1327
Natural variantiVAR_0108311743T → I in AT; associated with preleukemic T-cell proliferation; decreased phosphorylation of target proteins. 2 PublicationsCorresponds to variant dbSNP:rs587779844EnsemblClinVar.1
Natural variantiVAR_0108321812 – 1813AF → V in AT. 1 Publication2
Natural variantiVAR_0850661839 – 3056Missing in AT; unknown pathological significance; reduces protein abundance. 1 PublicationAdd BLAST1218
Natural variantiVAR_0108361913V → G in AT. 1 PublicationCorresponds to variant dbSNP:rs1060501688EnsemblClinVar.1
Natural variantiVAR_0108382016D → G in AT; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs587781302EnsemblClinVar.1
Natural variantiVAR_0772382023G → R in AT; loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs11212587EnsemblClinVar.1
Natural variantiVAR_0108392063G → E in AT; unknown pathological significance; reduces protein abundance. 1 PublicationCorresponds to variant dbSNP:rs866290641EnsemblClinVar.1
Natural variantiVAR_0108402067A → D in AT. 1 PublicationCorresponds to variant dbSNP:rs397514577EnsemblClinVar.1
Natural variantiVAR_0772392068L → S in AT; decreased protein abundance; loss of DNA damage induced protein autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs1555114558EnsemblClinVar.1
Natural variantiVAR_0772402080Y → D in AT; loss of DNA damage induced protein autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs1064795467EnsemblClinVar.1
Natural variantiVAR_0108442218S → C in AT. 1 Publication1
Natural variantiVAR_0108452224 – 2227MALR → IS in AT; unknown pathological significance. 1 Publication4
Natural variantiVAR_0108462227R → C in AT; unknown pathological significance; reduces protein abundance. 2 PublicationsCorresponds to variant dbSNP:rs564652222EnsemblClinVar.1
Natural variantiVAR_0108472246 – 2252CIKDILT → H in AT; unknown pathological significance. 2 Publications7
Natural variantiVAR_0108542424V → G in AT; also found in B-cell chronic lymphocytic leukemia and T-prolymphocytic leukemia; may be associated with increased risk for breast cancer; decreased phosphorylation of target proteins. 5 PublicationsCorresponds to variant dbSNP:rs28904921EnsemblClinVar.1
Natural variantiVAR_0108552427 – 2428Missing in AT; also found in T-prolymphocytic leukemia; lack of phosphorylation of target proteins. 4 Publications2
Natural variantiVAR_0108582470Y → D in AT. 1 PublicationCorresponds to variant dbSNP:rs876659365EnsemblClinVar.1
Natural variantiVAR_0108602491W → R in AT. 1 Publication1
Natural variantiVAR_0108612546 – 2548Missing in AT; also found in T-prolymphocytic leukemia and T-cell acute lymphoblastic leukemia; lack of phosphorylation of target proteins. 11 Publications3
Natural variantiVAR_0850672547 – 2549Missing in AT. 1 PublicationCorresponds to variant dbSNP:rs587776547Ensembl.3
Natural variantiVAR_0108622554H → D in AT; lack of phosphorylation of target proteins. 2 Publications1
Natural variantiVAR_0108642625 – 2626DA → EP in AT. Corresponds to variant dbSNP:rs267606668Ensembl.2
Natural variantiVAR_0850682625D → E in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1196903858EnsemblClinVar.1
Natural variantiVAR_0108632625D → Q in AT; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_0850692626A → P in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs267606669EnsemblClinVar.1
Natural variantiVAR_0772412627Y → H in AT; loss of protein expression. 1 Publication1
Natural variantiVAR_0108652656L → P in AT. 1 PublicationCorresponds to variant dbSNP:rs121434218EnsemblClinVar.1
Natural variantiVAR_0108662662Missing in AT. 1 Publication1
Natural variantiVAR_0850702664Missing in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1471563800Ensembl.1
Natural variantiVAR_0108682668E → G in AT; unknown pathological significance; no effect on phosphorylation of target proteins. 2 Publications1
Natural variantiVAR_0108702702I → R in AT. Corresponds to variant dbSNP:rs876659735EnsemblClinVar.1
Natural variantiVAR_0108742726A → V in AT; unknown pathological significance. 1 Publication1
Natural variantiVAR_0108782824C → Y in AT. 1 PublicationCorresponds to variant dbSNP:rs876660927EnsemblClinVar.1
Natural variantiVAR_0108792827F → C in AT; mild; decreased phosphorylation of target proteins. 3 PublicationsCorresponds to variant dbSNP:rs121434216EnsemblClinVar.1
Natural variantiVAR_0108802829P → L in AT. 1 PublicationCorresponds to variant dbSNP:rs938431501EnsemblClinVar.1
Natural variantiVAR_0108812832R → C in AT; also found in B-cell non-Hodgkin lymphoma; increases protein abundance. 4 PublicationsCorresponds to variant dbSNP:rs587779872EnsemblClinVar.1
Natural variantiVAR_0772422834F → L in AT; decreased protein abundance. 1 Publication1
Natural variantiVAR_0850712849 – 3056Missing in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs587778080Add BLAST208
Natural variantiVAR_0108822849R → P in AT. 1 PublicationCorresponds to variant dbSNP:rs587782202EnsemblClinVar.1
Natural variantiVAR_0108842855 – 2856SV → RI in AT; lack of phosphorylation of target proteins. 1 PublicationCorresponds to variant dbSNP:rs587781353Ensembl.2
Natural variantiVAR_0108832855S → R in AT; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs780905851EnsemblClinVar.1
Natural variantiVAR_0108852860Missing in AT. 2 Publications1
Natural variantiVAR_0108862867G → R in AT. 2 Publications1
Natural variantiVAR_0108892904E → G in AT. 1 PublicationCorresponds to variant dbSNP:rs786202826EnsemblClinVar.1
Natural variantiVAR_0108902909R → G in AT. 1 Publication1
Natural variantiVAR_0772433003N → D in AT; decreased protein abundance. 4 PublicationsCorresponds to variant dbSNP:rs1137889Ensembl.1
Natural variantiVAR_0108933008R → C in AT; also found in T-prolymphocytic leukemia and mantle cell lymphoma; lack of phosphorylation of target proteins. 6 PublicationsCorresponds to variant dbSNP:rs587782292EnsemblClinVar.1
Defects in ATM may contribute to T-cell acute lymphoblastic leukemia (TALL) and T-prolymphocytic leukemia (TPLL). TPLL is characterized by a high white blood cell count, with a predominance of prolymphocytes, marked splenomegaly, lymphadenopathy, skin lesions and serous effusion. The clinical course is highly aggressive, with poor response to chemotherapy and short survival time. TPLL occurs both in adults as a sporadic disease and in younger AT patients.5 Publications
Defects in ATM may contribute to B-cell non-Hodgkin lymphomas (BNHL), including mantle cell lymphoma (MCL).3 Publications
Defects in ATM may contribute to B-cell chronic lymphocytic leukemia (BCLL). BCLL is the commonest form of leukemia in the elderly. It is characterized by the accumulation of mature CD5+ B-lymphocytes, lymphadenopathy, immunodeficiency and bone marrow failure.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi367S → A: Loss of IR-induced S-367 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-1893 nor S-1981 autophosphorylation. 1 Publication1
Mutagenesisi1807K → E: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi1893S → A: Loss of IR-induced S-1893 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1981 autophosphorylation. 1 Publication1
Mutagenesisi1941V → L: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi1981S → A: Loss of IR-induced S-1981 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1893 autophosphorylation. No dimer disruption. 2 Publications1
Mutagenesisi1981S → D or E: Disrupts the dimer. 2 Publications1
Mutagenesisi2019Y → C: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2039E → K: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi2338L → P: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2394S → L: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2452L → P: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2685S → T: No effect on phosphorylation of target proteins. 1 Publication1
Mutagenesisi2699P → L: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2708D → N: Decreased phosphorylation of target proteins. 1 Publication1
Mutagenesisi2730Q → P: Loss of phosphorylation of target proteins. 1 Publication1
Mutagenesisi2870D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi2875N → K: Loss of kinase activity. 1 Publication1
Mutagenesisi3016K → Q: Mimics acetylation, preventing dephosphorylation and subsequent ATM deactivation during the late stage of DNA damage response. 1 Publication1
Mutagenesisi3016K → R: Loss of DNA damage-inducible acetylation. Retains constitutive kinase activity, but blocks DNA damage-induced kinase activation. Disrupts dimer and abolishes S-1981 autophosphorylation. 1 Publication1
Mutagenesisi3018K → R: Retains DNA damage-inducible acetylation and S-1981 autophosphorylation. 1 Publication1

Keywords - Diseasei

Disease variant, Neurodegeneration, Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		472

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		ATM

MalaCards human disease database

More...MalaCardsi		ATM
MIMi208900, phenotype

Open Targets

More...OpenTargetsi		ENSG00000149311

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		100, Ataxia-telangiectasia
370109, Ataxia-telangiectasia variant
67038, B-cell chronic lymphocytic leukemia
52416, Mantle cell lymphoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA61

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q13315, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3797

Drug and drug target database

More...DrugBanki		DB00201, Caffeine

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1934

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ATM

Domain mapping of disease mutations (DMDM)

More...DMDMi		317373479

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000888402 – 3056Serine-protein kinase ATMAdd BLAST3055

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei367Phosphoserine; by autocatalysis1 Publication1
Modified residuei1893Phosphoserine; by autocatalysis1 Publication1
Modified residuei1981Phosphoserine; by autocatalysisCombined sources5 Publications1
Modified residuei1983PhosphoserineCombined sources1
Modified residuei2996PhosphoserineCombined sources1
Modified residuei3016N6-acetyllysine2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by NUAK1/ARK5 (PubMed:12409306). Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA damage-mediated activation of the kinase (PubMed:12556884, PubMed:16141325, PubMed:16858402, PubMed:21144835, PubMed:27664052). During the late stages of DNA damage response, dephosphorylated following deacetylation by SIRT7, leading to ATM deactivation (PubMed:30944854).7 Publications
Acetylation, on DNA damage, is required for activation of the kinase activity, dimer-monomer transition, and subsequent autophosphorylation on Ser-1981 (PubMed:12556884, PubMed:16141325, PubMed:16858402, PubMed:17923702, PubMed:21144835). Acetylated in vitro by KAT5/TIP60 (PubMed:16141325). Deacetylated by SIRT7 during the late stages of DNA damage response, promoting ATM dephosphorylation and subsequent deactivation (PubMed:30944854).6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-3210
CPTAC-3211
CPTAC-3212
CPTAC-3213
CPTAC-912
CPTAC-913

Encyclopedia of Proteome Dynamics

More...EPDi		Q13315

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13315

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q13315

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13315

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q13315

PeptideAtlas

More...PeptideAtlasi		Q13315

PRoteomics IDEntifications database

More...PRIDEi		Q13315

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		59303

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q13315, 4 sites, 2 O-linked glycans (4 sites)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13315

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q13315

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By ionizing radiation.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000149311, Expressed in corpus callosum and 239 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13315, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13315, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000149311, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:28508083). Dimers or tetramers in inactive state. On DNA damage, autophosphorylation dissociates ATM into monomers rendering them catalytically active. Binds p53/TP53, ABL1, BRCA1, NBN/nibrin and TERF1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains.

Interacts with RAD17; DNA damage promotes the association.

Interacts with EEF1E1; the interaction, induced on DNA damage, up-regulates TP53.

Interacts with DCLRE1C, KAT8, KAT5, NABP2, ATMIN and CEP164.

Interacts with AP2B1 and AP3B2; the interaction occurs in cytoplasmic vesicles (By similarity).

Interacts with TELO2 and TTI1.

Interacts with DDX1.

Interacts with BRAT1.

Interacts with CYREN (via XLF motif) (By similarity).

By similarity19 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106962, 269 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13315

Database of interacting proteins

More...DIPi		DIP-182N

Protein interaction database and analysis system

More...IntActi		Q13315, 99 interactors

Molecular INTeraction database

More...MINTi		Q13315

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000278616

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q13315

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q13315, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

13056
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q13315

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1940 – 2566FATPROSITE-ProRule annotationAdd BLAST627
Domaini2686 – 2998PI3K/PI4K catalyticPROSITE-ProRule annotationAdd BLAST313
Domaini3024 – 3056FATCPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1373 – 1382Interaction with ABL11 Publication10
Regioni2692 – 2698G-loopPROSITE-ProRule annotation7
Regioni2867 – 2875Catalytic loopPROSITE-ProRule annotation9
Regioni2887 – 2911Activation loopPROSITE-ProRule annotationAdd BLAST25

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The FATC domain is required for interaction with KAT5.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0892, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00670000098061

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000178_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13315

Identification of Orthologs from Complete Genome Data

More...OMAi		MLPLKHQ

Database of Orthologous Groups

More...OrthoDBi		80538at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13315

TreeFam database of animal gene trees

More...TreeFami		TF101182

Family and domain databases

Conserved Domains Database

More...CDDi		cd05171, PIKKc_ATM, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1070.11, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016024, ARM-type_fold
IPR015519, ATM/Tel1
IPR003152, FATC_dom
IPR011009, Kinase-like_dom_sf
IPR000403, PI3/4_kinase_cat_dom
IPR036940, PI3/4_kinase_cat_sf
IPR018936, PI3/4_kinase_CS
IPR003151, PIK-rel_kinase_FAT
IPR014009, PIK_FAT
IPR044107, PIKKc_ATM
IPR021668, TAN

The PANTHER Classification System

More...PANTHERi		PTHR11139:SF72, PTHR11139:SF72, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02259, FAT, 1 hit
PF02260, FATC, 1 hit
PF00454, PI3_PI4_kinase, 1 hit
PF11640, TAN, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01343, FATC, 1 hit
SM00146, PI3Kc, 1 hit
SM01342, TAN, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48371, SSF48371, 1 hit
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51189, FAT, 1 hit
PS51190, FATC, 1 hit
PS00915, PI3_4_KINASE_1, 1 hit
PS00916, PI3_4_KINASE_2, 1 hit
PS50290, PI3_4_KINASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All

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

GWKAWV
Length:3,056
Mass (Da):350,687
Last modified:January 22, 2014 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC0B4866E1E3199E2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PIN0E9PIN0_HUMAN
Serine-protein kinase ATM
ATM
1,545Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A6Q8PH76A0A6Q8PH76_HUMAN
Serine-protein kinase ATM
ATM
1,545Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PRG7E9PRG7_HUMAN
Serine-protein kinase ATM
ATM
93Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0QXY8M0QXY8_HUMAN
Serine-protein kinase ATM
ATM
135Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087X0E9A0A087X0E9_HUMAN
Serine-protein kinase ATM
ATM
168Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q6P7P1Q6P7P1_HUMAN
ATM protein
ATM
112Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YDU7H0YDU7_HUMAN
Serine-protein kinase ATM
ATM
155Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YEC6H0YEC6_HUMAN
Serine-protein kinase ATM
ATM
77Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A804HL86A0A804HL86_HUMAN
Serine-protein kinase ATM
ATM
357Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti46H → N in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti56N → I in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti313Y → N in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti488W → G in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti554T → A in AAC50289 (PubMed:8589678).Curated1
Sequence conflicti750K → N in AAC50289 (PubMed:8589678).Curated1
Sequence conflicti754Q → K in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti887E → G in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti1003Q → L in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti1049L → W in CAA62603 (PubMed:8789452).Curated1
Sequence conflicti1089A → V in CAA62603 (PubMed:8789452).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04154523R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587779858EnsemblClinVar.1
Natural variantiVAR_08506035 – 3056Missing in AT. 1 PublicationCorresponds to variant dbSNP:rs55861249Add BLAST3022
Natural variantiVAR_05667845R → W Found in a patient with breast cancer; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs3218684EnsemblClinVar.1
Natural variantiVAR_01079849S → C in AT; increases protein abundance. 9 PublicationsCorresponds to variant dbSNP:rs1800054EnsemblClinVar.1
Natural variantiVAR_083373