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Serine-protein kinase ATM (EC 2.7.11.1) (Ataxia telangiectasia mutated) (A-T mutated)

 ATM_HUMAN               Reviewed;        3056 AA.
Q13315; B2RNX5; O15429; Q12758; Q16551; Q93007; Q9NP02; Q9UCX7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
22-JAN-2014, sequence version 4.
22-NOV-2017, entry version 216.
RecName: Full=Serine-protein kinase ATM;
EC=2.7.11.1;
AltName: Full=Ataxia telangiectasia mutated;
Short=A-T mutated;
Name=ATM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AT ASP-3003.
PubMed=8589678; DOI=10.1093/hmg/4.11.2025;
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 / MRNA], VARIANT AT ASP-3003, AND
VARIANTS CYS-49; ARG-1054; PHE-1420; ILE-2079 AND ALA-2287.
PubMed=8665503;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9199932;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-1983.
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2756.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1369, AND VARIANT AT
2546-SER--ILE-2548 DEL.
PubMed=8789452; DOI=10.1093/hmg/5.1.145;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=9108147; DOI=10.1093/nar/25.9.1678;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1332-3056, AND VARIANTS AT
2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860 DEL AND
ASP-3003.
TISSUE=Fibroblast;
PubMed=7792600; DOI=10.1126/science.7792600;
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-3056.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1349-3056.
PubMed=8521392;
Rasio D., Negrini M., Croce C.M.;
"Genomic organization of the ATM locus involved in ataxia-
telangiectasia.";
Cancer Res. 55:6053-6057(1995).
[12]
PHOSPHORYLATION.
PubMed=8969240; DOI=10.1074/jbc.271.52.33693;
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).
[13]
SUBCELLULAR LOCATION.
PubMed=9050866; DOI=10.1073/pnas.94.5.1840;
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).
[14]
SUBCELLULAR LOCATION, AND VARIANTS AT 2546-SER--ILE-2548 DEL AND
TYR-2824.
PubMed=9150358; DOI=10.1038/sj.onc.1201037;
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).
[15]
CATALYTIC ACTIVITY.
PubMed=8988033;
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).
[16]
INTERACTION WITH ABL1.
PubMed=9168117; DOI=10.1038/387520a0;
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).
[17]
ENZYME REGULATION.
PubMed=9766667;
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).
[18]
INTERACTION WITH TP53, AND CATALYTIC ACTIVITY.
PubMed=9843217; DOI=10.1038/3882;
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).
[19]
INTERACTION WITH BETA-ADAPTIN.
PubMed=9707615; DOI=10.1073/pnas.95.17.10146;
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).
[20]
PHOSPHORYLATION OF TP53.
PubMed=9733514; DOI=10.1126/science.281.5383.1674;
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).
[21]
PHOSPHORYLATION OF TP53, AND MUTAGENESIS OF ASP-2870 AND ASN-2875.
PubMed=9733515; DOI=10.1126/science.281.5383.1677;
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).
[22]
DNA-BINDING.
PubMed=10500142; DOI=10.1073/pnas.96.20.11134;
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).
[23]
PHOSPHORYLATION OF BRCA1.
PubMed=10550055; DOI=10.1126/science.286.5442.1162;
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).
[24]
IDENTIFICATION OF ATM AS MEMBER OF BASC.
PubMed=10783165;
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).
[25]
PHOSPHORYLATION OF NBN.
PubMed=10766245; DOI=10.1038/35007091;
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).
[26]
PHOSPHORYLATION OF NBN.
PubMed=10839545; DOI=10.1038/35013089;
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).
[27]
PHOSPHORYLATION OF CTIP.
PubMed=10910365; DOI=10.1038/35018134;
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).
[28]
PHOSPHORYLATION OF NBN.
PubMed=10802669; DOI=10.1038/75508;
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).
[29]
FUNCTION IN PHOSPHORYLATION OF CHEK2.
PubMed=10973490; DOI=10.1073/pnas.190030497;
Matsuoka S., Rotman G., Ogawa A., Shiloh Y., Tamai K., Elledge S.J.;
"Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in
vitro.";
Proc. Natl. Acad. Sci. U.S.A. 97:10389-10394(2000).
[30]
PHOSPHORYLATION OF TERF1.
PubMed=11375976; DOI=10.1074/jbc.M011534200;
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).
[31]
INTERACTION WITH RAD17.
PubMed=11418864; DOI=10.1038/35082110;
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).
[32]
PHOSPHORYLATION OF FANCD2.
PubMed=12086603; DOI=10.1016/S0092-8674(02)00747-X;
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).
[33]
PHOSPHORYLATION BY NUAK1.
PubMed=12409306; DOI=10.1074/jbc.M206025200;
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).
[34]
PHOSPHORYLATION AT SER-1981, SUBUNIT, FUNCTION, AND MUTAGENESIS OF
SER-1981.
PubMed=12556884; DOI=10.1038/nature01368;
Bakkenist C.J., Kastan M.B.;
"DNA damage activates ATM through intermolecular autophosphorylation
and dimer dissociation.";
Nature 421:499-506(2003).
[35]
FUNCTION IN DNA DAMAGE RESPONSE, AND INTERACTION WITH PPP5C.
PubMed=14871926; DOI=10.1101/gad.1176004;
Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M.,
Abraham R.T., Wang X.F.;
"Requirement of protein phosphatase 5 in DNA-damage-induced ATM
activation.";
Genes Dev. 18:249-254(2004).
[36]
INTERACTION WITH DCLRE1C.
PubMed=15456891; DOI=10.1128/MCB.24.20.9207-9220.2004;
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).
[37]
INTERACTION WITH EEF1E1.
PubMed=15680327; DOI=10.1016/j.cell.2004.11.054;
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).
[38]
FUNCTION.
PubMed=15916964; DOI=10.1016/j.molcel.2005.04.015;
Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N.,
Ronai Z.;
"ATM-dependent phosphorylation of ATF2 is required for the DNA damage
response.";
Mol. Cell 18:577-587(2005).
[39]
INTERACTION WITH KAT8.
PubMed=15923642; DOI=10.1128/MCB.25.12.5292-5305.2005;
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).
[40]
FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=16086026; DOI=10.1038/nsmb972;
Kaygun H., Marzluff W.F.;
"Regulated degradation of replication-dependent histone mRNAs requires
both ATR and Upf1.";
Nat. Struct. Mol. Biol. 12:794-800(2005).
[41]
INTERACTION WITH HTATIP, PHOSPHORYLATION AT SER-1981, AND ACETYLATION.
PubMed=16141325; DOI=10.1073/pnas.0504211102;
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).
[42]
PHOSPHORYLATION AT SER-367; SER-1893 AND SER-1981, FUNCTION,
MUTAGENESIS OF SER-367; SER-1893 AND SER-1981, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16858402; DOI=10.1038/sj.emboj.7601231;
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).
[43]
INTERACTION WITH ATMIN.
PubMed=17525732; DOI=10.1038/sj.emboj.7601733;
Kanu N., Behrens A.;
"ATMIN defines an NBS1-independent pathway of ATM signalling.";
EMBO J. 26:2933-2941(2007).
[44]
ACETYLATION AT LYS-3016, FUNCTION, AND MUTAGENESIS OF LYS-3016 AND
LYS-3018.
PubMed=17923702; DOI=10.1128/MCB.01382-07;
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).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1981 AND SER-1983, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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).
[46]
INTERACTION WITH CEP164.
PubMed=18283122; DOI=10.1101/gad.1627708;
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).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
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).
[48]
INTERACTION WITH NABP2.
PubMed=18449195; DOI=10.1038/nature06883;
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).
[49]
INTERACTION WITH DDX1.
PubMed=18710941; DOI=10.1128/MCB.01053-08;
Li L., Monckton E.A., Godbout R.;
"A role for DEAD box 1 at DNA double-strand breaks.";
Mol. Cell. Biol. 28:6413-6425(2008).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[51]
FUNCTION AS DYRK2 KINASE.
PubMed=19965871; DOI=10.1074/jbc.M109.042341;
Taira N., Yamamoto H., Yamaguchi T., Miki Y., Yoshida K.;
"ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the
apoptotic response to DNA damage.";
J. Biol. Chem. 285:4909-4919(2010).
[52]
INTERACTION WITH TTI1.
PubMed=20810650; DOI=10.1101/gad.1934210;
Hurov K.E., Cotta-Ramusino C., Elledge S.J.;
"A genetic screen identifies the Triple T complex required for DNA
damage signaling and ATM and ATR stability.";
Genes Dev. 24:1939-1950(2010).
[53]
INTERACTION WITH TELO2.
PubMed=20801936; DOI=10.1101/gad.1956410;
Takai H., Xie Y., de Lange T., Pavletich N.P.;
"Tel2 structure and function in the Hsp90-dependent maturation of mTOR
and ATR complexes.";
Genes Dev. 24:2019-2030(2010).
[54]
INTERACTION WITH TELO2 AND TTI1.
PubMed=20427287; DOI=10.1074/jbc.M110.121699;
Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
Iemura S., Natsume T., Mizushima N.;
"Tti1 and Tel2 are critical factors in mammalian target of rapamycin
complex assembly.";
J. Biol. Chem. 285:20109-20116(2010).
[55]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[56]
PHOSPHORYLATION AT SER-1981.
PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005;
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y.,
Jun J.Y., You H.J.;
"Protein phosphatase 5 is necessary for ATR-mediated DNA repair.";
Biochem. Biophys. Res. Commun. 404:476-481(2011).
[57]
INTERACTION WITH BRAT1.
PubMed=22977523; DOI=10.3892/etm.2011.232;
So E.Y., Ouchi T.;
"Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK
catalytic subunit.";
Exp. Ther. Med. 2:443-447(2011).
[58]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[59]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[60]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[61]
VARIANTS AT GLY-2424; 2546-SER--ILE-2548 DEL AND CYS-2827.
PubMed=8755918;
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).
[62]
VARIANT AT 2546-SER--ILE-2548 DEL, AND VARIANT ILE-2438.
PubMed=8808599;
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).
[63]
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;
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).
[64]
VARIANT AT 705-PHE--PRO-707, AND VARIANTS LEU-858 AND ARG-1054.
PubMed=9043869;
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).
[65]
VARIANT AT ARG-2867.
PubMed=8698354; DOI=10.1007/s004390050202;
Baumer A., Bernthaler U., Wolz W., Hoehn H., Schindler D.;
"New mutations in the ataxia telangiectasia gene.";
Hum. Genet. 98:246-249(1996).
[66]
VARIANTS AT 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860
DEL AND GLY-2904.
PubMed=8845835; DOI=10.1093/hmg/5.4.433;
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).
[67]
POSSIBLE INVOLVEMENT IN TPLL AND BNHL, AND VARIANTS VAL-1040;
THR-1407; SER-1463; 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; CYS-2832 AND 2871-ARG-HIS-2872 DELINS SER AND
VAL-2890.
PubMed=9288106; DOI=10.1038/ng0997-96;
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).
[68]
POSSIBLE INVOLVEMENT IN TPLL, AND VARIANTS GLY-2725; PRO-3006 AND
CYS-3008.
PubMed=9334731; DOI=10.1038/nm1097-1155;
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).
[69]
VARIANT AT CYS-2832.
PubMed=9443866; DOI=10.1086/301673;
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).
[70]
POSSIBLE INVOLVEMENT IN TALL, AND 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.
PubMed=9463314; DOI=10.1086/301706;
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).
[71]
VARIANT AT 1812-ALA-PHE-1813 DELINS VAL.
PubMed=9497252; DOI=10.1086/301755;
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).
[72]
VARIANT AT PRO-2656.
PubMed=9450874;
DOI=10.1002/(SICI)1096-8628(19980113)75:2<141::AID-AJMG4>3.0.CO;2-W;
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).
[73]
VARIANT TPLL GLY-2486.
PubMed=9573030;
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).
[74]
VARIANTS AT 2855-ARG-ILE-2856 AND CYS-3008, AND VARIANT VAL-1853.
PubMed=9872980;
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).
[75]
VARIANT AT 2625-GLU-PRO-2626.
PubMed=9521587; DOI=10.1007/s004390050675;
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).
[76]
VARIANT AT LEU-2829, AND VARIANTS GLU-126; ASP-514 AND ASN-1853.
PubMed=9711876;
DOI=10.1002/(SICI)1098-1004(1998)12:3<186::AID-HUMU6>3.0.CO;2-F;
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).
[77]
VARIANTS AT ASP-1091 AND ARG-1566, AND VARIANTS LEU-858 AND ARG-1054.
PubMed=9792409;
DOI=10.1002/(SICI)1098-1004(1998)12:5<330::AID-HUMU6>3.0.CO;2-H;
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).
[78]
VARIANTS AT ARG-2491 AND GLY-2909.
PubMed=9792410;
DOI=10.1002/(SICI)1098-1004(1998)12:5<338::AID-HUMU7>3.0.CO;2-9;
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).
[79]
VARIANTS TPLL GLY-2139; VAL-2890 AND CYS-3008.
PubMed=9488043; DOI=10.1038/sj.onc.1201603;
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).
[80]
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).
[81]
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;
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).
[82]
VARIANTS BCLL CYS-332; ARG-1691 AND GLY-2424.
PubMed=9892178;
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).
[83]
VARIANT AT PRO-1465.
PubMed=10234507; DOI=10.1038/sj.ejhg.5200288;
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).
[84]
VARIANTS CYS-49; LEU-182; PRO-707; LEU-858; PHE-1420; ALA-1570;
ASN-1853 AND SER-2765.
PubMed=10534763;
DOI=10.1002/(SICI)1098-2264(199912)26:4<286::AID-GCC2>3.3.CO;2-O;
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).
[85]
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.
PubMed=9887333; DOI=10.1093/hmg/8.1.69;
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).
[86]
VARIANTS AT, AND VARIANTS ASN-1454 AND ASN-1853.
PubMed=10425038;
DOI=10.1002/(SICI)1098-1004(1999)14:2<156::AID-HUMU7>3.0.CO;2-E;
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).
[87]
VARIANTS BCLL THR-350; THR-352; ARG-1054; THR-2274 AND ALA-2695.
PubMed=10023947; DOI=10.1016/S0140-6736(98)10117-4;
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).
[88]
VARIANT ARG-1054.
PubMed=10217116; DOI=10.1016/S0140-6736(05)75199-0;
Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.;
"Missense mutations at ATM gene and cancer risk.";
Lancet 353:1276-1276(1999).
[89]
ERRATUM.
Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.;
Lancet 354:780-780(1999).
[90]
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.
PubMed=10817650;
DOI=10.1002/(SICI)1096-8628(20000529)92:3<170::AID-AJMG3>3.0.CO;2-#;
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).
[91]
VARIANTS AT.
PubMed=10873394; DOI=10.1006/mgme.2000.2998;
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).
[92]
VARIANTS MCL LYS-2418 INS; GLY-2423 AND CYS-3008.
PubMed=10706620; DOI=10.1073/pnas.050400997;
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).
[93]
VARIANTS [LARGE SCALE ANALYSIS] GLN-23; CYS-49; GLU-126; HIS-140;
GLN-250; PHE-333; CYS-337; HIS-337; ALA-410; SER-504; ASP-514;
TYR-540; VAL-546; LEU-582; PRO-707; GLN-848; LEU-858; SER-872;
TRP-924; ALA-935; ARG-1054; PHE-1179; ILE-1321; TYR-1380; SER-1382;
PHE-1420; MET-1469; CYS-1475; SER-1650; THR-1739; ASN-1853; VAL-1853;
ILE-1916; THR-1945; CYS-1961; ASP-1991; PHE-2307; PRO-2332; PHE-2356;
LEU-2408; PRO-2442; GLN-2443; ARG-2464; ARG-2492; ALA-2666; HIS-2719;
ARG-2842 AND ASN-2870.
PubMed=17344846; DOI=10.1038/nature05610;
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).
[94]
VARIANTS AT VAL-323; PRO-1046; ARG-2023; SER-2068; ASP-2080; HIS-2627;
LEU-2834 AND ASP-3003, CHARACTERIZATION OF VARIANTS AT VAL-323;
PRO-1046; ARG-2023; SER-2068; ASP-2080; HIS-2627; LEU-2834 AND
ASP-3003, AND PHOSPHORYLATION.
PubMed=27664052; DOI=10.1007/s12017-016-8440-8;
Carranza D., Vega A.K., Torres-Rusillo S., Montero E., Martinez L.J.,
Santamaria M., Santos J.L., Molina I.J.;
"Molecular and functional characterization of a cohort of Spanish
patients with ataxia-telangiectasia.";
NeuroMolecular Med. 19:161-174(2017).
-!- FUNCTION: Serine/threonine protein kinase which activates
checkpoint signaling upon double strand breaks (DSBs), apoptosis
and genotoxic stresses such as ionizing ultraviolet A light (UVA),
thereby acting as a DNA damage sensor. Recognizes the substrate
consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone
variant H2AX/H2AFX at double strand breaks (DSBs), thereby
regulating DNA damage response mechanism. Also plays a role in
pre-B cell allelic exclusion, a process leading to expression of a
single immunoglobulin heavy chain allele to enforce clonality and
monospecific recognition by the B-cell antigen receptor (BCR)
expressed on individual B-lymphocytes. After the introduction of
DNA breaks by the RAG complex on one immunoglobulin allele, acts
by mediating a repositioning of the second allele to
pericentromeric heterochromatin, preventing accessibility to the
RAG complex and recombination of the second allele. Also involved
in signal transduction and cell cycle control. May function as a
tumor suppressor. Necessary for activation of ABL1 and SAPK.
Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1,
CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in
vesicle and/or protein transport. Could play a role in T-cell
development, gonad and neurological function. Plays a role in
replication-dependent histone mRNA degradation. Binds DNA ends.
Phosphorylation of DYRK2 in nucleus in response to genotoxic
stress prevents its MDM2-mediated ubiquitination and subsequent
proteasome degradation. Phosphorylates ATF2 which stimulates its
function in DNA damage response. {ECO:0000269|PubMed:10973490,
ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926,
ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:16086026,
ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702,
ECO:0000269|PubMed:19965871}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:8988033, ECO:0000269|PubMed:9843217}.
-!- ENZYME REGULATION: Inhibited by wortmannin.
{ECO:0000269|PubMed:9766667}.
-!- SUBUNIT: 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. {ECO:0000250|UniProtKB:Q62388, ECO:0000269|PubMed:11418864,
ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926,
ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15680327,
ECO:0000269|PubMed:15923642, ECO:0000269|PubMed:16141325,
ECO:0000269|PubMed:17525732, ECO:0000269|PubMed:18283122,
ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:18710941,
ECO:0000269|PubMed:20427287, ECO:0000269|PubMed:20801936,
ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:22977523,
ECO:0000269|PubMed:9168117, ECO:0000269|PubMed:9707615,
ECO:0000269|PubMed:9843217}.
-!- INTERACTION:
P27958:- (xeno); NbExp=3; IntAct=EBI-495465, EBI-6904388;
Q9NY61:AATF; NbExp=3; IntAct=EBI-495465, EBI-372428;
P00519:ABL1; NbExp=4; IntAct=EBI-495465, EBI-375543;
O43313:ATMIN; NbExp=5; IntAct=EBI-495465, EBI-7422202;
Q6PJG6:BRAT1; NbExp=3; IntAct=EBI-495465, EBI-10826195;
Q5XUX0:FBXO31; NbExp=2; IntAct=EBI-495465, EBI-6162477;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-495465, EBI-81279;
Q13007:IL24; NbExp=2; IntAct=EBI-495465, EBI-3915542;
Q14676:MDC1; NbExp=2; IntAct=EBI-495465, EBI-495644;
Q9BQ15:NABP2; NbExp=4; IntAct=EBI-495465, EBI-2120336;
P11245:NAT2; NbExp=2; IntAct=EBI-495465, EBI-9057228;
O60934:NBN; NbExp=2; IntAct=EBI-495465, EBI-494844;
P46531:NOTCH1; NbExp=8; IntAct=EBI-495465, EBI-636374;
Q9BZ95:NSD3; NbExp=3; IntAct=EBI-495465, EBI-3390132;
Q7LG56:RRM2B; NbExp=3; IntAct=EBI-495465, EBI-9009083;
Q9Y4R8:TELO2; NbExp=4; IntAct=EBI-495465, EBI-1043674;
P54274:TERF1; NbExp=3; IntAct=EBI-495465, EBI-710997;
P54274-2:TERF1; NbExp=5; IntAct=EBI-495465, EBI-711018;
Q15554:TERF2; NbExp=2; IntAct=EBI-495465, EBI-706637;
O43156:TTI1; NbExp=5; IntAct=EBI-495465, EBI-1055680;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9050866,
ECO:0000269|PubMed:9150358}. Cytoplasmic vesicle
{ECO:0000269|PubMed:9050866, ECO:0000269|PubMed:9150358}.
Note=Primarily nuclear. Found also in endocytic vesicles in
association with beta-adaptin. {ECO:0000269|PubMed:9050866,
ECO:0000269|PubMed:9150358}.
-!- 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 KAT5.
-!- PTM: Phosphorylated by NUAK1/ARK5. Autophosphorylation on Ser-367,
Ser-1893, Ser-1981 correlates with DNA damage-mediated activation
of the kinase. {ECO:0000269|PubMed:12556884,
ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16858402,
ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:27664052}.
-!- 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
KAT5/TIP60. {ECO:0000269|PubMed:12556884,
ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16858402,
ECO:0000269|PubMed:17923702, ECO:0000269|PubMed:21144835}.
-!- DISEASE: Ataxia telangiectasia (AT) [MIM:208900]: A rare recessive
disorder characterized by progressive cerebellar ataxia, dilation
of the blood vessels in the conjunctiva and eyeballs,
immunodeficiency, growth retardation and sexual immaturity.
Patients have a strong predisposition to cancer; about 30% of
patients develop tumors, particularly lymphomas and leukemias.
Cells from affected individuals are highly sensitive to damage by
ionizing radiation and resistant to inhibition of DNA synthesis
following irradiation. {ECO:0000269|PubMed:10234507,
ECO:0000269|PubMed:10425038, ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:10873394, ECO:0000269|PubMed:27664052,
ECO:0000269|PubMed:7792600, ECO:0000269|PubMed:8589678,
ECO:0000269|PubMed:8665503, ECO:0000269|PubMed:8698354,
ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:8789452,
ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:8808599,
ECO:0000269|PubMed:8845835, ECO:0000269|PubMed:9043869,
ECO:0000269|PubMed:9150358, ECO:0000269|PubMed:9443866,
ECO:0000269|PubMed:9450874, ECO:0000269|PubMed:9463314,
ECO:0000269|PubMed:9497252, ECO:0000269|PubMed:9521587,
ECO:0000269|PubMed:9711876, ECO:0000269|PubMed:9792409,
ECO:0000269|PubMed:9792410, ECO:0000269|PubMed:9872980,
ECO:0000269|PubMed:9887333}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:9288106,
ECO:0000269|PubMed:9334731, ECO:0000269|PubMed:9463314,
ECO:0000269|PubMed:9488043, ECO:0000269|PubMed:9573030}.
-!- DISEASE: Note=Defects in ATM contribute to B-cell non-Hodgkin
lymphomas (BNHL), including mantle cell lymphoma (MCL).
{ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:10706620,
ECO:0000269|PubMed:9288106}.
-!- DISEASE: Note=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. {ECO:0000269|PubMed:10023947,
ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:9892178}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA86520.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA86520.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=AAI37170.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI37170.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=EAW67111.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ATMID123.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/atm/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Ataxia telangiectasia mutated
entry;
URL="https://en.wikipedia.org/wiki/Ataxia_telangiectasia_mutated";
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EMBL; U33841; AAC50289.1; -; mRNA.
EMBL; U55757; AAB38309.1; -; Genomic_DNA.
EMBL; U55704; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55705; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55707; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55708; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55709; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55710; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55711; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55712; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55713; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55714; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55715; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55716; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55717; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55718; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55719; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55720; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55721; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55722; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55723; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55724; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55725; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55726; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55727; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55728; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55729; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55730; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55731; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55732; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55733; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55734; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55735; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55736; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55737; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55738; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55739; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55740; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55741; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55742; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55743; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55744; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55745; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55746; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55747; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55748; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55749; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55750; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55751; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55752; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55753; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55754; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55755; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55756; AAB38309.1; JOINED; Genomic_DNA.
EMBL; U55757; AAB38310.1; -; Genomic_DNA.
EMBL; U55726; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55727; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55728; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55729; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55730; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55731; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55732; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55733; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55734; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55735; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55736; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55737; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55738; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55739; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55740; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55741; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55742; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55743; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55744; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55745; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55746; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55747; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55748; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55749; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55750; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55751; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55752; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55753; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55754; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55755; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U55756; AAB38310.1; JOINED; Genomic_DNA.
EMBL; U82828; AAB65827.1; -; Genomic_DNA.
EMBL; AP001925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67111.1; ALT_SEQ; Genomic_DNA.
EMBL; X91196; CAA62603.1; -; mRNA.
EMBL; U67092; AAC51298.1; -; Genomic_DNA.
EMBL; AY220758; AAO26044.1; -; Genomic_DNA.
EMBL; U26455; AAA86520.1; ALT_SEQ; mRNA.
EMBL; BC137169; AAI37170.1; ALT_SEQ; mRNA.
CCDS; CCDS31669.1; -.
PIR; A43100; A43100.
RefSeq; NP_000042.3; NM_000051.3.
RefSeq; XP_005271618.2; XM_005271561.4.
RefSeq; XP_005271619.2; XM_005271562.4.
RefSeq; XP_006718906.1; XM_006718843.3.
RefSeq; XP_006718908.1; XM_006718845.1.
RefSeq; XP_011541142.1; XM_011542840.2.
RefSeq; XP_016873278.1; XM_017017789.1.
RefSeq; XP_016873279.1; XM_017017790.1.
UniGene; Hs.367437; -.
PDB; 5NP0; EM; 5.70 A; A/B=1-3056.
PDB; 5NP1; EM; 5.70 A; A=1-3056.
PDBsum; 5NP0; -.
PDBsum; 5NP1; -.
ProteinModelPortal; Q13315; -.
SMR; Q13315; -.
BioGrid; 106962; 192.
CORUM; Q13315; -.
DIP; DIP-182N; -.
IntAct; Q13315; 81.
MINT; MINT-194471; -.
STRING; 9606.ENSP00000278616; -.
BindingDB; Q13315; -.
ChEMBL; CHEMBL3797; -.
DrugBank; DB00201; Caffeine.
GuidetoPHARMACOLOGY; 1934; -.
iPTMnet; Q13315; -.
PhosphoSitePlus; Q13315; -.
BioMuta; ATM; -.
DMDM; 317373479; -.
EPD; Q13315; -.
MaxQB; Q13315; -.
PaxDb; Q13315; -.
PeptideAtlas; Q13315; -.
PRIDE; Q13315; -.
DNASU; 472; -.
Ensembl; ENST00000278616; ENSP00000278616; ENSG00000149311.
Ensembl; ENST00000452508; ENSP00000388058; ENSG00000149311.
GeneID; 472; -.
KEGG; hsa:472; -.
UCSC; uc001pkb.1; human.
CTD; 472; -.
DisGeNET; 472; -.
EuPathDB; HostDB:ENSG00000149311.17; -.
GeneCards; ATM; -.
GeneReviews; ATM; -.
H-InvDB; HIX0010089; -.
H-InvDB; HIX0201637; -.
HGNC; HGNC:795; ATM.
HPA; CAB000102; -.
HPA; HPA067142; -.
MalaCards; ATM; -.
MIM; 208900; phenotype.
MIM; 607585; gene.
neXtProt; NX_Q13315; -.
OpenTargets; ENSG00000149311; -.
Orphanet; 100; Ataxia-telangiectasia.
Orphanet; 370109; Ataxia-telangiectasia variant.
Orphanet; 67038; B-cell chronic lymphocytic leukemia.
Orphanet; 370114; Combined cervical dystonia.
Orphanet; 52416; Mantle cell lymphoma.
PharmGKB; PA61; -.
eggNOG; KOG0892; Eukaryota.
eggNOG; ENOG410XNPY; LUCA.
GeneTree; ENSGT00670000098061; -.
HOVERGEN; HBG004304; -.
InParanoid; Q13315; -.
KO; K04728; -.
OMA; SPVCEKQ; -.
OrthoDB; EOG091G002B; -.
PhylomeDB; Q13315; -.
TreeFam; TF101182; -.
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-69541; Stabilization of p53.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-912446; Meiotic recombination.
SignaLink; Q13315; -.
SIGNOR; Q13315; -.
ChiTaRS; ATM; human.
GeneWiki; Ataxia_telangiectasia_mutated; -.
GenomeRNAi; 472; -.
PRO; PR:Q13315; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149311; -.
CleanEx; HS_ATM; -.
ExpressionAtlas; Q13315; baseline and differential.
Genevisible; Q13315; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:1990391; C:DNA repair complex; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0005819; C:spindle; IEA:Ensembl.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004677; F:DNA-dependent protein kinase activity; IDA:BHF-UCL.
GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IDA:BHF-UCL.
GO; GO:0046983; F:protein dimerization activity; IDA:BHF-UCL.
GO; GO:0047485; F:protein N-terminus binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IMP:BHF-UCL.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:CAFA.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:CAFA.
GO; GO:0071500; P:cellular response to nitrosative stress; IDA:ParkinsonsUK-UCL.
GO; GO:0071481; P:cellular response to X-ray; IDA:ParkinsonsUK-UCL.
GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IDA:BHF-UCL.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0097695; P:establishment of macromolecular complex localization to telomere; IC:BHF-UCL.
GO; GO:0097694; P:establishment of RNA localization to telomere; IMP:BHF-UCL.
GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0071044; P:histone mRNA catabolic process; IDA:UniProtKB.
GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
GO; GO:0002377; P:immunoglobulin production; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:1904354; P:negative regulation of telomere capping; IMP:BHF-UCL.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:ParkinsonsUK-UCL.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0048599; P:oocyte development; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; IMP:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:1903626; P:positive regulation of DNA catabolic process; IEA:Ensembl.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1904884; P:positive regulation of telomerase catalytic core complex assembly; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISS:BHF-UCL.
GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0002331; P:pre-B cell allelic exclusion; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0010506; P:regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:1905843; P:regulation of cellular response to gamma radiation; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:1903978; P:regulation of microglial cell activation; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IGI:BHF-UCL.
GO; GO:0090399; P:replicative senescence; IMP:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0072434; P:signal transduction involved in mitotic G2 DNA damage checkpoint; IMP:BHF-UCL.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 1.25.10.20; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015519; ATM.
InterPro; IPR003152; FATC_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011030; Lipovitellin_superhlx_dom.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR021668; TAN.
PANTHER; PTHR11139:SF96; PTHR11139:SF96; 1.
Pfam; PF02259; FAT; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF11640; TAN; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SMART; SM01342; TAN; 1.
SUPFAM; SSF48371; SSF48371; 5.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Complete proteome;
Cytoplasmic vesicle; Disease mutation; DNA damage; DNA-binding;
Kinase; Neurodegeneration; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tumor suppressor.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 3056 Serine-protein kinase ATM.
/FTId=PRO_0000088840.
DOMAIN 1960 2566 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
DOMAIN 2712 2962 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 3024 3056 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
REGION 1373 1382 Interaction with ABL1.
{ECO:0000269|PubMed:9168117}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 367 367 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16858402}.
MOD_RES 1893 1893 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:16858402}.
MOD_RES 1981 1981 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:17525332,
ECO:0000269|PubMed:12556884,
ECO:0000269|PubMed:16141325,
ECO:0000269|PubMed:16858402,
ECO:0000269|PubMed:21144835}.
MOD_RES 1983 1983 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 2996 2996 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 3016 3016 N6-acetyllysine.
{ECO:0000269|PubMed:17923702}.
VARIANT 23 23 R -> Q (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs587779858).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041545.
VARIANT 45 45 R -> W (in dbSNP:rs3218684).
/FTId=VAR_056678.
VARIANT 49 49 S -> C (in dbSNP:rs1800054).
{ECO:0000269|PubMed:10534763,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8665503,
ECO:0000269|PubMed:8797579,
ECO:0000269|PubMed:9887333}.
/FTId=VAR_010798.
VARIANT 126 126 D -> E (in dbSNP:rs2234997).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9711876}.
/FTId=VAR_010799.
VARIANT 140 140 D -> H (in dbSNP:rs55633650).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041546.
VARIANT 182 182 V -> L (in dbSNP:rs3218707).
{ECO:0000269|PubMed:10534763}.
/FTId=VAR_010800.
VARIANT 224 224 K -> E (in AT; dbSNP:rs145053092).
{ECO:0000269|PubMed:10817650}.
/FTId=VAR_010801.
VARIANT 250 250 R -> Q (in dbSNP:rs56123940).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041547.
VARIANT 292 292 P -> L (in AT; associated with lymphoma;
dbSNP:rs747727055).
{ECO:0000269|PubMed:9463314}.
/FTId=VAR_010802.
VARIANT 323 323 I -> V (in AT; loss of protein
expression; dbSNP:rs587781511).
{ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:27664052}.
/FTId=VAR_010803.
VARIANT 332 332 Y -> C (in B-cell chronic lymphocytic
leukemia). {ECO:0000269|PubMed:9892178}.
/FTId=VAR_010804.
VARIANT 333 333 S -> F (in dbSNP:rs28904919).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041548.
VARIANT 337 337 R -> C (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs138398778).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041549.
VARIANT 337 337 R -> H (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs202160435).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041550.
VARIANT 350 350 A -> T (in B-cell chronic lymphocytic
leukemia). {ECO:0000269|PubMed:10023947}.
/FTId=VAR_010805.
VARIANT 352 352 I -> T (in B-cell chronic lymphocytic
leukemia; dbSNP:rs369203092).
{ECO:0000269|PubMed:10023947}.
/FTId=VAR_010806.
VARIANT 410 410 V -> A (in dbSNP:rs56128736).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041551.
VARIANT 504 504 N -> S (in dbSNP:rs56365018).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041552.
VARIANT 514 514 G -> D (in dbSNP:rs2235000).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9711876}.
/FTId=VAR_010807.
VARIANT 540 540 C -> Y (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041553.
VARIANT 546 546 L -> V (in dbSNP:rs2227924).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041554.
VARIANT 570 570 F -> S (in AT; dbSNP:rs777301065).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010808.
VARIANT 582 582 F -> L (in dbSNP:rs2235006).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041555.
VARIANT 705 707 YSS -> FIP (in AT; might be associated
with susceptibility to cancer).
/FTId=VAR_010809.
VARIANT 707 707 S -> P (in dbSNP:rs4986761).
{ECO:0000269|PubMed:10534763,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_010810.
VARIANT 761 761 T -> S (in dbSNP:rs2235011).
/FTId=VAR_056679.
VARIANT 768 768 N -> D (in AT).
{ECO:0000269|PubMed:9463314}.
/FTId=VAR_010812.
VARIANT 785 785 R -> C (in AT; dbSNP:rs587778065).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010813.
VARIANT 788 788 S -> R (in dbSNP:rs641252).
/FTId=VAR_056680.
VARIANT 814 814 D -> E (in dbSNP:rs3218695).
/FTId=VAR_056681.
VARIANT 848 848 E -> Q (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041556.
VARIANT 858 858 F -> L (rare polymorphism;
dbSNP:rs1800056).
{ECO:0000269|PubMed:10534763,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8797579,
ECO:0000269|PubMed:9043869,
ECO:0000269|PubMed:9792409,
ECO:0000269|PubMed:9887333}.
/FTId=VAR_010814.
VARIANT 872 872 P -> S (in dbSNP:rs3218673).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041557.
VARIANT 924 924 R -> W (in dbSNP:rs55723361).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041558.
VARIANT 935 935 T -> A (in dbSNP:rs35813135).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041559.
VARIANT 935 935 T -> M (in dbSNP:rs3218708).
/FTId=VAR_056682.
VARIANT 942 942 L -> F (in dbSNP:rs3218688).
/FTId=VAR_056683.
VARIANT 950 950 L -> R (in AT; dbSNP:rs786203054).
/FTId=VAR_010815.
VARIANT 1001 1001 L -> Q (in AT; associated with T-cell
acute lymphoblastic leukemia).
{ECO:0000269|PubMed:9463314}.
/FTId=VAR_010816.
VARIANT 1040 1040 M -> V (found in B-cell non-Hodgkin
lymphoma; unknown pathological
significance; dbSNP:rs3092857).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010817.
VARIANT 1046 1046 L -> P (in AT; loss of protein
expression; dbSNP:rs568461905).
{ECO:0000269|PubMed:27664052}.
/FTId=VAR_077237.
VARIANT 1054 1054 P -> R (in dbSNP:rs1800057).
{ECO:0000269|PubMed:10023947,
ECO:0000269|PubMed:10217116,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8665503,
ECO:0000269|PubMed:8797579,
ECO:0000269|PubMed:9043869,
ECO:0000269|PubMed:9792409,
ECO:0000269|PubMed:9887333}.
/FTId=VAR_010818.
VARIANT 1082 1082 H -> L (in AT).
/FTId=VAR_010819.
VARIANT 1091 1091 E -> D (in AT).
{ECO:0000269|PubMed:9792409}.
/FTId=VAR_010820.
VARIANT 1179 1179 S -> F (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041560.
VARIANT 1313 1313 E -> Q (in dbSNP:rs3092841).
/FTId=VAR_056684.
VARIANT 1321 1321 M -> I (in dbSNP:rs35184530).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041561.
VARIANT 1380 1380 H -> Y (in dbSNP:rs3092856).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041562.
VARIANT 1382 1382 P -> S (in dbSNP:rs55859590).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041563.
VARIANT 1407 1407 I -> T (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010821.
VARIANT 1420 1420 L -> F (rare polymorphism;
dbSNP:rs1800058).
{ECO:0000269|PubMed:10534763,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8665503,
ECO:0000269|PubMed:8797579}.
/FTId=VAR_010822.
VARIANT 1420 1420 L -> P (in AT).
{ECO:0000269|PubMed:10817650}.
/FTId=VAR_010823.
VARIANT 1427 1427 A -> T (in dbSNP:rs2229021).
/FTId=VAR_056685.
VARIANT 1454 1454 K -> N (in dbSNP:rs148993589).
{ECO:0000269|PubMed:10425038}.
/FTId=VAR_010824.
VARIANT 1463 1463 F -> S (found in B-cell non-Hodgkin
lymphoma; unknown pathological
significance).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010825.
VARIANT 1465 1465 L -> P (in AT; dbSNP:rs730881391).
{ECO:0000269|PubMed:10234507}.
/FTId=VAR_010826.
VARIANT 1469 1469 I -> M (in a renal papillary cancer
sample; somatic mutation;
dbSNP:rs775047783).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041564.
VARIANT 1475 1475 Y -> C (in dbSNP:rs34640941).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041565.
VARIANT 1541 1541 L -> F (in dbSNP:rs3092849).
/FTId=VAR_056686.
VARIANT 1566 1566 P -> R (in AT).
{ECO:0000269|PubMed:9792409}.
/FTId=VAR_010827.
VARIANT 1570 1570 V -> A (in dbSNP:rs140856217).
{ECO:0000269|PubMed:10534763}.
/FTId=VAR_010828.
VARIANT 1650 1650 N -> S (in dbSNP:rs55870064).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041566.
VARIANT 1682 1682 D -> H (in T-prolymphocytic leukemia;
dbSNP:rs121434217).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010829.
VARIANT 1691 1691 S -> R (in AT and B-cell chronic
lymphocytic leukemia; unknown
pathological significance;
dbSNP:rs1800059).
{ECO:0000269|PubMed:8797579,
ECO:0000269|PubMed:9463314,
ECO:0000269|PubMed:9892178}.
/FTId=VAR_010830.
VARIANT 1729 1729 V -> L (in dbSNP:rs3092907).
/FTId=VAR_056687.
VARIANT 1739 1739 N -> T (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041567.
VARIANT 1743 1743 T -> I (in AT; associated with
preleukemic T-cell proliferation;
dbSNP:rs587779844).
{ECO:0000269|PubMed:9463314}.
/FTId=VAR_010831.
VARIANT 1812 1813 AF -> V (in AT).
{ECO:0000269|PubMed:9497252}.
/FTId=VAR_010832.
VARIANT 1853 1853 D -> N (common polymorphism;
dbSNP:rs1801516).
{ECO:0000269|PubMed:10397742,
ECO:0000269|PubMed:10425038,
ECO:0000269|PubMed:10534763,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9711876,
ECO:0000269|PubMed:9887333}.
/FTId=VAR_010833.
VARIANT 1853 1853 D -> V (might contribute to B-cell
chronic lymphocytic leukemia;
dbSNP:rs1801673).
{ECO:0000269|PubMed:10397742,
ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9872980,
ECO:0000269|PubMed:9887333}.
/FTId=VAR_010834.
VARIANT 1910 1910 L -> H (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010835.
VARIANT 1913 1913 V -> G (in AT).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010836.
VARIANT 1916 1916 M -> I (in a breast pleomorphic lobular
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041568.
VARIANT 1945 1945 A -> T (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041569.
VARIANT 1953 1953 T -> R (in B-cell chronic lymphocytic
leukemia). {ECO:0000269|PubMed:10397742}.
/FTId=VAR_010837.
VARIANT 1961 1961 Y -> C (in dbSNP:rs56399311).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041570.
VARIANT 1983 1983 S -> N (in dbSNP:rs659243).
{ECO:0000269|PubMed:16554811}.
/FTId=VAR_041571.
VARIANT 1991 1991 E -> D (in a renal clear cell carcinoma
sample; somatic mutation;
dbSNP:rs587782274).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041572.
VARIANT 2016 2016 D -> G (in AT; dbSNP:rs587781302).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010838.
VARIANT 2023 2023 G -> R (in AT; loss of protein
expression; dbSNP:rs11212587).
{ECO:0000269|PubMed:27664052}.
/FTId=VAR_077238.
VARIANT 2034 2034 R -> Q (in dbSNP:rs3218670).
/FTId=VAR_056688.
VARIANT 2063 2063 G -> E (in AT; dbSNP:rs866290641).
/FTId=VAR_010839.
VARIANT 2067 2067 A -> D (in AT; dbSNP:rs397514577).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010840.
VARIANT 2068 2068 L -> S (in AT; decreased protein
abundance; loss of DNA damage induced
protein autophosphorylation).
{ECO:0000269|PubMed:27664052}.
/FTId=VAR_077239.
VARIANT 2079 2079 V -> I (in dbSNP:rs1800060).
{ECO:0000269|PubMed:8665503}.
/FTId=VAR_010841.
VARIANT 2080 2080 Y -> D (in AT; loss of DNA damage induced
protein autophosphorylation).
{ECO:0000269|PubMed:27664052}.
/FTId=VAR_077240.
VARIANT 2139 2139 E -> G (in T-prolymphocytic leukemia;
somatic mutation).
{ECO:0000269|PubMed:9488043}.
/FTId=VAR_010842.
VARIANT 2164 2164 E -> K (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010843.
VARIANT 2218 2218 S -> C (in AT).
{ECO:0000269|PubMed:10817650}.
/FTId=VAR_010844.
VARIANT 2224 2227 MALR -> IS (in AT).
/FTId=VAR_010845.
VARIANT 2227 2227 R -> C (in AT; dbSNP:rs564652222).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010846.
VARIANT 2246 2252 CIKDILT -> H (in AT).
/FTId=VAR_010847.
VARIANT 2274 2274 A -> T (in B-cell chronic lymphocytic
leukemia; dbSNP:rs567060474).
{ECO:0000269|PubMed:10023947}.
/FTId=VAR_010848.
VARIANT 2287 2287 G -> A (in dbSNP:rs1800061).
{ECO:0000269|PubMed:8665503}.
/FTId=VAR_010849.
VARIANT 2307 2307 L -> F (in dbSNP:rs56009889).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041573.
VARIANT 2332 2332 L -> P (in dbSNP:rs4988111).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041574.
VARIANT 2335 2335 T -> K (in dbSNP:rs3092831).
/FTId=VAR_056689.
VARIANT 2356 2356 I -> F (in a renal clear cell carcinoma
sample; somatic mutation;
dbSNP:rs876658517).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041575.
VARIANT 2396 2396 T -> S (in T-prolymphocytic leukemia;
dbSNP:rs370559102).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010850.
VARIANT 2408 2408 S -> L (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs730881315).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041576.
VARIANT 2418 2418 K -> KK (in mantle cell lymphoma).
{ECO:0000269|PubMed:10397742,
ECO:0000269|PubMed:10706620}.
/FTId=VAR_010851.
VARIANT 2420 2420 A -> P (in B-cell chronic lymphocytic
leukemia). {ECO:0000269|PubMed:10397742}.
/FTId=VAR_010852.
VARIANT 2423 2423 E -> G (in mantle cell lymphoma;
dbSNP:rs121434221).
{ECO:0000269|PubMed:10397742,
ECO:0000269|PubMed:10706620}.
/FTId=VAR_010853.
VARIANT 2424 2424 V -> G (in AT, B-cell chronic lymphocytic
leukemia and T-prolymphocytic leukemia;
associated with increased risk for breast
cancer; dbSNP:rs28904921).
{ECO:0000269|PubMed:8755918,
ECO:0000269|PubMed:9288106,
ECO:0000269|PubMed:9463314,
ECO:0000269|PubMed:9892178}.
/FTId=VAR_010854.
VARIANT 2427 2428 Missing (in AT; associated with T-
prolymphocytic leukemia).
{ECO:0000269|PubMed:7792600,
ECO:0000269|PubMed:8845835,
ECO:0000269|PubMed:9463314}.
/FTId=VAR_010855.
VARIANT 2438 2438 T -> I (in dbSNP:rs147604227).
{ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:8808599}.
/FTId=VAR_010856.
VARIANT 2442 2442 Q -> P (in T-prolymphocytic leukemia;
also in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9288106}.
/FTId=VAR_010857.
VARIANT 2443 2443 R -> Q (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs587782310).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041577.
VARIANT 2464 2464 C -> R (in dbSNP:rs55801750).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041578.
VARIANT 2470 2470 Y -> D (in AT; dbSNP:rs876659365).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010858.
VARIANT 2486 2486 R -> G (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9573030}.
/FTId=VAR_010859.
VARIANT 2491 2491 W -> R (in AT).
{ECO:0000269|PubMed:9792410}.
/FTId=VAR_010860.
VARIANT 2492 2492 L -> R (in dbSNP:rs56399857).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041579.
VARIANT 2546 2548 Missing (in AT, T-prolymphocytic leukemia
and T-cell acute lymphoblastic leukemia).
{ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:7792600,
ECO:0000269|PubMed:8755918,
ECO:0000269|PubMed:8789452,
ECO:0000269|PubMed:8797579,
ECO:0000269|PubMed:8808599,
ECO:0000269|PubMed:8845835,
ECO:0000269|PubMed:9150358,
ECO:0000269|PubMed:9288106,
ECO:0000269|PubMed:9463314}.
/FTId=VAR_010861.
VARIANT 2554 2554 H -> D (in AT).
{ECO:0000269|PubMed:9463314}.
/FTId=VAR_010862.
VARIANT 2570 2570 E -> G (in dbSNP:rs28904920).
/FTId=VAR_056690.
VARIANT 2625 2626 DA -> EP (in AT; dbSNP:rs267606668).
/FTId=VAR_010864.
VARIANT 2625 2625 D -> Q (in AT; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:10817650}.
/FTId=VAR_010863.
VARIANT 2627 2627 Y -> H (in AT; loss of protein
expression).
{ECO:0000269|PubMed:27664052}.
/FTId=VAR_077241.
VARIANT 2640 2640 T -> I (in dbSNP:rs4988125).
/FTId=VAR_056691.
VARIANT 2656 2656 L -> P (in AT; dbSNP:rs121434218).
{ECO:0000269|PubMed:9450874}.
/FTId=VAR_010865.
VARIANT 2662 2662 Missing (in AT).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010866.
VARIANT 2663 2663 Missing (in AT).
/FTId=VAR_010867.
VARIANT 2666 2666 T -> A (in a lung adenocarcinoma sample;
somatic mutation; dbSNP:rs745775382).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041580.
VARIANT 2668 2668 E -> G (in AT).
{ECO:0000269|PubMed:9463314}.
/FTId=VAR_010868.
VARIANT 2695 2695 G -> A (in T-prolymphocytic leukemia and
B-cell chronic lymphocytic leukemia).
{ECO:0000269|PubMed:10023947,
ECO:0000269|PubMed:9288106}.
/FTId=VAR_010869.
VARIANT 2702 2702 I -> R (in AT; dbSNP:rs876659735).
/FTId=VAR_010870.
VARIANT 2709 2709 G -> S (in dbSNP:rs3218680).
/FTId=VAR_056692.
VARIANT 2719 2719 R -> H (in dbSNP:rs55982963).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041581.
VARIANT 2722 2722 L -> R (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010871.
VARIANT 2725 2725 D -> G (found in T-prolymphocytic
leukemia; unknown pathological
significance).
{ECO:0000269|PubMed:9334731}.
/FTId=VAR_010872.
VARIANT 2725 2725 D -> V (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010873.
VARIANT 2726 2726 A -> V (in AT).
/FTId=VAR_010874.
VARIANT 2732 2732 F -> L (in T-prolymphocytic leukemia;
dbSNP:rs876659619).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010875.
VARIANT 2765 2765 G -> S (may contribute to breast cancer;
dbSNP:rs748634900).
{ECO:0000269|PubMed:10534763}.
/FTId=VAR_010876.
VARIANT 2810 2810 Missing (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010877.
VARIANT 2824 2824 C -> Y (in AT; dbSNP:rs876660927).
{ECO:0000269|PubMed:9150358}.
/FTId=VAR_010878.
VARIANT 2827 2827 F -> C (in AT; mild; dbSNP:rs121434216).
{ECO:0000269|PubMed:8755918,
ECO:0000269|PubMed:9463314}.
/FTId=VAR_010879.
VARIANT 2829 2829 P -> L (in AT).
{ECO:0000269|PubMed:9711876}.
/FTId=VAR_010880.
VARIANT 2832 2832 R -> C (in AT; also found in B-cell non-
Hodgkin lymphoma; dbSNP:rs587779872).
{ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:9288106,
ECO:0000269|PubMed:9443866}.
/FTId=VAR_010881.
VARIANT 2834 2834 F -> L (in AT; decreased protein
abundance).
{ECO:0000269|PubMed:27664052}.
/FTId=VAR_077242.
VARIANT 2842 2842 P -> R (in a lung adenocarcinoma sample;
somatic mutation; dbSNP:rs879254065).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041582.
VARIANT 2849 2849 R -> P (in AT).
{ECO:0000269|PubMed:9887333}.
/FTId=VAR_010882.
VARIANT 2855 2856 SV -> RI (in AT; dbSNP:rs587781353).
/FTId=VAR_010884.
VARIANT 2855 2855 S -> R (in AT; dbSNP:rs780905851).
/FTId=VAR_010883.
VARIANT 2860 2860 Missing (in AT).
{ECO:0000269|PubMed:7792600,
ECO:0000269|PubMed:8845835}.
/FTId=VAR_010885.
VARIANT 2867 2867 G -> R (in AT).
{ECO:0000269|PubMed:8698354,
ECO:0000269|PubMed:9887333}.
/FTId=VAR_010886.
VARIANT 2870 2870 D -> N (in dbSNP:rs55798854).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041583.
VARIANT 2871 2872 RH -> S (in T-prolymphocytic leukemia).
{ECO:0000269|PubMed:9288106}.
/FTId=VAR_010887.
VARIANT 2890 2890 L -> V (in T-prolymphocytic leukemia;
dbSNP:rs587779874).
{ECO:0000269|PubMed:9288106,
ECO:0000269|PubMed:9488043}.
/FTId=VAR_010888.
VARIANT 2904 2904 E -> G (in AT; dbSNP:rs786202826).
{ECO:0000269|PubMed:8845835}.
/FTId=VAR_010889.
VARIANT 2909 2909 R -> G (in AT).
{ECO:0000269|PubMed:9792410}.
/FTId=VAR_010890.
VARIANT 3003 3003 N -> D (in AT; decreased protein
abundance; dbSNP:rs1137889).
{ECO:0000269|PubMed:27664052,
ECO:0000269|PubMed:7792600,
ECO:0000269|PubMed:8589678,
ECO:0000269|PubMed:8665503}.
/FTId=VAR_077243.
VARIANT 3006 3006 A -> P (found in T-prolymphocytic
leukemia; unknown pathological
significance; dbSNP:rs876658767).
{ECO:0000269|PubMed:9334731}.
/FTId=VAR_010892.
VARIANT 3008 3008 R -> C (in AT; also found in T-
prolymphocytic leukemia and mantle cell
lymphoma; dbSNP:rs587782292).
{ECO:0000269|PubMed:10706620,
ECO:0000269|PubMed:10817650,
ECO:0000269|PubMed:9334731,
ECO:0000269|PubMed:9488043,
ECO:0000269|PubMed:9872980}.
/FTId=VAR_010893.
VARIANT 3008 3008 R -> H (in B-cell chronic lymphocytic
leukemia; dbSNP:rs587781894).
{ECO:0000269|PubMed:10397742}.
/FTId=VAR_010894.
VARIANT 3018 3018 K -> N (in B-cell chronic lymphocytic
leukemia). {ECO:0000269|PubMed:10397742}.
/FTId=VAR_010895.
MUTAGEN 367 367 S->A: Loss of IR-induced S-367
autophosphorylation. Reduced correction
of cell cycle checkpoint defects and DNA-
repair activity. No effect on S-1893 nor
S-1981 autophosphorylation.
{ECO:0000269|PubMed:16858402}.
MUTAGEN 1893 1893 S->A: Loss of IR-induced S-1893
autophosphorylation. Reduced correction
of cell cycle checkpoint defects and DNA-
repair activity. No effect on S-367 nor
S-1981 autophosphorylation.
{ECO:0000269|PubMed:16858402}.
MUTAGEN 1981 1981 S->A: Loss of IR-induced S-1981
autophosphorylation. Reduced correction
of cell cycle checkpoint defects and DNA-
repair activity. No effect on S-367 nor
S-1893 autophosphorylation. No dimer
disruption. {ECO:0000269|PubMed:12556884,
ECO:0000269|PubMed:16858402}.
MUTAGEN 1981 1981 S->D,E: Disrupts the dimer.
{ECO:0000269|PubMed:12556884,
ECO:0000269|PubMed:16858402}.
MUTAGEN 2870 2870 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:9733515}.
MUTAGEN 2875 2875 N->K: Loss of kinase activity.
{ECO:0000269|PubMed:9733515}.
MUTAGEN 3016 3016 K->R: Loss of DNA damage-inducible
acetylation. Retains constitutive kinase
activity, but blocks DNA damage-induced
kinase activation. Disrupts dimer and
abolishes S-1981 autophosphorylation.
{ECO:0000269|PubMed:17923702}.
MUTAGEN 3018 3018 K->R: Retains DNA damage-inducible
acetylation and S-1981
autophosphorylation.
{ECO:0000269|PubMed:17923702}.
CONFLICT 46 46 H -> N (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 56 56 N -> I (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 313 313 Y -> N (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 488 488 W -> G (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 554 554 T -> A (in Ref. 1; AAC50289).
{ECO:0000305}.
CONFLICT 750 750 K -> N (in Ref. 1; AAC50289).
{ECO:0000305}.
CONFLICT 754 754 Q -> K (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 887 887 E -> G (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 1003 1003 Q -> L (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 1049 1049 L -> W (in Ref. 7; CAA62603).
{ECO:0000305}.
CONFLICT 1089 1089 A -> V (in Ref. 7; CAA62603).
{ECO:0000305}.
SEQUENCE 3056 AA; 350687 MW; C0B4866E1E3199E2 CRC64;
MSLVLNDLLI CCRQLEHDRA TERKKEVEKF KRLIRDPETI KHLDRHSDSK QGKYLNWDAV
FRFLQKYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL VKYFIKCANR RAPRLKCQEL
LNYIMDTVKD SSNGAIYGAD CSNILLKDIL SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ
DVHRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQCA RQEKSSSGLN HILAALTIFL
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK
GAYESTKWRS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA DICHQVFNED
TRSLEISQSY TTTQRESSDY SVPCKRKKIE LGWEVIKDHL QKSQNDFDLV PWLQIATQLI
SKYPASLPNC ELSPLLMILS QLLPQQRHGE RTPYVLRCLT EVALCQDKRS NLESSQKSDL
LKLWNKIWCI TFRGISSEQI QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACRPSCPAVC
CLTLALTTSI VPGTVKMGIE QNMCEVNRSF SLKESIMKWL LFYQLEGDLE NSTEVPPILH
SNFPHLVLEK ILVSLTMKNC KAAMNFFQSV PECEHHQKDK EELSFSEVEE LFLQTTFDKM
DFLTIVRECG IEKHQSSIGF SVHQNLKESL DRCLLGLSEQ LLNNYSSEIT NSETLVRCSR
LLVGVLGCYC YMGVIAEEEA YKSELFQKAK SLMQCAGESI TLFKNKTNEE FRIGSLRNMM
QLCTRCLSNC TKKSPNKIAS GFFLRLLTSK LMNDIADICK SLASFIKKPF DRGEVESMED
DTNGNLMEVE DQSSMNLFND YPDSSVSDAN EPGESQSTIG AINPLAEEYL SKQDLLFLDM
LKFLCLCVTT AQTNTVSFRA ADIRRKLLML IDSSTLEPTK SLHLHMYLML LKELPGEEYP
LPMEDVLELL KPLSNVCSLY RRDQDVCKTI LNHVLHVVKN LGQSNMDSEN TRDAQGQFLT
VIGAFWHLTK ERKYIFSVRM ALVNCLKTLL EADPYSKWAI LNVMGKDFPV NEVFTQFLAD
NHHQVRMLAA ESINRLFQDT KGDSSRLLKA LPLKLQQTAF ENAYLKAQEG MREMSHSAEN
PETLDEIYNR KSVLLTLIAV VLSCSPICEK QALFALCKSV KENGLEPHLV KKVLEKVSET
FGYRRLEDFM ASHLDYLVLE WLNLQDTEYN LSSFPFILLN YTNIEDFYRS CYKVLIPHLV
IRSHFDEVKS IANQIQEDWK SLLTDCFPKI LVNILPYFAY EGTRDSGMAQ QRETATKVYD
MLKSENLLGK QIDHLFISNL PEIVVELLMT LHEPANSSAS QSTDLCDFSG DLDPAPNPPH
FPSHVIKATF AYISNCHKTK LKSILEILSK SPDSYQKILL AICEQAAETN NVYKKHRILK
IYHLFVSLLL KDIKSGLGGA WAFVLRDVIY TLIHYINQRP SCIMDVSLRS FSLCCDLLSQ
VCQTAVTYCK DALENHLHVI VGTLIPLVYE QVEVQKQVLD LLKYLVIDNK DNENLYITIK
LLDPFPDHVV FKDLRITQQK IKYSRGPFSL LEEINHFLSV SVYDALPLTR LEGLKDLRRQ
LELHKDQMVD IMRASQDNPQ DGIMVKLVVN LLQLSKMAIN HTGEKEVLEA VGSCLGEVGP
IDFSTIAIQH SKDASYTKAL KLFEDKELQW TFIMLTYLNN TLVEDCVKVR SAAVTCLKNI
LATKTGHSFW EIYKMTTDPM LAYLQPFRTS RKKFLEVPRF DKENPFEGLD DINLWIPLSE
NHDIWIKTLT CAFLDSGGTK CEILQLLKPM CEVKTDFCQT VLPYLIHDIL LQDTNESWRN
LLSTHVQGFF TSCLRHFSQT SRSTTPANLD SESEHFFRCC LDKKSQRTML AVVDYMRRQK
RPSSGTIFND AFWLDLNYLE VAKVAQSCAA HFTALLYAEI YADKKSMDDQ EKRSLAFEEG
SQSTTISSLS EKSKEETGIS LQDLLLEIYR SIGEPDSLYG CGGGKMLQPI TRLRTYEHEA
MWGKALVTYD LETAIPSSTR QAGIIQALQN LGLCHILSVY LKGLDYENKD WCPELEELHY
QAAWRNMQWD HCTSVSKEVE GTSYHESLYN ALQSLRDREF STFYESLKYA RVKEVEEMCK
RSLESVYSLY PTLSRLQAIG ELESIGELFS RSVTHRQLSE VYIKWQKHSQ LLKDSDFSFQ
EPIMALRTVI LEILMEKEMD NSQRECIKDI LTKHLVELSI LARTFKNTQL PERAIFQIKQ
YNSVSCGVSE WQLEEAQVFW AKKEQSLALS ILKQMIKKLD ASCAANNPSL KLTYTECLRV
CGNWLAETCL ENPAVIMQTY LEKAVEVAGN YDGESSDELR NGKMKAFLSL ARFSDTQYQR
IENYMKSSEF ENKQALLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEL ALRALKEDRK
RFLCKAVENY INCLLSGEEH DMWVFRLCSL WLENSGVSEV NGMMKRDGMK IPTYKFLPLM
YQLAARMGTK MMGGLGFHEV LNNLISRISM DHPHHTLFII LALANANRDE FLTKPEVARR
SRITKNVPKQ SSQLDEDRTE AANRIICTIR SRRPQMVRSV EALCDAYIIL ANLDATQWKT
QRKGINIPAD QPITKLKNLE DVVVPTMEIK VDHTGEYGNL VTIQSFKAEF RLAGGVNLPK
IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL TICTYKVVPL
SQRSGVLEWC TGTVPIGEFL VNNEDGAHKR YRPNDFSAFQ CQKKMMEVQK KSFEEKYEVF
MDVCQNFQPV FRYFCMEKFL DPAIWFEKRL AYTRSVATSS IVGYILGLGD RHVQNILINE
QSAELVHIDL GVAFEQGKIL PTPETVPFRL TRDIVDGMGI TGVEGVFRRC CEKTMEVMRN
SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDETEL HPTLNADDQE CKRNLSDIDQ
SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAI DPKNLSRLFP GWKAWV


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