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UniProtKB/Swiss-Prot entry Q13315

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Entry information
Entry name ATM_HUMAN
Primary accession number Q13315
Secondary accession numbers O15429 Q12758 Q16551 Q93007 Q9NP02 Q9UCX7
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 121)
Name and origin of the protein
Protein name Serine-protein kinase ATM
Synonyms EC 2.7.11.1
Ataxia telangiectasia mutated
A-T, mutated
Gene name
Name: ATM
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/hmg/4.11.2025; PubMed=8589678 [NCBI, ExPASy, EBI, Israel, Japan]
Savitsky K., Sfez S., Tagle D.A., Ziv Y., Sartiel A., Collins F.S., Shiloh Y., Rotman G.;
"The complete sequence of the coding region of the ATM gene reveals similarity to cell cycle regulators in different species.";
Hum. Mol. Genet. 4:2025-2032(1995).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9199932 [NCBI, ExPASy, EBI, Israel, Japan]
Platzer M., Rotman G., Bauer D., Uziel T., Savitsky K., Bar-Shira A., Gilad S., Shiloh Y., Rosenthal A.;
"Ataxia-telangiectasia locus: sequence analysis of 184 kb of human genomic DNA containing the entire ATM gene.";
Genome Res. 7:592-605(1997).
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
DOI=10.1093/nar/25.9.1678; PubMed=9108147 [NCBI, ExPASy, EBI, Israel, Japan]
Savitsky K., Platzer M., Uziel T., Gilad S., Sartiel A., Rosenthal A., Elroy-Stein O., Shiloh Y., Rotman G.;
"Ataxia-telangiectasia: structural diversity of untranslated sequences suggests complex post-transcriptional regulation of ATM gene expression.";
Nucleic Acids Res. 25:1678-1684(1997).
[4]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-1369, AND VARIANT AT 2546-SER--ILE-2548 DEL.
DOI=10.1093/hmg/5.1.145; PubMed=8789452 [NCBI, ExPASy, EBI, Israel, Japan]
Byrd P.J., McConville C.M., Cooper P., Parkhill J., Stankovic T., McGuire G.M., Thick J.A., Taylor A.M.R.;
"Mutations revealed by sequencing the 5' half of the gene for ataxia telangiectasia.";
Hum. Mol. Genet. 5:145-149(1996).
[5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2756, AND VARIANT MCL LYS-750.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1349-3056, AND VARIANT ASN-3003.
PubMed=8521392 [NCBI, ExPASy, EBI, Israel, Japan]
Rasio D., Negrini M., Croce C.M.;
"Genomic organization of the ATM locus involved in ataxia-telangiectasia.";
Cancer Res. 55:6053-6057(1995).
[7]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1349-3056, AND VARIANTS AT 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL AND SER-2860 DEL.
TISSUE=Fibroblast;
DOI=10.1126/science.7792600; PubMed=7792600 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A single ataxia telangiectasia gene with a product similar to PI-3 kinase.";
Science 268:1749-1753(1995).
[8]
 PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS CYS-49; ARG-1054; PHE-1420; ILE-2079 AND ALA-2287.
PubMed=8665503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The ATM gene and susceptibility to breast cancer: analysis of 38 breast tumors reveals no evidence for mutation.";
Cancer Res. 56:2726-2732(1996).
[9]
 PHOSPHORYLATION.
DOI=10.1074/jbc.271.52.33693; PubMed=8969240 [NCBI, ExPASy, EBI, Israel, Japan]
Chen G., Lee E.Y.-H.P.;
"The product of the ATM gene is a 370-kDa nuclear phosphoprotein.";
J. Biol. Chem. 271:33693-33697(1996).
[10]
 SUBCELLULAR LOCATION.
DOI=10.1073/pnas.94.5.1840; PubMed=9050866 [NCBI, ExPASy, EBI, Israel, Japan]
Brown K.D., Ziv Y., Sadanandan S.N., Chessa L., Collins F.S., Shiloh Y., Tagle D.A.;
"The ataxia-telangiectasia gene product, a constitutively expressed nuclear protein that is not up-regulated following genome damage.";
Proc. Natl. Acad. Sci. U.S.A. 94:1840-1845(1997).
[11]
 SUBCELLULAR LOCATION, AND VARIANTS AT 2546-SER--ILE-2548 DEL AND TYR-2824.
DOI=10.1038/sj.onc.1201037; PubMed=9150358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Cellular localisation of the ataxia-telangiectasia (ATM) gene product and discrimination between mutated and normal forms.";
Oncogene 14:1911-1921(1997).
[12]
 KINASE ACTIVITY.
PubMed=8988033 [NCBI, ExPASy, EBI, Israel, Japan]
Jung M., Kondratyev A., Lee S.A., Dimtchev A., Dritschilo A.;
"ATM gene product phosphorylates I kappa B-alpha.";
Cancer Res. 57:24-27(1997).
[13]
 INTERACTION WITH ABL1.
DOI=10.1038/387520a0; PubMed=9168117 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Interaction between ATM protein and c-Abl in response to DNA damage.";
Nature 387:520-523(1997).
[14]
 ENZYME REGULATION.
PubMed=9766667 [NCBI, ExPASy, EBI, Israel, Japan]
Sarkaria J.N., Tibbetts R.S., Busby E.C., Kennedy A.P., Hill D.E., Abraham R.T.;
"Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin.";
Cancer Res. 58:4375-4382(1998).
[15]
 INTERACTION WITH TP53, AND KINASE ACTIVITY.
DOI=10.1038/3882; PubMed=9843217 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM associates with and phosphorylates p53: mapping the region of interaction.";
Nat. Genet. 20:398-400(1998).
[16]
 INTERACTION WITH BETA-ADAPTIN.
DOI=10.1073/pnas.95.17.10146; PubMed=9707615 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM binds to beta-adaptin in cytoplasmic vesicles.";
Proc. Natl. Acad. Sci. U.S.A. 95:10146-10151(1998).
[17]
 PHOSPHORYLATION OF TP53.
DOI=10.1126/science.281.5383.1674; PubMed=9733514 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Enhanced phosphorylation of p53 by ATM in response to DNA damage.";
Science 281:1674-1677(1998).
[18]
 PHOSPHORYLATION OF TP53, AND MUTAGENESIS OF ASP-2870 AND ASN-2875.
DOI=10.1126/science.281.5383.1677; PubMed=9733515 [NCBI, ExPASy, EBI, Israel, Japan]
Canman C.E., Lim D.-S., Cimprich K.A., Taya Y., Tamai K., Sakaguchi K., Appella E., Kastan M.B., Siliciano J.D.;
"Activation of the ATM kinase by ionizing radiation and phosphorylation of p53.";
Science 281:1677-1679(1998).
[19]
 DNA-BINDING.
DOI=10.1073/pnas.96.20.11134; PubMed=10500142 [NCBI, ExPASy, EBI, Israel, Japan]
Smith G.C.M., Cary R.B., Lakin N.D., Hann B.C., Teo S.-H., Chen D.J., Jackson S.P.;
"Purification and DNA binding properties of the ataxia-telangiectasia gene product ATM.";
Proc. Natl. Acad. Sci. U.S.A. 96:11134-11139(1999).
[20]
 PHOSPHORYLATION OF BRCA1.
DOI=10.1126/science.286.5442.1162; PubMed=10550055 [NCBI, ExPASy, EBI, Israel, Japan]
Cortez D., Wang Y., Qin J., Elledge S.J.;
"Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage response to double-strand breaks.";
Science 286:1162-1166(1999).
[21]
 IDENTIFICATION OF ATM AS MEMBER OF BASC.
DOI=10.1101/gad.827000; PubMed=10783165 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
"BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures.";
Genes Dev. 14:927-939(2000).
[22]
 PHOSPHORYLATION OF NBN.
DOI=10.1038/35007091; PubMed=10766245 [NCBI, ExPASy, EBI, Israel, Japan]
Lim D.-S., Kim S.-T., Xu B., Maser R.S., Lin J., Petrini J.H.J., Kastan M.B.;
"ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway.";
Nature 404:613-617(2000).
[23]
 PHOSPHORYLATION OF NBN.
DOI=10.1038/35013089; PubMed=10839545 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM phosphorylation of Nijmegen breakage syndrome protein is required in a DNA damage response.";
Nature 405:477-482(2000).
[24]
 PHOSPHORYLATION OF CTIP.
DOI=10.1038/35018134; PubMed=10910365 [NCBI, ExPASy, EBI, Israel, Japan]
Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y., Lee E.Y.-H.P., Lee W.-H.;
"Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response.";
Nature 406:210-215(2000).
[25]
 PHOSPHORYLATION OF NBN.
DOI=10.1038/75508; PubMed=10802669 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM-dependent phosphorylation of nibrin in response to radiation exposure.";
Nat. Genet. 25:115-119(2000).
[26]
 PHOSPHORYLATION OF TERF1.
DOI=10.1074/jbc.M011534200; PubMed=11375976 [NCBI, ExPASy, EBI, Israel, Japan]
Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.;
"Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks.";
J. Biol. Chem. 276:29282-29291(2001).
[27]
 INTERACTION WITH RAD17.
DOI=10.1038/35082110; PubMed=11418864 [NCBI, ExPASy, EBI, Israel, Japan]
Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A., Chen S.M., Abraham R.T., Wang X.-F.;
"ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses.";
Nature 411:969-974(2001).
[28]
 PHOSPHORYLATION OF FANCD2.
DOI=10.1016/S0092-8674(02)00747-X; PubMed=12086603 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Convergence of the fanconi anemia and ataxia telangiectasia signaling pathways.";
Cell 109:459-472(2002).
[29]
 PHOSPHORYLATION BY ARK5.
DOI=10.1074/jbc.M206025200; PubMed=12409306 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki A., Kusakai G., Kishimoto A., Lu J., Ogura T., Lavin M.F., Esumi H.;
"Identification of a novel protein kinase mediating Akt survival signaling to the ATM protein.";
J. Biol. Chem. 278:48-53(2003).
[30]
 AUTOPHOSPHORYLATION AT SER-1981, SUBUNIT, FUNCTION, AND MUTAGENESIS OF SER-1981.
DOI=10.1038/nature01368; PubMed=12556884 [NCBI, ExPASy, EBI, Israel, Japan]
Bakkenist C.J., Kastan M.B.;
"DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation.";
Nature 421:499-506(2003).
[31]
 INTERACTION WITH DCLRE1C.
DOI=10.1128/MCB.24.20.9207-9220.2004; PubMed=15456891 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.;
"Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response.";
Mol. Cell. Biol. 24:9207-9220(2004).
[32]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1981, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[33]
 INTERACTION WITH EEF1E1.
DOI=10.1016/j.cell.2004.11.054; PubMed=15680327 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR.";
Cell 120:209-221(2005).
[34]
 INTERACTION WITH MYST1.
DOI=10.1128/MCB.25.12.5292-5305.2005; PubMed=15923642 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Involvement of human MOF in ATM function.";
Mol. Cell. Biol. 25:5292-5305(2005).
[35]
 INTERACTION WITH HTATIP, AUTOPHOSPHORYLATION AT SER-1981, AND ACETYLATION.
DOI=10.1073/pnas.0504211102; PubMed=16141325 [NCBI, ExPASy, EBI, Israel, Japan]
Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.;
"A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM.";
Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005).
[36]
 AUTOPHOSPHORYLATION AT SER-367; SER-1893 AND SER-1981, FUNCTION, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-367; SER-1893 AND SER-1981.
DOI=10.1038/sj.emboj.7601231; PubMed=16858402 [NCBI, ExPASy, EBI, Israel, Japan]
Kozlov S.V., Graham M.E., Peng C., Chen P., Robinson P.J., Lavin M.F.;
"Involvement of novel autophosphorylation sites in ATM activation.";
EMBO J. 25:3504-3514(2006).
[37]
 INTERACTION WITH ATMIN.
DOI=10.1038/sj.emboj.7601733; PubMed=17525732 [NCBI, ExPASy, EBI, Israel, Japan]
Kanu N., Behrens A.;
"ATMIN defines an NBS1-independent pathway of ATM signalling.";
EMBO J. 26:2933-2941(2007).
[38]
 ACETYLATION AT LYS-3016, FUNCTION, AND MUTAGENESIS OF LYS-3016 AND LYS-3018.
DOI=10.1128/MCB.01382-07; PubMed=17923702 [NCBI, ExPASy, EBI, Israel, Japan]
Sun Y., Xu Y., Roy K., Price B.D.;
"DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity.";
Mol. Cell. Biol. 27:8502-8509(2007).
[39]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-85; THR-86; SER-367; THR-373; SER-1981 AND THR-1985, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[40]
 INTERACTION WITH CEP164.
DOI=10.1101/gad.1627708; PubMed=18283122 [NCBI, ExPASy, EBI, Israel, Japan]
Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.;
"Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1.";
Genes Dev. 22:587-600(2008).
[41]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1981 AND SER-2996, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[42]
 INTERACTION WITH OBFC2B.
DOI=10.1038/nature06883; PubMed=18449195 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Single-stranded DNA-binding protein hSSB1 is critical for genomic stability.";
Nature 453:677-681(2008).
[43]
 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[44]
 VARIANTS AT GLY-2424; 2546-SER--ILE-2548 DEL AND CYS-2827.
PubMed=8755918 [NCBI, ExPASy, EBI, Israel, Japan]
McConville C.M., Stankovic T., Byrd P.J., McGuire G.M., Yao Q.-Y., Lennox G.G., Taylor A.M.R.;
"Mutations associated with variant phenotypes in ataxia-telangiectasia.";
Am. J. Hum. Genet. 59:320-330(1996).
[45]
 VARIANT AT 2546-SER--ILE-2548 DEL, AND VARIANT ILE-2438.
PubMed=8808599 [NCBI, ExPASy, EBI, Israel, Japan]
Wright J., Teraoka S., Onengut S., Tolun A., Gatti R.A., Ochs H.D., Concannon P.;
"A high frequency of distinct ATM gene mutations in ataxia-telangiectasia.";
Am. J. Hum. Genet. 59:839-846(1996).
[46]
 VARIANTS AT 705-PHE--PRO-707 AND 2546-SER--ILE-2548 DEL, AND VARIANTS CYS-49; LEU-858; ARG-1054; PHE-1420 AND ARG-1691.
PubMed=8797579 [NCBI, ExPASy, EBI, Israel, Japan]
Vorechovsky I., Luo L., Lindblom A., Negrini M., Webster A.D.B., Croce C.M., Hammarstroem L.;
"ATM mutations in cancer families.";
Cancer Res. 56:4130-4133(1996).
[47]
 VARIANT AT 705-PHE--PRO-707, AND VARIANTS LEU-858 AND ARG-1054.
PubMed=9043869 [NCBI, ExPASy, EBI, Israel, Japan]
Vorechovsky I., Luo L., Prudente S., Chessa L., Russo G., Kanariou M., James M.R., Negrini M., Webster A.D.B., Hammarstroem L.;
"Exon-scanning mutation analysis of the ATM gene in patients with ataxia-telangiectasia.";
Eur. J. Hum. Genet. 4:352-355(1996).
[48]
 VARIANT AT ARG-2867.
DOI=10.1007/s004390050202; PubMed=8698354 [NCBI, ExPASy, EBI, Israel, Japan]
Baumer A., Bernthaler U., Wolz W., Hoehn H., Schindler D.;
"New mutations in the ataxia telangiectasia gene.";
Hum. Genet. 98:246-249(1996).
[49]
 VARIANTS AT 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860 DEL AND GLY-2904.
DOI=10.1093/hmg/5.4.433; PubMed=8845835 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Predominance of null mutations in ataxia-telangiectasia.";
Hum. Mol. Genet. 5:433-439(1996).
[50]
 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, AND VARIANTS BNHL VAL-1040; SER-1463 AND CYS-2832.
DOI=10.1038/ng0997-96; PubMed=9288106 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Clustering of missense mutations in the ataxia-telangiectasia gene in a sporadic T-cell leukaemia.";
Nat. Genet. 17:96-99(1997).
[51]
 VARIANTS TPLL GLY-2725; PRO-3006 AND CYS-3008.
DOI=10.1038/nm1097-1155; PubMed=9334731 [NCBI, ExPASy, EBI, Israel, Japan]
Stilgenbauer S., Schaffner C., Litterst A., Liebisch P., Gilad S., Bar-Shira A., James M.R., Lichter P., Doehner H.;
"Biallelic mutations in the ATM gene in T-prolymphocytic leukemia.";
Nat. Med. 3:1155-1159(1997).
[52]
 VARIANT AT CYS-2832.
DOI=10.1086/301673; PubMed=9443866 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Ataxia-telangiectasia: identification and detection of founder-effect mutations in the ATM gene in ethnic populations.";
Am. J. Hum. Genet. 62:86-97(1998).
[53]
 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.
DOI=10.1086/301706; PubMed=9463314 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Am. J. Hum. Genet. 62:334-345(1998).
[54]
 VARIANT AT 1812-ALA-PHE-1813 DELINS VAL.
DOI=10.1086/301755; PubMed=9497252 [NCBI, ExPASy, EBI, Israel, Japan]
Gilad S., Chessa L., Khosravi R., Russell P., Galanty Y., Piane M., Gatti R.A., Jorgensen T.J., Shiloh Y., Bar-Shira A.;
"Genotype-phenotype relationships in ataxia-telangiectasia and variants.";
Am. J. Hum. Genet. 62:551-561(1998).
[55]
 VARIANT AT PRO-2656.
DOI=10.1002/(SICI)1096-8628(19980113)75:2<141::AID-AJMG4>3.3.CO;2-8; PubMed=9450874 [NCBI, ExPASy, EBI, Israel, Japan]
Toyoshima M., Hara T., Zhang H., Yamamoto T., Akaboshi S., Nanba E., Ohno K., Hori N., Sato K., Takeshita K.;
"Ataxia-telangiectasia without immunodeficiency: novel point mutations within and adjacent to the phosphatidylinositol 3-kinase-like domain.";
Am. J. Med. Genet. 75:141-144(1998).
[56]
 VARIANT TPLL GLY-2486.
PubMed=9573030 [NCBI, ExPASy, EBI, Israel, Japan]
Stoppa-Lyonnet D., Soulier J., Lauge A., Dastot H., Garand R., Sigaux F., Stern M.-H.;
"Inactivation of the ATM gene in T-cell prolymphocytic leukemias.";
Blood 91:3920-3926(1998).
[57]
 VARIANTS AT 2855-ARG-ILE-2856 AND CYS-3008, AND VARIANT VAL-1853.
PubMed=9872980 [NCBI, ExPASy, EBI, Israel, Japan]
Hacia J.G., Sun B., Hunt N., Edgemon K., Mosbrook D., Robbins C., Fodor S.P.A., Tagle D.A., Collins F.S.;
"Strategies for mutational analysis of the large multiexon ATM gene using high-density oligonucleotide arrays.";
Genome Res. 8:1245-1258(1998).
[58]
 VARIANT AT 2625-GLU-PRO-2626.
DOI=10.1007/s004390050675; PubMed=9521587 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A double missense mutation in the ATM gene of a Dutch family with ataxia telangiectasia.";
Hum. Genet. 102:187-191(1998).
[59]
 VARIANT AT LEU-2829, AND VARIANTS GLU-126; ASP-514 AND ASN-1853.
DOI=10.1002/(SICI)1098-1004(1998)12:3<186::AID-HUMU6>3.3.CO;2-3; PubMed=9711876 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM mutations in patients with ataxia telangiectasia screened by a hierarchical strategy.";
Hum. Mutat. 12:186-195(1998).
[60]
 VARIANTS AT ASP-1091 AND ARG-1566, AND VARIANTS LEU-858 AND ARG-1054.
DOI=10.1002/(SICI)1098-1004(1998)12:5<330::AID-HUMU6>3.0.CO;2-H; PubMed=9792409 [NCBI, ExPASy, EBI, Israel, Japan]
Broeks A., de Klein A., Floore A.N., Muijtjens M., Kleijer W.J., Jaspers N.G.J., van 't Veer L.J.;
"ATM germline mutations in classical ataxia-telangiectasia patients in the Dutch population.";
Hum. Mutat. 12:330-337(1998).
[61]
 VARIANTS AT ARG-2491 AND GLY-2909.
DOI=10.1002/(SICI)1098-1004(1998)12:5<338::AID-HUMU7>3.0.CO;2-9; PubMed=9792410 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Ataxia-telangiectasia in the Japanese population: identification of R1917X, W2491R, R2909G, IVS33+2T-->A, and 7883del5, the latter two being relatively common mutations.";
Hum. Mutat. 12:338-343(1998).
[62]
 VARIANTS TPLL GLY-2139; VAL-2890 AND CYS-3008.
DOI=10.1038/sj.onc.1201603; PubMed=9488043 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM is usually rearranged in T-cell prolymphocytic leukaemia.";
Oncogene 16:789-796(1998).
[63]
 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).
[64]
 VARIANTS BCLL VAL-1853; ARG-1953; PRO-2420; HIS-3008 AND ASN-3018, VARIANTS MCL LYS-2418 INS AND GLY-2423, AND VARIANT ASN-1853.
PubMed=10397742 [NCBI, ExPASy, EBI, Israel, Japan]
Schaffner C., Stilgenbauer S., Rappold G.A., Doehner H., Lichter P.;
"Somatic ATM mutations indicate a pathogenic role of ATM in B-cell chronic lymphocytic leukemia.";
Blood 94:748-753(1999).
[65]
 VARIANTS BCLL CYS-332; ARG-1691 AND GLY-2424.
PubMed=9892178 [NCBI, ExPASy, EBI, Israel, Japan]
Bullrich F., Rasio D., Kitada S., Starostik P., Kipps T., Keating M., Albitar M., Reed J.C., Croce C.M.;
"ATM mutations in B-cell chronic lymphocytic leukemia.";
Cancer Res. 59:24-27(1999).
[66]
 VARIANT AT PRO-1465.
DOI=10.1038/sj.ejhg.5200288; PubMed=10234507 [NCBI, ExPASy, EBI, Israel, Japan]
Izatt L., Vessey C., Hodgson S.V., Solomon E.;
"Rapid and efficient ATM mutation detection by fluorescent chemical cleavage of mismatch: identification of four novel mutations.";
Eur. J. Hum. Genet. 7:310-320(1999).
[67]
 VARIANTS CYS-49; LEU-182; PRO-707; LEU-858; PHE-1420; ALA-1570; ASN-1853 AND SER-2765.
DOI=10.1002/(SICI)1098-2264(199912)26:4<286::AID-GCC2>3.3.CO;2-O; PubMed=10534763 [NCBI, ExPASy, EBI, Israel, Japan]
Izatt L., Greenman J., Hodgson S.V., Ellis D., Watts S., Scott G., Jacobs C., Liebmann R., Zvelebil M.J., Mathew C., Solomon E.;
"Identification of germline missense mutations and rare allelic variants in the ATM gene in early-onset breast cancer.";
Genes Chromosomes Cancer 26:286-294(1999).
[68]
 VARIANTS AT SER-570; CYS-785; GLY-1913; GLY-2016; ASP-2067; CYS-2227; ASP-2470; VAL-2662 DEL; PRO-2849 AND ARG-2867, AND VARIANTS CYS-49; LEU-858; ARG-1054; ASN-1853 AND VAL-1853.
DOI=10.1093/hmg/8.1.69; PubMed=9887333 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Characterization of ATM gene mutations in 66 ataxia telangiectasia families.";
Hum. Mol. Genet. 8:69-79(1999).
[69]
 VARIANTS AT, AND VARIANTS ASN-1454 AND ASN-1853.
DOI=10.1002/(SICI)1098-1004(1999)14:2<156::AID-HUMU7>3.0.CO;2-E; PubMed=10425038 [NCBI, ExPASy, EBI, Israel, Japan]
Castellvi-Bel S., Sheikhavandi S., Telatar M., Tai L.-Q., Hwang M.J., Wang Z., Yang Z., Cheng R., Gatti R.A.;
"New mutations, polymorphisms, and rare variants in the ATM gene detected by a novel SSCP strategy.";
Hum. Mutat. 14:156-162(1999).
[70]
 VARIANTS BCLL THR-350; THR-352; ARG-1054; THR-2274 AND ALA-2695, AND VARIANT ASN-3003.
DOI=10.1016/S0140-6736(98)10117-4; PubMed=10023947 [NCBI, ExPASy, EBI, Israel, Japan]
Stankovic T., Weber P., Stewart G., Bedenham T., Murray J., Byrd P.J., Moss P.A.H., Taylor A.M.R.;
"Inactivation of ataxia telangiectasia mutated gene in B-cell chronic lymphocytic leukaemia.";
Lancet 353:26-29(1999).
[71]
 VARIANT ARG-1054.
DOI=10.1016/S0140-6736(05)75199-0; PubMed=10217116 [NCBI, ExPASy, EBI, Israel, Japan]
Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.;
"Missense mutations at ATM gene and cancer risk.";
Lancet 353:1276-1276(1999).
[72]
 ERRATUM.
Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.;
Lancet 354:780-780(1999).
[73]
 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, AND VARIANTS VAL-1853 AND ILE-2438.
DOI=10.1002/(SICI)1096-8628(20000529)92:3<170::AID-AJMG3>3.0.CO;2-#; PubMed=10817650 [NCBI, ExPASy, EBI, Israel, Japan]
Li A., Swift M.;
"Mutations at the ataxia-telangiectasia locus and clinical phenotypes of A-T patients.";
Am. J. Med. Genet. 92:170-177(2000).
[74]
 VARIANTS AT.
DOI=10.1006/mgme.2000.2998; PubMed=10873394 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Ataxia-telangiectasia: phenotype/genotype studies of ATM protein expression, mutations, and radiosensitivity.";
Mol. Genet. Metab. 70:122-133(2000).
[75]
 VARIANTS MCL LYS-750; LYS-2418 INS; GLY-2423 AND CYS-3008.
DOI=10.1073/pnas.050400997; PubMed=10706620 [NCBI, ExPASy, EBI, Israel, Japan]
Schaffner C., Idler I., Stilgenbauer S., Doehner H., Lichter P.;
"Mantle cell lymphoma is characterized by inactivation of the ATM gene.";
Proc. Natl. Acad. Sci. U.S.A. 97:2773-2778(2000).
[76]
 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; ASN-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.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
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 involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates 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.
  • CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
  • ENZYME REGULATION: Inhibited by wortmannin.
  • SUBUNIT: Dimers or tetramers in inactive state. On DNA damage, autophosphorylation dissociates ATM into monomers rendering them catalytically active. Binds DNA ends, 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. DNA damage promotes association with RAD17. Interacts with EEF1E1; the interaction, induced on DNA damage, upregulates TP53. Interacts with DCLRE1C, MYST1, HTATIP, OBFC2B, ATMIN and CEP164. Interacts with the beta-adaptin complex subunits, AP2B1 AND AP3B2; the interaction occurs in cytoplasmic vesicles (By similarity).
  • INTERACTION:
    Q9NY61:AATF; NbExp=2; IntAct=EBI-495465, EBI-372428;
    P00519:ABL1; NbExp=1; IntAct=EBI-495465, EBI-375543;
    Q14676:MDC1; NbExp=1; IntAct=EBI-495465, EBI-495644;
    Q9BQ15:OBFC2B; NbExp=3; IntAct=EBI-495465, EBI-2120336;
    P62136:PPP1CA; NbExp=1; IntAct=EBI-495465, EBI-357253;
    P36873-1:PPP1CC; NbExp=1; IntAct=EBI-495465, EBI-356289;
    Q14683:SMC1A; NbExp=1; IntAct=EBI-495465, EBI-80690;
    Q9Y4R8:TELO2; NbExp=1; IntAct=EBI-495465, EBI-1043674;
    P54274:TERF1; NbExp=1; IntAct=EBI-495465, EBI-710997;
    P54274-1:TERF1; NbExp=1; IntAct=EBI-495465, EBI-711014;
    P54274-2:TERF1; NbExp=4; IntAct=EBI-495465, EBI-711018;
    P02340:Tp53 (xeno); NbExp=1; IntAct=EBI-495465, EBI-474016;
  • SUBCELLULAR LOCATION: Nucleus. Cytoplasmic vesicle. Note=Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin.
  • 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.
  • DOMAIN: The FATC domain is required for interaction with HTATIP.
  • PTM: Phosphorylated by NUAK1/ARK5. Autophosphorylation on Ser-367, Ser-1983, Ser-1981 correlates with DNA damage-mediated activation of the kinase.
  • PTM: 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 HTATIP/TIP60.
  • DISEASE: Defects in ATM are the cause of ataxia telangiectasia (AT) [MIM:208900]; also known as Louis-Bar syndrome, which includes four complementation groups: A, C, D and E. This rare recessive disorder is characterized by progressive cerebellar ataxia, dilation of the blood vessels in the conjunctiva and eyeballs, immunodeficiency, growth retardation and sexual immaturity. AT 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.
  • DISEASE: 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.
  • DISEASE: Defects in ATM contribute to B-cell non-Hodgkin lymphomas (BNHL), including mantle cell lymphoma (MCL).
  • DISEASE: 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.
  • SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
  • SIMILARITY: Contains 1 FAT domain.
  • SIMILARITY: Contains 1 FATC domain.
  • SIMILARITY: Contains 1 PI3K/PI4K domain.
  • WEB RESOURCE: Name=Ataxia talangiectasia mutation db; URL="http://benaroyaresearch.org/investigators/concannon_patrick/atm.htm";.
  • WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/ATM123.html";.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ATM";.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/atm/";.
  • WEB RESOURCE: Name=Wikipedia; Note=Ataxia telangiectasia mutated entry; URL="http://en.wikipedia.org/wiki/Ataxia_telangiectasia_mutated";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U33841; AAC50289.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U82828; AAB65827.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U67092; AAC51298.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY220758; AAO26044.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55757; AAB38309.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55704; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55705; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55707; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55708; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55709; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55710; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55711; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55712; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55713; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55714; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55715; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55716; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55717; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55718; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55719; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55720; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55721; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55722; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55723; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55724; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55725; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55726; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55727; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55728; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55729; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55730; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55731; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55732; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55733; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55734; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55735; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55736; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55737; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55738; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55739; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55740; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55741; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55742; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55743; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55744; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55745; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55746; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55747; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55748; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55749; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55750; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55751; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55752; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55753; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55754; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55755; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55756; AAB38309.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55757; AAB38310.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55726; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55727; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55728; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55729; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55730; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55731; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55732; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55733; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55734; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55735; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55736; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55737; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55738; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55739; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55740; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55741; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55742; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55743; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55744; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55745; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55746; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55747; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55748; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55749; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55750; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55751; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55752; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55753; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55754; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55755; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U55756; AAB38310.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U26455; AAA86520.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X91196; CAA62603.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00298306; -.
PIR A43100; A43100.
RefSeq NP_000042.3; -.
NP_612149.1; -.
UniGene Hs.367437
3D structure databases
ModBase Q13315.
Protein-protein interaction databases
DIP DIP:182N; -.
DIP:24193N; -.
IntAct Q13315; 19.
PTM databases
PhosphoSite Q13315; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
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_1538; Cell Cycle Checkpoints.
REACT_216; DNA Repair.
Organism-specific databases
GeneCards GC11P107598; -.
GC11P107599; -.
H-InvDB HIX0010089; -.
HIX0010090; -.
HGNC HGNC:795; ATM.
GenAtlas ATM.
HPA CAB000102; -.
MIM 208900; phenotype. [NCBI / EBI]
607585; gene. [NCBI / EBI]
Orphanet 100; Ataxia-telangiectasia.
52416; Mantle cell lymphoma.
PharmGKB PA61; -.
Gene expression databases
ArrayExpress Q13315; -.
Bgee Q13315; -.
CleanEx HS_ATM; -.
GermOnline ENSG00000149311; Homo sapiens.
Ontologies
GO
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0016303; Molecular function: 1-phosphatidylinositol-3-kinase activity (inferred from mutant phenotype from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0047485; Molecular function: protein N-terminus binding (inferred from direct assay from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from direct assay from UniProtKB).
GO:0008219; Biological process: cell death (inferred from electronic annotation from UniProtKB-KW).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0007094; Biological process: mitotic cell cycle spindle assembly checkpoint (inferred from mutant phenotype from UniProtKB).
GO:0007131; Biological process: reciprocal meiotic recombination (traceable author statement from ProtInc).
GO:0010212; Biological process: response to ionizing radiation (inferred from direct assay from UniProtKB).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR015519; Ataxia_Telang_Mut.
IPR003152; FATC.
IPR000403; PI3/4_kinase_cat.
IPR018936; PI3/4_kinase_CS.
IPR003151; PIK-rel_kinase_FAT.
IPR014009; PIK_FAT.
Graphical view of domain structure.
PANTHER PTHR11139:SF3; Ataxia_Telang_Mut; 1.
Pfam PF02259; FAT; 1.
PF02260; FATC; 1.
PF00454; PI3_PI4_kinase; 1.
Pfam graphical view of domain structure.
SMART SM00146; PI3Kc; 1.
SMART graphical view of domain structure.
PROSITE PS51189; FAT; 1.
PS51190; FATC; 1.
PS00915; PI3_4_KINASE_1; 1.
PS00916; PI3_4_KINASE_2; 1.
PS50290; PI3_4_KINASE_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q13315; -.
Genome annotation databases
Ensembl ENSG00000149311; Homo sapiens. [Contig view]
GeneID 472; -.
KEGG hsa:472; -.
Phylogenomic databases
HOVERGEN Q13315; -.
Other
NextBio 1949; -.
SOURCE ATM; Homo sapiens.
ProtoNet Q13315.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Anti-oncogene; ATP-binding; Cell cycle; Cytoplasmic vesicle; Disease mutation; DNA damage; DNA repair; DNA-binding; Kinase; Neurodegeneration; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   3056  3056     Serine-protein kinase ATM. PRO_0000088840
DOMAIN   1960   2566  607     FAT. 
DOMAIN   2712   2962  251     PI3K/PI4K. 
DOMAIN   3024   3056  33     FATC. 
REGION   1373   1382  10     Interaction with ABL1. 
MOD_RES   72     72        Phosphothreonine. 
MOD_RES   85     85        Phosphoserine. 
MOD_RES   86     86        Phosphothreonine. 
MOD_RES   367    367        Phosphoserine; by autocatalysis. 
MOD_RES   373    373        Phosphothreonine. 
MOD_RES   1893   1893        Phosphoserine; by autocatalysis. 
MOD_RES   1981   1981        Phosphoserine; by autocatalysis. 
MOD_RES   1985   1985        Phosphothreonine. 
MOD_RES   2996   2996        Phosphoserine. 
MOD_RES   3016   3016        N6-acetyllysine. 
VARIANT   23     23  1     R -> Q (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041545 
VARIANT   45     45  1     R -> W (in dbSNP:rs3218684 [NCBI]). VAR_056678 
VARIANT   49     49  1     S -> C (in dbSNP:rs1800054 [NCBI]). VAR_010798 
VARIANT   126    126  1     D -> E. VAR_010799 
VARIANT   140    140  1     D -> H. VAR_041546 
VARIANT   182    182  1     V -> L. VAR_010800 
VARIANT   224    224  1     K -> E (in AT). VAR_010801 
VARIANT   250    250  1     R -> Q. VAR_041547 
VARIANT   292    292  1     P -> L (in AT; associated with lymphoma). VAR_010802 
VARIANT   323    323  1     I -> V (in AT). VAR_010803 
VARIANT   332    332  1     Y -> C (in B-cell chronic lymphocytic leukemia). VAR_010804 
VARIANT   333    333  1     S -> F. VAR_041548 
VARIANT   337    337  1     R -> C (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041549 
VARIANT   337    337  1     R -> H (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041550 
VARIANT   350    350  1     A -> T (in B-cell chronic lymphocytic leukemia). VAR_010805 
VARIANT   352    352  1     I -> T (in B-cell chronic lymphocytic leukemia). VAR_010806 
VARIANT   410    410  1     V -> A. VAR_041551 
VARIANT   504    504  1     N -> S. VAR_041552 
VARIANT   514    514  1     G -> D. VAR_010807 
VARIANT   540    540  1     C -> Y (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041553 
VARIANT   546    546  1     L -> V. VAR_041554 
VARIANT   570    570  1     F -> S (in AT). VAR_010808 
VARIANT   582    582  1     F -> L. VAR_041555 
VARIANT   705    707  3     YSS -> FIP (in AT; might be associated with susceptibility to cancer). VAR_010809
VARIANT   707    707  1     S -> P. VAR_010810 
VARIANT   750    750  1     N -> K (in mantle cell lymphoma). VAR_010811 
VARIANT   761    761  1     T -> S (in dbSNP:rs2235011 [NCBI]). VAR_056679 
VARIANT   768    768  1     N -> D (in AT). VAR_010812 
VARIANT   785    785  1     R -> C (in AT). VAR_010813 
VARIANT   788    788  1     S -> R (in dbSNP:rs641252 [NCBI]). VAR_056680 
VARIANT   814    814  1     D -> E (in dbSNP:rs3218695 [NCBI]). VAR_056681 
VARIANT   848    848  1     E -> Q (in a lung adenocarcinoma sample; somatic mutation). VAR_041556 
VARIANT   858    858  1     F -> L (rare polymorphism; dbSNP:rs1800056 [NCBI]). VAR_010814 
VARIANT   872    872  1     P -> S. VAR_041557 
VARIANT   924    924  1     R -> W. VAR_041558 
VARIANT   935    935  1     T -> A. VAR_041559 
VARIANT   935    935  1     T -> M (in dbSNP:rs3218708 [NCBI]). VAR_056682 
VARIANT   942    942  1     L -> F (in dbSNP:rs3218688 [NCBI]). VAR_056683 
VARIANT   950    950  1     L -> R (in AT). VAR_010815 
VARIANT   1001   1001  1     L -> Q (in AT; associated with T-cell acute lymphoblastic leukemia). VAR_010816 
VARIANT   1040   1040  1     M -> V (in B-cell non-Hodgkin lymphoma; dbSNP:rs3092857 [NCBI]). VAR_010817 
VARIANT   1054   1054  1     P -> R (in dbSNP:rs1800057 [NCBI]). VAR_010818 
VARIANT   1082   1082  1     H -> L (in AT). VAR_010819 
VARIANT   1091   1091  1     E -> D (in AT). VAR_010820 
VARIANT   1179   1179  1     S -> F (in a gastric adenocarcinoma sample; somatic mutation). VAR_041560 
VARIANT   1313   1313  1     E -> Q (in dbSNP:rs3092841 [NCBI]). VAR_056684 
VARIANT   1321   1321  1     M -> I. VAR_041561 
VARIANT   1380   1380  1     H -> Y. VAR_041562 
VARIANT   1382   1382  1     P -> S. VAR_041563 
VARIANT   1407   1407  1     I -> T (in T-prolymphocytic leukemia). VAR_010821 
VARIANT   1420   1420  1     L -> F (rare polymorphism; dbSNP:rs1800058 [NCBI]). VAR_010822 
VARIANT   1420   1420  1     L -> P (in AT). VAR_010823 
VARIANT   1427   1427  1     A -> T (in dbSNP:rs2229021 [NCBI]). VAR_056685 
VARIANT   1454   1454  1     K -> N. VAR_010824 
VARIANT   1463   1463  1     F -> S (in B-cell non-Hodgkin lymphoma). VAR_010825 
VARIANT   1465   1465  1     L -> P (in AT). VAR_010826 
VARIANT   1469   1469  1     I -> M (in a renal papillary cancer sample; somatic mutation). VAR_041564 
VARIANT   1475   1475  1     Y -> C. VAR_041565 
VARIANT   1541   1541  1     L -> F (in dbSNP:rs3092849 [NCBI]). VAR_056686 
VARIANT   1566   1566  1     P -> R (in AT). VAR_010827 
VARIANT   1570   1570  1     V -> A. VAR_010828 
VARIANT   1650   1650  1     N -> S. VAR_041566 
VARIANT   1682   1682  1     D -> H (in T-prolymphocytic leukemia). VAR_010829 
VARIANT   1691   1691  1     S -> R (in AT and B-cell chronic lymphocytic leukemia; could be a rare polymorphism; dbSNP:rs1800059 [NCBI]). VAR_010830 
VARIANT   1729   1729  1     V -> L (in dbSNP:rs3092907 [NCBI]). VAR_056687 
VARIANT   1739   1739  1     N -> T (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041567 
VARIANT   1743   1743  1     T -> I (in AT; associated with preleukemic T-cell proliferation). VAR_010831 
VARIANT   1812   1813  2     AF -> V (in AT). VAR_010832
VARIANT   1853   1853  1     D -> N (common polymorphism; dbSNP:rs1801516 [NCBI]). VAR_010833 
VARIANT   1853   1853  1     D -> V (might contribute to B-cell chronic lymphocytic leukemia; dbSNP:rs1801673 [NCBI]). VAR_010834 
VARIANT   1910   1910  1     L -> H (in T-prolymphocytic leukemia). VAR_010835 
VARIANT   1913   1913  1     V -> G (in AT). VAR_010836 
VARIANT   1916   1916  1     M -> I (in a breast pleomorphic lobular carcinoma sample; somatic mutation). VAR_041568 
VARIANT   1945   1945  1     A -> T (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041569 
VARIANT   1953   1953  1     T -> R (in B-cell chronic lymphocytic leukemia). VAR_010837 
VARIANT   1961   1961  1     Y -> C. VAR_041570 
VARIANT   1983   1983  1     S -> N. VAR_041571 
VARIANT   1991   1991  1     E -> D (in a renal clear cell carcinoma sample; somatic mutation). VAR_041572 
VARIANT   2016   2016  1     D -> G (in AT). VAR_010838 
VARIANT   2034   2034  1     R -> Q (in dbSNP:rs3218670 [NCBI]). VAR_056688 
VARIANT   2063   2063  1     G -> E (in AT). VAR_010839 
VARIANT   2067   2067  1     A -> D (in AT). VAR_010840 
VARIANT   2079   2079  1     V -> I (in dbSNP:rs1800060 [NCBI]). VAR_010841 
VARIANT   2139   2139  1     E -> G (in T-prolymphocytic leukemia; somatic mutation). VAR_010842 
VARIANT   2164   2164  1     E -> K (in T-prolymphocytic leukemia). VAR_010843 
VARIANT   2218   2218  1     S -> C (in AT). VAR_010844 
VARIANT   2224   2227  4     MALR -> IS (in AT). VAR_010845
VARIANT   2227   2227  1     R -> C (in AT). VAR_010846 
VARIANT   2246   2252  7     CIKDILT -> H (in AT). VAR_010847
VARIANT   2274   2274  1     A -> T (in B-cell chronic lymphocytic leukemia). VAR_010848 
VARIANT   2287   2287  1     G -> A (in dbSNP:rs1800061 [NCBI]). VAR_010849 
VARIANT   2307   2307  1     L -> F. VAR_041573 
VARIANT   2332   2332  1     L -> P. VAR_041574 
VARIANT   2335   2335  1     T -> K (in dbSNP:rs3092831 [NCBI]). VAR_056689 
VARIANT   2356   2356  1     I -> F (in a renal clear cell carcinoma sample; somatic mutation). VAR_041575 
VARIANT   2396   2396  1     T -> S (in T-prolymphocytic leukemia). VAR_010850 
VARIANT   2408   2408  1     S -> L (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041576 
VARIANT   2418   2418  1     K -> KK (in mantle cell lymphoma). VAR_010851
VARIANT   2420   2420  1     A -> P (in B-cell chronic lymphocytic leukemia). VAR_010852 
VARIANT   2423   2423  1     E -> G (in mantle cell lymphoma). VAR_010853 
VARIANT   2424   2424  1     V -> G (in AT, B-cell chronic lymphocytic leukemia and T-prolymphocytic leukemia; associated with increased risk for breast cancer). VAR_010854 
VARIANT   2427   2428  2     Missing (in AT; associated with T-prolymphocytic leukemia). VAR_010855
VARIANT   2438   2438  1     T -> I. VAR_010856 
VARIANT   2442   2442  1     Q -> P (in T-prolymphocytic leukemia; also in a lung adenocarcinoma sample; somatic mutation). VAR_010857 
VARIANT   2443   2443  1     R -> Q (in a colorectal adenocarcinoma sample; somatic mutation). VAR_041577 
VARIANT   2464   2464  1     C -> R. VAR_041578 
VARIANT   2470   2470  1     Y -> D (in AT). VAR_010858 
VARIANT   2486   2486  1     R -> G (in T-prolymphocytic leukemia). VAR_010859 
VARIANT   2491   2491  1     W -> R (in AT). VAR_010860 
VARIANT   2492   2492  1     L -> R. VAR_041579 
VARIANT   2546   2548  3     Missing (in AT, T-prolymphocytic leukemia and T-cell acute lymphoblastic leukemia). VAR_010861
VARIANT   2554   2554  1     H -> D (in AT). VAR_010862 
VARIANT   2570   2570  1     E -> G (in dbSNP:rs28904920 [NCBI]). VAR_056690 
VARIANT   2625   2626  2     DA -> EP (in AT). VAR_010864
VARIANT   2625   2625  1     D -> Q (in AT; requires 2 nucleotide substitutions). VAR_010863 
VARIANT   2640   2640  1     T -> I (in dbSNP:rs4988125 [NCBI]). VAR_056691 
VARIANT   2656   2656  1     L -> P (in AT; partial functional loss). VAR_010865 
VARIANT   2662   2662  1     Missing (in AT). VAR_010866
VARIANT   2663   2663  1     Missing (in AT). VAR_010867
VARIANT   2666   2666  1     T -> A (in a lung adenocarcinoma sample; somatic mutation). VAR_041580 
VARIANT   2668   2668  1     E -> G (in AT). VAR_010868 
VARIANT   2695   2695  1     G -> A (in T-prolymphocytic leukemia and B-cell chronic lymphocytic leukemia). VAR_010869 
VARIANT   2702   2702  1     I -> R (in AT). VAR_010870 
VARIANT   2709   2709  1     G -> S (in dbSNP:rs3218680 [NCBI]). VAR_056692 
VARIANT   2719   2719  1     R -> H. VAR_041581 
VARIANT   2722   2722  1     L -> R (in T-prolymphocytic leukemia). VAR_010871 
VARIANT   2725   2725  1     D -> G (in T-prolymphocytic leukemia). VAR_010872 
VARIANT   2725   2725  1     D -> V (in T-prolymphocytic leukemia). VAR_010873 
VARIANT   2726   2726  1     A -> V (in AT). VAR_010874 
VARIANT   2732   2732  1     F -> L (in T-prolymphocytic leukemia). VAR_010875 
VARIANT   2765   2765  1     G -> S (may contribute to breast cancer). VAR_010876 
VARIANT   2810   2810  1     Missing (in T-prolymphocytic leukemia). VAR_010877
VARIANT   2824   2824  1     C -> Y (in AT). VAR_010878 
VARIANT   2827   2827  1     F -> C (in AT; mild). VAR_010879 
VARIANT   2829   2829  1     P -> L (in AT). VAR_010880 
VARIANT   2832   2832  1     R -> C (in AT and B-cell non-Hodgkin lymphoma). VAR_010881 
VARIANT   2842   2842  1     P -> R (in a lung adenocarcinoma sample; somatic mutation). VAR_041582 
VARIANT   2849   2849  1     R -> P (in AT). VAR_010882 
VARIANT   2855   2856  2     SV -> RI (in AT). VAR_010884
VARIANT   2855   2855  1     S -> R (in AT). VAR_010883 
VARIANT   2860   2860  1     Missing (in AT). VAR_010885
VARIANT   2867   2867  1     G -> R (in AT). VAR_010886 
VARIANT   2870   2870  1     D -> N. VAR_041583 
VARIANT   2871   2872  2     RH -> S (in T-prolymphocytic leukemia). VAR_010887
VARIANT   2890   2890  1     L -> V (in T-prolymphocytic leukemia). VAR_010888 
VARIANT   2904   2904  1     E -> G (in AT). VAR_010889 
VARIANT   2909   2909  1     R -> G (in AT). VAR_010890 
VARIANT   3003   3003  1     D -> N. VAR_010891 
VARIANT   3006   3006  1     A -> P (in T-prolymphocytic leukemia). VAR_010892 
VARIANT   3008   3008  1     R -> C (in AT, T-prolymphocytic leukemia and mantle cell lymphoma). VAR_010893 
VARIANT   3008   3008  1     R -> H (in B-cell chronic lymphocytic leukemia). VAR_010894 
VARIANT   3018   3018  1     K -> N (in B-cell chronic lymphocytic leukemia). VAR_010895 
MUTAGEN   367    367        S->A: Loss of IR-induced Ser-367 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on Ser-1893 nor Ser-1981 autophosphorylation. 
MUTAGEN   1893   1893        S->A: Loss of IR-induced Ser-1893 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on Ser-367 nor Ser-1981 autophosphorylation. 
MUTAGEN   1981   1981        S->A: Loss of IR-induced Ser-1981 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on Ser-367 nor Ser-1893 autophosphorylation. No dimer disruption. 
MUTAGEN   1981   1981        S->D,E: Disrupts the dimer. 
MUTAGEN   2870   2870        D->A: Loss of kinase activity. 
MUTAGEN   2875   2875        N->K: Loss of kinase activity. 
MUTAGEN   3016   3016        K->R: Loss of DNA damage-inducible acetylation. Retains constituitive kinase activity, but blocks DNA damage-induced kinase activation. Disrupts dimer and abolishes Ser-1981 autophosphorylation. 
MUTAGEN   3018   3018        K->R: Retains DNA damage-inducible acetylation and Ser-1981 autophosphorylation. 
CONFLICT   46     46        H -> N (in Ref. 4). 
CONFLICT   56     56        N -> I (in Ref. 4). 
CONFLICT   313    313        Y -> N (in Ref. 4). 
CONFLICT   488    488        W -> G (in Ref. 4). 
CONFLICT   554    554        A -> T (in Ref. 2, 4, 5 and 8). 
CONFLICT   754    754        Q -> K (in Ref. 4). 
CONFLICT   887    887        E -> G (in Ref. 4). 
CONFLICT   1003   1003        Q -> L (in Ref. 4). 
CONFLICT   1049   1049        L -> W (in Ref. 4). 
CONFLICT   1089   1089        A -> V (in Ref. 4). 
Sequence information
Length: 3056 AA [This is the length of the unprocessed precursor] Molecular weight: 350644 Da [This is the MW of the unprocessed precursor] CRC64: 9AB9F31BBD58B08D [This is a checksum on the sequence] 
        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 VPGAVKMGIE 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 YKSELFQKAN SLMQCAGESI TLFKNKTNEE FRIGSLRNMM 

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

      3010       3020       3030       3040       3050 
SFDKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAI DPKNLSRLFP GWKAWV
Q13315 in FASTA format

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