ID ATM_HUMAN Reviewed; 3056 AA. AC Q13315; B2RNX5; O15429; Q12758; Q16551; Q93007; Q9NP02; Q9UCX7; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 22-JAN-2014, sequence version 4. DT 27-MAR-2024, entry version 261. DE RecName: Full=Serine-protein kinase ATM; DE EC=2.7.11.1 {ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:28508083, ECO:0000269|PubMed:30886146, ECO:0000269|PubMed:8988033, ECO:0000269|PubMed:9843217}; DE AltName: Full=Ataxia telangiectasia mutated; DE Short=A-T mutated; GN Name=ATM; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AT ASP-3003. RX PubMed=8589678; DOI=10.1093/hmg/4.11.2025; RA Savitsky K., Sfez S., Tagle D.A., Ziv Y., Sartiel A., Collins F.S., RA Shiloh Y., Rotman G.; RT "The complete sequence of the coding region of the ATM gene reveals RT similarity to cell cycle regulators in different species."; RL Hum. Mol. Genet. 4:2025-2032(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT AT ASP-3003, AND VARIANTS RP CYS-49; ARG-1054; PHE-1420; ILE-2079 AND ALA-2287. RX PubMed=8665503; RA Vorechovsky I., Rasio D., Luo L., Monaco C., Hammarstroem L., RA Webster A.D.B., Zaloudik J., Barbanti-Brodano G., James M.R., Russo G., RA Croce C.M., Negrini M.; RT "The ATM gene and susceptibility to breast cancer: analysis of 38 breast RT tumors reveals no evidence for mutation."; RL Cancer Res. 56:2726-2732(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9199932; DOI=10.1101/gr.7.6.592; RA Platzer M., Rotman G., Bauer D., Uziel T., Savitsky K., Bar-Shira A., RA Gilad S., Shiloh Y., Rosenthal A.; RT "Ataxia-telangiectasia locus: sequence analysis of 184 kb of human genomic RT DNA containing the entire ATM gene."; RL Genome Res. 7:592-605(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-1983. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2756. RG NIEHS SNPs program; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1369, AND VARIANT AT 2546-SER--ILE-2548 RP DEL. RX PubMed=8789452; DOI=10.1093/hmg/5.1.145; RA Byrd P.J., McConville C.M., Cooper P., Parkhill J., Stankovic T., RA McGuire G.M., Thick J.A., Taylor A.M.R.; RT "Mutations revealed by sequencing the 5' half of the gene for ataxia RT telangiectasia."; RL Hum. Mol. Genet. 5:145-149(1996). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24. RX PubMed=9108147; DOI=10.1093/nar/25.9.1678; RA Savitsky K., Platzer M., Uziel T., Gilad S., Sartiel A., Rosenthal A., RA Elroy-Stein O., Shiloh Y., Rotman G.; RT "Ataxia-telangiectasia: structural diversity of untranslated sequences RT suggests complex post-transcriptional regulation of ATM gene expression."; RL Nucleic Acids Res. 25:1678-1684(1997). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1332-3056, AND VARIANTS 2427-LEU-ARG-2428 RP DEL; 2546-SER--ILE-2548 DEL; SER-2860 DEL AND ASP-3003. RC TISSUE=Fibroblast; RX PubMed=7792600; DOI=10.1126/science.7792600; RA Savitsky K., Bar-Shira A., Gilad S., Rotman G., Ziv Y., Vanagaite L., RA Tagle D.A., Smith S., Uziel T., Sfez S., Ashkenazi M., Pecker I., RA Frydman M., Harnik R., Patanjali S.R., Simmons A., Clines G.A., Sartiel A., RA Gatti R.A., Chessa L., Sanal O., Lavin M.F., Jaspers N.G.J., Taylor A.M.R., RA Arlett C.F., Miki T., Weissman S.M., Lovett M., Collins F.S., Shiloh Y.; RT "A single ataxia telangiectasia gene with a product similar to PI-3 RT kinase."; RL Science 268:1749-1753(1995). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-3056. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1349-3056. RX PubMed=8521392; RA Rasio D., Negrini M., Croce C.M.; RT "Genomic organization of the ATM locus involved in ataxia-telangiectasia."; RL Cancer Res. 55:6053-6057(1995). RN [12] RP PHOSPHORYLATION. RX PubMed=8969240; DOI=10.1074/jbc.271.52.33693; RA Chen G., Lee E.Y.-H.P.; RT "The product of the ATM gene is a 370-kDa nuclear phosphoprotein."; RL J. Biol. Chem. 271:33693-33697(1996). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=9050866; DOI=10.1073/pnas.94.5.1840; RA Brown K.D., Ziv Y., Sadanandan S.N., Chessa L., Collins F.S., Shiloh Y., RA Tagle D.A.; RT "The ataxia-telangiectasia gene product, a constitutively expressed nuclear RT protein that is not up-regulated following genome damage."; RL Proc. Natl. Acad. Sci. U.S.A. 94:1840-1845(1997). RN [14] RP SUBCELLULAR LOCATION, AND VARIANTS 2546-SER--ILE-2548 DEL AND TYR-2824. RX PubMed=9150358; DOI=10.1038/sj.onc.1201037; RA Watters D., Khanna K.K., Beamish H., Birrell G., Spring K., Kedar P., RA Gatei M., Stenzel D., Hobson K., Kozlov S., Zhang N., Farrell A., RA Ramsay J., Gatti R.A., Lavin M.F.; RT "Cellular localisation of the ataxia-telangiectasia (ATM) gene product and RT discrimination between mutated and normal forms."; RL Oncogene 14:1911-1921(1997). RN [15] RP CATALYTIC ACTIVITY. RX PubMed=8988033; RA Jung M., Kondratyev A., Lee S.A., Dimtchev A., Dritschilo A.; RT "ATM gene product phosphorylates I kappa B-alpha."; RL Cancer Res. 57:24-27(1997). RN [16] RP INTERACTION WITH ABL1. RX PubMed=9168117; DOI=10.1038/387520a0; RA Shafman T., Khanna K.K., Kedar P., Spring K., Kozlov S., Yen T., Hobson K., RA Gatei M., Zhang N., Watters D., Egerton M., Shiloh Y., Kharbanda S., RA Kufe D., Lavin M.F.; RT "Interaction between ATM protein and c-Abl in response to DNA damage."; RL Nature 387:520-523(1997). RN [17] RP ACTIVITY REGULATION. RX PubMed=9766667; RA Sarkaria J.N., Tibbetts R.S., Busby E.C., Kennedy A.P., Hill D.E., RA Abraham R.T.; RT "Inhibition of phosphoinositide 3-kinase related kinases by the RT radiosensitizing agent wortmannin."; RL Cancer Res. 58:4375-4382(1998). RN [18] RP FUNCTION, INTERACTION WITH TP53, AND CATALYTIC ACTIVITY. RX PubMed=9843217; DOI=10.1038/3882; RA Khanna K.K., Keating K.E., Kozlov S., Scott S., Gatei M., Hobson K., RA Taya Y., Gabrielli B., Chan D., Lees-Miller S.P., Lavin M.F.; RT "ATM associates with and phosphorylates p53: mapping the region of RT interaction."; RL Nat. Genet. 20:398-400(1998). RN [19] RP INTERACTION WITH BETA-ADAPTIN. RX PubMed=9707615; DOI=10.1073/pnas.95.17.10146; RA Lim D.-S., Kirsch D.G., Canman C.E., Ahn J.-H., Ziv Y., Newman L.S., RA Darnell R.B., Shiloh Y., Kastan M.B.; RT "ATM binds to beta-adaptin in cytoplasmic vesicles."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10146-10151(1998). RN [20] RP FUNCTION IN PHOSPHORYLATION OF TP53. RX PubMed=9733514; DOI=10.1126/science.281.5383.1674; RA Banin S., Moyal L., Shieh S.-Y., Taya Y., Anderson C.W., Chessa L., RA Smorodinsky N.I., Prives C., Reiss Y., Shiloh Y., Ziv Y.; RT "Enhanced phosphorylation of p53 by ATM in response to DNA damage."; RL Science 281:1674-1677(1998). RN [21] RP FUNCTION IN PHOSPHORYLATION OF TP53, AND MUTAGENESIS OF ASP-2870 AND RP ASN-2875. RX PubMed=9733515; DOI=10.1126/science.281.5383.1677; RA Canman C.E., Lim D.-S., Cimprich K.A., Taya Y., Tamai K., Sakaguchi K., RA Appella E., Kastan M.B., Siliciano J.D.; RT "Activation of the ATM kinase by ionizing radiation and phosphorylation of RT p53."; RL Science 281:1677-1679(1998). RN [22] RP DNA-BINDING. RX PubMed=10500142; DOI=10.1073/pnas.96.20.11134; RA Smith G.C.M., Cary R.B., Lakin N.D., Hann B.C., Teo S.-H., Chen D.J., RA Jackson S.P.; RT "Purification and DNA binding properties of the ataxia-telangiectasia gene RT product ATM."; RL Proc. Natl. Acad. Sci. U.S.A. 96:11134-11139(1999). RN [23] RP FUNCTION IN PHOSPHORYLATION OF BRCA1. RX PubMed=10550055; DOI=10.1126/science.286.5442.1162; RA Cortez D., Wang Y., Qin J., Elledge S.J.; RT "Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage RT response to double-strand breaks."; RL Science 286:1162-1166(1999). RN [24] RP IDENTIFICATION OF ATM AS MEMBER OF BASC. RX PubMed=10783165; RA Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.; RT "BASC, a super complex of BRCA1-associated proteins involved in the RT recognition and repair of aberrant DNA structures."; RL Genes Dev. 14:927-939(2000). RN [25] RP FUNCTION IN PHOSPHORYLATION OF NBN. RX PubMed=10766245; DOI=10.1038/35007091; RA Lim D.-S., Kim S.-T., Xu B., Maser R.S., Lin J., Petrini J.H.J., RA Kastan M.B.; RT "ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway."; RL Nature 404:613-617(2000). RN [26] RP FUNCTION IN PHOSPHORYLATION OF NBN. RX PubMed=10839545; DOI=10.1038/35013089; RA Wu X., Ranganathan V., Weisman D.S., Heine W.F., Ciccone D.N., RA O'Neill T.B., Crick K.E., Pierce K.A., Lane W.S., Rathbun G., RA Livingston D.M., Weaver D.T.; RT "ATM phosphorylation of Nijmegen breakage syndrome protein is required in a RT DNA damage response."; RL Nature 405:477-482(2000). RN [27] RP FUNCTION IN PHOSPHORYLATION OF CTIP. RX PubMed=10910365; DOI=10.1038/35018134; RA Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y., Lee E.Y.-H.P., RA Lee W.-H.; RT "Functional link of BRCA1 and ataxia telangiectasia gene product in DNA RT damage response."; RL Nature 406:210-215(2000). RN [28] RP FUNCTION IN PHOSPHORYLATION OF NBN. RX PubMed=10802669; DOI=10.1038/75508; RA Gatei M., Young D., Cerosaletti K.M., Desai-Mehta A., Spring K., Kozlov S., RA Lavin M.F., Gatti R.A., Concannon P., Khanna K.K.; RT "ATM-dependent phosphorylation of nibrin in response to radiation RT exposure."; RL Nat. Genet. 25:115-119(2000). RN [29] RP FUNCTION IN PHOSPHORYLATION OF CHEK2. RX PubMed=10973490; DOI=10.1073/pnas.190030497; RA Matsuoka S., Rotman G., Ogawa A., Shiloh Y., Tamai K., Elledge S.J.; RT "Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 97:10389-10394(2000). RN [30] RP FUNCTION IN PHOSPHORYLATION OF TERF1. RX PubMed=11375976; DOI=10.1074/jbc.m011534200; RA Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.; RT "Telomeric protein Pin2/TRF1 as an important ATM target in response to RT double strand DNA breaks."; RL J. Biol. Chem. 276:29282-29291(2001). RN [31] RP INTERACTION WITH RAD17. RX PubMed=11418864; DOI=10.1038/35082110; RA Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A., RA Chen S.M., Abraham R.T., Wang X.-F.; RT "ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic RT stress responses."; RL Nature 411:969-974(2001). RN [32] RP FUNCTION IN PHOSPHORYLATION OF FANCD2. RX PubMed=12086603; DOI=10.1016/s0092-8674(02)00747-x; RA Taniguchi T., Garcia-Higuera I., Xu B., Andreassen P.R., Gregory R.C., RA Kim S.-T., Lane W.S., Kastan M.B., D'Andrea A.D.; RT "Convergence of the Fanconi anemia and ataxia telangiectasia signaling RT pathways."; RL Cell 109:459-472(2002). RN [33] RP PHOSPHORYLATION BY NUAK1. RX PubMed=12409306; DOI=10.1074/jbc.m206025200; RA Suzuki A., Kusakai G., Kishimoto A., Lu J., Ogura T., Lavin M.F., Esumi H.; RT "Identification of a novel protein kinase mediating Akt survival signaling RT to the ATM protein."; RL J. Biol. Chem. 278:48-53(2003). RN [34] RP PHOSPHORYLATION AT SER-1981, SUBUNIT, FUNCTION, AND MUTAGENESIS OF RP SER-1981. RX PubMed=12556884; DOI=10.1038/nature01368; RA Bakkenist C.J., Kastan M.B.; RT "DNA damage activates ATM through intermolecular autophosphorylation and RT dimer dissociation."; RL Nature 421:499-506(2003). RN [35] RP FUNCTION IN DNA DAMAGE RESPONSE, AND INTERACTION WITH PPP5C. RX PubMed=14871926; DOI=10.1101/gad.1176004; RA Ali A., Zhang J., Bao S., Liu I., Otterness D., Dean N.M., Abraham R.T., RA Wang X.F.; RT "Requirement of protein phosphatase 5 in DNA-damage-induced ATM RT activation."; RL Genes Dev. 18:249-254(2004). RN [36] RP FUNCTION IN PHOSPHORYLATION OF DCLRE1C, AND INTERACTION WITH DCLRE1C. RX PubMed=15456891; DOI=10.1128/mcb.24.20.9207-9220.2004; RA Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., RA Legerski R.J.; RT "Artemis is a phosphorylation target of ATM and ATR and is involved in the RT G2/M DNA damage checkpoint response."; RL Mol. Cell. Biol. 24:9207-9220(2004). RN [37] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15448695; DOI=10.1038/ncb1170; RA Demonacos C., Krstic-Demonacos M., Smith L., Xu D., O'Connor D.P., RA Jansson M., La Thangue N.B.; RT "A new effector pathway links ATM kinase with the DNA damage response."; RL Nat. Cell Biol. 6:968-976(2004). RN [38] RP INTERACTION WITH EEF1E1. RX PubMed=15680327; DOI=10.1016/j.cell.2004.11.054; RA Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H., RA Choi Y.H., Choi D., Lee K.S., Kim S.; RT "The haploinsufficient tumor suppressor p18 upregulates p53 via RT interactions with ATM/ATR."; RL Cell 120:209-221(2005). RN [39] RP FUNCTION. RX PubMed=15916964; DOI=10.1016/j.molcel.2005.04.015; RA Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., Ronai Z.; RT "ATM-dependent phosphorylation of ATF2 is required for the DNA damage RT response."; RL Mol. Cell 18:577-587(2005). RN [40] RP INTERACTION WITH KAT8. RX PubMed=15923642; DOI=10.1128/mcb.25.12.5292-5305.2005; RA Gupta A., Sharma G.G., Young C.S.H., Agarwal M., Smith E.R., Paull T.T., RA Lucchesi J.C., Khanna K.K., Ludwig T., Pandita T.K.; RT "Involvement of human MOF in ATM function."; RL Mol. Cell. Biol. 25:5292-5305(2005). RN [41] RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY. RX PubMed=16086026; DOI=10.1038/nsmb972; RA Kaygun H., Marzluff W.F.; RT "Regulated degradation of replication-dependent histone mRNAs requires both RT ATR and Upf1."; RL Nat. Struct. Mol. Biol. 12:794-800(2005). RN [42] RP INTERACTION WITH HTATIP, PHOSPHORYLATION AT SER-1981, AND ACETYLATION. RX PubMed=16141325; DOI=10.1073/pnas.0504211102; RA Sun Y., Jiang X., Chen S., Fernandes N., Price B.D.; RT "A role for the Tip60 histone acetyltransferase in the acetylation and RT activation of ATM."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13182-13187(2005). RN [43] RP PHOSPHORYLATION AT SER-367; SER-1893 AND SER-1981, FUNCTION, CATALYTIC RP ACTIVITY, MUTAGENESIS OF SER-367; SER-1893 AND SER-1981, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=16858402; DOI=10.1038/sj.emboj.7601231; RA Kozlov S.V., Graham M.E., Peng C., Chen P., Robinson P.J., Lavin M.F.; RT "Involvement of novel autophosphorylation sites in ATM activation."; RL EMBO J. 25:3504-3514(2006). RN [44] RP INTERACTION WITH ATMIN. RX PubMed=17525732; DOI=10.1038/sj.emboj.7601733; RA Kanu N., Behrens A.; RT "ATMIN defines an NBS1-independent pathway of ATM signalling."; RL EMBO J. 26:2933-2941(2007). RN [45] RP ACETYLATION AT LYS-3016, FUNCTION, AND MUTAGENESIS OF LYS-3016 AND RP LYS-3018. RX PubMed=17923702; DOI=10.1128/mcb.01382-07; RA Sun Y., Xu Y., Roy K., Price B.D.; RT "DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase RT activity."; RL Mol. Cell. Biol. 27:8502-8509(2007). RN [46] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1981 AND SER-1983, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [47] RP INTERACTION WITH CEP164. RX PubMed=18283122; DOI=10.1101/gad.1627708; RA Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.; RT "Cep164 is a mediator protein required for the maintenance of genomic RT stability through modulation of MDC1, RPA, and CHK1."; RL Genes Dev. 22:587-600(2008). RN [48] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [49] RP INTERACTION WITH NABP2. RX PubMed=18449195; DOI=10.1038/nature06883; RA Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K., RA Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J., Pandita R.K., RA Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T., Pandita T.K., RA White M.F., Khanna K.K.; RT "Single-stranded DNA-binding protein hSSB1 is critical for genomic RT stability."; RL Nature 453:677-681(2008). RN [50] RP INTERACTION WITH DDX1. RX PubMed=18710941; DOI=10.1128/mcb.01053-08; RA Li L., Monckton E.A., Godbout R.; RT "A role for DEAD box 1 at DNA double-strand breaks."; RL Mol. Cell. Biol. 28:6413-6425(2008). RN [51] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2996, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [52] RP FUNCTION AS DYRK2 KINASE. RX PubMed=19965871; DOI=10.1074/jbc.m109.042341; RA Taira N., Yamamoto H., Yamaguchi T., Miki Y., Yoshida K.; RT "ATM augments nuclear stabilization of DYRK2 by inhibiting MDM2 in the RT apoptotic response to DNA damage."; RL J. Biol. Chem. 285:4909-4919(2010). RN [53] RP INTERACTION WITH TTI1. RX PubMed=20810650; DOI=10.1101/gad.1934210; RA Hurov K.E., Cotta-Ramusino C., Elledge S.J.; RT "A genetic screen identifies the Triple T complex required for DNA damage RT signaling and ATM and ATR stability."; RL Genes Dev. 24:1939-1950(2010). RN [54] RP INTERACTION WITH TELO2. RX PubMed=20801936; DOI=10.1101/gad.1956410; RA Takai H., Xie Y., de Lange T., Pavletich N.P.; RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and RT ATR complexes."; RL Genes Dev. 24:2019-2030(2010). RN [55] RP INTERACTION WITH TELO2 AND TTI1. RX PubMed=20427287; DOI=10.1074/jbc.m110.121699; RA Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., RA Iemura S., Natsume T., Mizushima N.; RT "Tti1 and Tel2 are critical factors in mammalian target of rapamycin RT complex assembly."; RL J. Biol. Chem. 285:20109-20116(2010). RN [56] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [57] RP PHOSPHORYLATION AT SER-1981. RX PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005; RA Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y., RA You H.J.; RT "Protein phosphatase 5 is necessary for ATR-mediated DNA repair."; RL Biochem. Biophys. Res. Commun. 404:476-481(2011). RN [58] RP INTERACTION WITH BRAT1. RX PubMed=22977523; DOI=10.3892/etm.2011.232; RA So E.Y., Ouchi T.; RT "Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK RT catalytic subunit."; RL Exp. Ther. Med. 2:443-447(2011). RN [59] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [60] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [61] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [62] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PEX5, RP AND MUTAGENESIS OF ARG-3047. RX PubMed=26344566; DOI=10.1038/ncb3230; RA Zhang J., Tripathi D.N., Jing J., Alexander A., Kim J., Powell R.T., RA Dere R., Tait-Mulder J., Lee J.H., Paull T.T., Pandita R.K., Charaka V.K., RA Pandita T.K., Kastan M.B., Walker C.L.; RT "ATM functions at the peroxisome to induce pexophagy in response to ROS."; RL Nat. Cell Biol. 17:1259-1269(2015). RN [63] RP FUNCTION IN PHOSPHORYLATION OF FBXW7. RX PubMed=26774286; DOI=10.1016/j.molcel.2015.12.010; RA Zhang Q., Karnak D., Tan M., Lawrence T.S., Morgan M.A., Sun Y.; RT "FBXW7 facilitates nonhomologous end-joining via K63-linked RT polyubiquitylation of XRCC4."; RL Mol. Cell 61:419-433(2016). RN [64] RP FUNCTION. RX PubMed=29203878; DOI=10.1038/s41467-017-02114-x; RA Batenburg N.L., Walker J.R., Noordermeer S.M., Moatti N., Durocher D., RA Zhu X.D.; RT "ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair RT pathway choice."; RL Nat. Commun. 8:1921-1921(2017). RN [65] RP FUNCTION. RX PubMed=30612738; DOI=10.1016/j.cell.2018.11.024; RA Jachimowicz R.D., Beleggia F., Isensee J., Velpula B.B., Goergens J., RA Bustos M.A., Doll M.A., Shenoy A., Checa-Rodriguez C., Wiederstein J.L., RA Baranes-Bachar K., Bartenhagen C., Hertwig F., Teper N., Nishi T., RA Schmitt A., Distelmaier F., Luedecke H.J., Albrecht B., Krueger M., RA Schumacher B., Geiger T., Hoon D.S.B., Huertas P., Fischer M., Hucho T., RA Peifer M., Ziv Y., Reinhardt H.C., Wieczorek D., Shiloh Y.; RT "UBQLN4 represses homologous recombination and is overexpressed in RT aggressive tumors."; RL Cell 0:0-0(2019). RN [66] RP FUNCTION IN PHOSPHORYLATION OF UFL1, AND CATALYTIC ACTIVITY. RX PubMed=30886146; DOI=10.1038/s41467-019-09175-0; RA Qin B., Yu J., Nowsheen S., Wang M., Tu X., Liu T., Li H., Wang L., Lou Z.; RT "UFL1 promotes histone H4 ufmylation and ATM activation."; RL Nat. Commun. 10:1242-1242(2019). RN [67] RP ACETYLATION AT LYS-3016, PHOSPHORYLATION AT SER-1981, AND MUTAGENESIS OF RP LYS-3016. RX PubMed=30944854; DOI=10.1126/sciadv.aav1118; RA Tang M., Li Z., Zhang C., Lu X., Tu B., Cao Z., Li Y., Chen Y., Jiang L., RA Wang H., Wang L., Wang J., Liu B., Xu X., Wang H., Zhu W.G.; RT "SIRT7-mediated ATM deacetylation is essential for its deactivation and DNA RT damage repair."; RL Sci. Adv. 5:EAAV1118-EAAV1118(2019). RN [68] {ECO:0007744|PDB:5NP0, ECO:0007744|PDB:5NP1} RP STRUCTURE BY ELECTRON MICROSCOPY (5.70 ANGSTROMS), CATALYTIC ACTIVITY, AND RP SUBUNIT. RX PubMed=28508083; DOI=10.1126/sciadv.1700933; RA Baretic D., Pollard H.K., Fisher D.I., Johnson C.M., Santhanam B., RA Truman C.M., Kouba T., Fersht A.R., Phillips C., Williams R.L.; RT "Structures of closed and open conformations of dimeric human ATM."; RL Sci. Adv. 3:E1700933-E1700933(2017). RN [69] RP VARIANTS GLY-2424; 2546-SER--ILE-2548 DEL AND CYS-2827. RX PubMed=8755918; RA McConville C.M., Stankovic T., Byrd P.J., McGuire G.M., Yao Q.-Y., RA Lennox G.G., Taylor A.M.R.; RT "Mutations associated with variant phenotypes in ataxia-telangiectasia."; RL Am. J. Hum. Genet. 59:320-330(1996). RN [70] RP VARIANT AT 2546-SER--ILE-2548 DEL, AND VARIANT ILE-2438. RX PubMed=8808599; RA Wright J., Teraoka S., Onengut S., Tolun A., Gatti R.A., Ochs H.D., RA Concannon P.; RT "A high frequency of distinct ATM gene mutations in ataxia- RT telangiectasia."; RL Am. J. Hum. Genet. 59:839-846(1996). RN [71] RP VARIANTS 705-TYR--SER-707 DELINS PHE-ILE-PRO AND 2546-SER--ILE-2548 DEL, RP AND VARIANTS CYS-49; LEU-858; ARG-1054; PHE-1420 AND ARG-1691. RX PubMed=8797579; RA Vorechovsky I., Luo L., Lindblom A., Negrini M., Webster A.D.B., RA Croce C.M., Hammarstroem L.; RT "ATM mutations in cancer families."; RL Cancer Res. 56:4130-4133(1996). RN [72] RP VARIANT AT 705-TYR--SER-707 DELINS PHE-ILE-PRO, AND VARIANTS LEU-858 AND RP ARG-1054. RX PubMed=9043869; DOI=10.1159/000472231; RA Vorechovsky I., Luo L., Prudente S., Chessa L., Russo G., Kanariou M., RA James M.R., Negrini M., Webster A.D.B., Hammarstroem L.; RT "Exon-scanning mutation analysis of the ATM gene in patients with ataxia- RT telangiectasia."; RL Eur. J. Hum. Genet. 4:352-355(1996). RN [73] RP VARIANT AT ARG-2867. RX PubMed=8698354; DOI=10.1007/s004390050202; RA Baumer A., Bernthaler U., Wolz W., Hoehn H., Schindler D.; RT "New mutations in the ataxia telangiectasia gene."; RL Hum. Genet. 98:246-249(1996). RN [74] RP VARIANTS 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860 DEL AND RP GLY-2904. RX PubMed=8845835; DOI=10.1093/hmg/5.4.433; RA Gilad S., Khosravi R., Shkedy D., Uziel T., Ziv Y., Savitsky K., Rotman G., RA Smith S., Chessa L., Jorgensen T.J., Harnik R., Frydman M., Sanal O., RA Portnoi S., Goldwicz Z., Jaspers N.G.J., Gatti R.A., Lenoir G., Lavin M.F., RA Tatsumi K., Wegner R.-D., Shiloh Y., Bar-Shira A.; RT "Predominance of null mutations in ataxia-telangiectasia."; RL Hum. Mol. Genet. 5:433-439(1996). RN [75] RP POSSIBLE INVOLVEMENT IN TPLL AND BNHL, AND VARIANTS VAL-1040; THR-1407; RP SER-1463; HIS-1682; HIS-1910; LYS-2164; SER-2396; GLY-2424; PRO-2442; RP 2546-SER--ILE-2548 DEL; ALA-2695; ARG-2722; VAL-2725; LEU-2732; LYS-2810 RP DEL; CYS-2832 AND 2871-ARG-HIS-2872 DELINS SER AND VAL-2890. RX PubMed=9288106; DOI=10.1038/ng0997-96; RA Vorechovsky I., Luo L., Dyer M.J.S., Catovsky D., Amlot P.L., Yaxley J.C., RA Foroni L., Hammarstroem L., Webster A.D.B., Yuille M.A.R.; RT "Clustering of missense mutations in the ataxia-telangiectasia gene in a RT sporadic T-cell leukaemia."; RL Nat. Genet. 17:96-99(1997). RN [76] RP POSSIBLE INVOLVEMENT IN TPLL, AND VARIANTS GLY-2725; PRO-3006 AND CYS-3008. RX PubMed=9334731; DOI=10.1038/nm1097-1155; RA Stilgenbauer S., Schaffner C., Litterst A., Liebisch P., Gilad S., RA Bar-Shira A., James M.R., Lichter P., Doehner H.; RT "Biallelic mutations in the ATM gene in T-prolymphocytic leukemia."; RL Nat. Med. 3:1155-1159(1997). RN [77] RP VARIANT AT CYS-2832. RX PubMed=9443866; DOI=10.1086/301673; RA Telatar M., Teraoka S., Wang Z., Chun H.H., Liang T., Castellvi-Bel S., RA Udar N., Boerresen-Dale A.-L., Chessa L., Bernatowska-Matuszkiewicz E., RA Porras O., Watanabe M., Junker A., Concannon P., Gatti R.A.; RT "Ataxia-telangiectasia: identification and detection of founder-effect RT mutations in the ATM gene in ethnic populations."; RL Am. J. Hum. Genet. 62:86-97(1998). RN [78] RP POSSIBLE INVOLVEMENT IN TALL, AND VARIANTS AT LEU-292; ASP-768; GLN-1001; RP ARG-1691; ILE-1743; GLY-2424; 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 RP DEL; ASP-2554; GLY-2668 AND CYS-2827. RX PubMed=9463314; DOI=10.1086/301706; RA Stankovic T., Kidd A.M.J., Sutcliffe A., McGuire G.M., Robinson P., RA Weber P., Bedenham T., Bradwell A.R., Easton D.F., Lennox G.G., Haites N., RA Byrd P.J., Taylor A.M.R.; RT "ATM mutations and phenotypes in ataxia-telangiectasia families in the RT British Isles: expression of mutant ATM and the risk of leukemia, lymphoma, RT and breast cancer."; RL Am. J. Hum. Genet. 62:334-345(1998). RN [79] RP VARIANT AT 1812-ALA-PHE-1813 DELINS VAL. RX PubMed=9497252; DOI=10.1086/301755; RA Gilad S., Chessa L., Khosravi R., Russell P., Galanty Y., Piane M., RA Gatti R.A., Jorgensen T.J., Shiloh Y., Bar-Shira A.; RT "Genotype-phenotype relationships in ataxia-telangiectasia and variants."; RL Am. J. Hum. Genet. 62:551-561(1998). RN [80] RP VARIANT AT PRO-2656. RX PubMed=9450874; RX DOI=10.1002/(sici)1096-8628(19980113)75:2<141::aid-ajmg4>3.3.co;2-8; RA Toyoshima M., Hara T., Zhang H., Yamamoto T., Akaboshi S., Nanba E., RA Ohno K., Hori N., Sato K., Takeshita K.; RT "Ataxia-telangiectasia without immunodeficiency: novel point mutations RT within and adjacent to the phosphatidylinositol 3-kinase-like domain."; RL Am. J. Med. Genet. 75:141-144(1998). RN [81] RP VARIANT TPLL GLY-2486. RX PubMed=9573030; RA Stoppa-Lyonnet D., Soulier J., Lauge A., Dastot H., Garand R., Sigaux F., RA Stern M.-H.; RT "Inactivation of the ATM gene in T-cell prolymphocytic leukemias."; RL Blood 91:3920-3926(1998). RN [82] RP VARIANTS 2855-SER-VAL-2856 DELINS ARG-ILE AND CYS-3008, AND VARIANT RP VAL-1853. RX PubMed=9872980; DOI=10.1101/gr.8.12.1245; RA Hacia J.G., Sun B., Hunt N., Edgemon K., Mosbrook D., Robbins C., RA Fodor S.P.A., Tagle D.A., Collins F.S.; RT "Strategies for mutational analysis of the large multiexon ATM gene using RT high-density oligonucleotide arrays."; RL Genome Res. 8:1245-1258(1998). RN [83] RP VARIANT AT 2625-ASP-ALA-2626 DELINS GLU-PRO. RX PubMed=9521587; DOI=10.1007/s004390050675; RA van Belzen M.J., Hiel J.A.P., Weemaes C.M.R., Gabreeels F.J.M., RA van Engelen B.G.M., Smeets D.F.C.M., van den Heuvel L.P.W.J.; RT "A double missense mutation in the ATM gene of a Dutch family with ataxia RT telangiectasia."; RL Hum. Genet. 102:187-191(1998). RN [84] RP VARIANT AT LEU-2829, AND VARIANTS GLU-126; ASP-514 AND ASN-1853. RX PubMed=9711876; RX DOI=10.1002/(sici)1098-1004(1998)12:3<186::aid-humu6>3.0.co;2-f; RA Sasaki T., Tian H., Kukita Y., Inazuka M., Tahira T., Imai T., Yamauchi M., RA Saito T., Hori T., Hashimoto-Tamaoki T., Komatsu K., Nikaido O., RA Hayashi K.; RT "ATM mutations in patients with ataxia telangiectasia screened by a RT hierarchical strategy."; RL Hum. Mutat. 12:186-195(1998). RN [85] RP VARIANTS AT LEU-858; ARG-1054; ASP-1091 AND ARG-1566. RX PubMed=9792409; RX DOI=10.1002/(sici)1098-1004(1998)12:5<330::aid-humu6>3.0.co;2-h; RA Broeks A., de Klein A., Floore A.N., Muijtjens M., Kleijer W.J., RA Jaspers N.G.J., van 't Veer L.J.; RT "ATM germline mutations in classical ataxia-telangiectasia patients in the RT Dutch population."; RL Hum. Mutat. 12:330-337(1998). RN [86] RP VARIANTS AT ARG-2491 AND GLY-2909. RX PubMed=9792410; RX DOI=10.1002/(sici)1098-1004(1998)12:5<338::aid-humu7>3.0.co;2-9; RA Fukao T., Song X.-Q., Yoshida T., Tashita H., Kaneko H., Teramoto T., RA Inoue R., Katamura K., Mayumi M., Hiratani M., Taniguchi N., Arai J., RA Wakiguchi H., Bar-Shira A., Shiloh Y., Kondo N.; RT "Ataxia-telangiectasia in the Japanese population: identification of RT R1917X, W2491R, R2909G, IVS33+2T-->A, and 7883del5, the latter two being RT relatively common mutations."; RL Hum. Mutat. 12:338-343(1998). RN [87] RP VARIANTS TPLL GLY-2139; VAL-2890 AND CYS-3008. RX PubMed=9488043; DOI=10.1038/sj.onc.1201603; RA Yuille M.A.R., Coignet L.J.A., Abraham S.M., Yaqub F., Luo L., Matutes E., RA Brito-Babapulle V., Vorechovsky I., Dyer M.J.S., Catovsky D.; RT "ATM is usually rearranged in T-cell prolymphocytic leukaemia."; RL Oncogene 16:789-796(1998). RN [88] RP ERRATUM OF PUBMED:9488043. RA Yuille M.A.R., Coignet L.J.A., Abraham S.M., Yaqub F., Luo L., Matutes E., RA Brito-Babapulle V., Vorechovsky I., Dyer M.J.S., Catovsky D.; RL Oncogene 16:2955-2955(1998). RN [89] RP POSSIBLE INVOLVEMENT IN BCLL AND MCL, AND VARIANTS ASN-1853; VAL-1853; RP ARG-1953; LYS-2418 INS; PRO-2420; GLY-2423; HIS-3008 AND ASN-3018. RX PubMed=10397742; RA Schaffner C., Stilgenbauer S., Rappold G.A., Doehner H., Lichter P.; RT "Somatic ATM mutations indicate a pathogenic role of ATM in B-cell chronic RT lymphocytic leukemia."; RL Blood 94:748-753(1999). RN [90] RP POSSIBLE INVOLVEMENT IN BCLL, AND VARIANTS CYS-332; ARG-1691 AND GLY-2424. RX PubMed=9892178; RA Bullrich F., Rasio D., Kitada S., Starostik P., Kipps T., Keating M., RA Albitar M., Reed J.C., Croce C.M.; RT "ATM mutations in B-cell chronic lymphocytic leukemia."; RL Cancer Res. 59:24-27(1999). RN [91] RP VARIANT AT PRO-1465. RX PubMed=10234507; DOI=10.1038/sj.ejhg.5200288; RA Izatt L., Vessey C., Hodgson S.V., Solomon E.; RT "Rapid and efficient ATM mutation detection by fluorescent chemical RT cleavage of mismatch: identification of four novel mutations."; RL Eur. J. Hum. Genet. 7:310-320(1999). RN [92] RP VARIANTS CYS-49; LEU-182; PRO-707; LEU-858; PHE-1420; ALA-1570; ASN-1853 RP AND SER-2765. RX PubMed=10534763; RX DOI=10.1002/(sici)1098-2264(199912)26:4<286::aid-gcc2>3.3.co;2-o; RA Izatt L., Greenman J., Hodgson S.V., Ellis D., Watts S., Scott G., RA Jacobs C., Liebmann R., Zvelebil M.J., Mathew C., Solomon E.; RT "Identification of germline missense mutations and rare allelic variants in RT the ATM gene in early-onset breast cancer."; RL Genes Chromosomes Cancer 26:286-294(1999). RN [93] RP VARIANTS AT SER-570; CYS-785; GLY-1913; GLY-2016; ASP-2067; CYS-2227; RP ASP-2470; VAL-2662 DEL; PRO-2849 AND ARG-2867, AND VARIANTS CYS-49; RP LEU-858; ARG-1054; ASN-1853 AND VAL-1853. RX PubMed=9887333; DOI=10.1093/hmg/8.1.69; RA Sandoval N., Platzer M., Rosenthal A., Doerk T., Bendix R., Skawran B., RA Stuhrmann M., Wegner R.-D., Sperling K., Banin S., Shiloh Y., Baumer A., RA Bernthaler U., Sennefelder H., Brohm M., Weber B.H.F., Schindler D.; RT "Characterization of ATM gene mutations in 66 ataxia telangiectasia RT families."; RL Hum. Mol. Genet. 8:69-79(1999). RN [94] RP VARIANTS AT CYS-49; 375-GLN--VAL-3056 DEL; 1466-ARG--VAL-3056 DEL; RP 1730-ARG--VAL-3056 DEL; GLY-2016; 2224-MET--ARG-2227 DELINS ILE-SER; RP 2246-CYS--THR-2252 DELINS HIS; VAL-2664 DEL; VAL-2726; 2849-ARG--VAL-3056 RP DEL AND ARG-2855. RX PubMed=10425038; RX DOI=10.1002/(sici)1098-1004(1999)14:2<156::aid-humu7>3.0.co;2-e; RA Castellvi-Bel S., Sheikhavandi S., Telatar M., Tai L.-Q., Hwang M.J., RA Wang Z., Yang Z., Cheng R., Gatti R.A.; RT "New mutations, polymorphisms, and rare variants in the ATM gene detected RT by a novel SSCP strategy."; RL Hum. Mutat. 14:156-162(1999). RN [95] RP POSSIBLE INVOLVEMENT IN BCLL, AND VARIANTS THR-350; THR-352; ARG-1054; RP THR-2274 AND ALA-2695. RX PubMed=10023947; DOI=10.1016/s0140-6736(98)10117-4; RA Stankovic T., Weber P., Stewart G., Bedenham T., Murray J., Byrd P.J., RA Moss P.A.H., Taylor A.M.R.; RT "Inactivation of ataxia telangiectasia mutated gene in B-cell chronic RT lymphocytic leukaemia."; RL Lancet 353:26-29(1999). RN [96] RP VARIANT ARG-1054. RX PubMed=10217116; DOI=10.1016/s0140-6736(05)75199-0; RA Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.; RT "Missense mutations at ATM gene and cancer risk."; RL Lancet 353:1276-1276(1999). RN [97] RP ERRATUM OF PUBMED:10217116. RA Vorechovsky I., Luo L., Ortmann E., Steinmann D., Doerk T.; RL Lancet 354:780-780(1999). RN [98] RP VARIANTS AT GLU-224; VAL-323; PRO-1420; CYS-2218; 2546-SER--ILE-2548 DEL; RP GLN-2625; CYS-2832; 2855-SER-VAL-2856 DELINS ARG-ILE AND CYS-3008, AND RP VARIANTS VAL-1853 AND ILE-2438. RX PubMed=10817650; RX DOI=10.1002/(sici)1096-8628(20000529)92:3<170::aid-ajmg3>3.0.co;2-#; RA Li A., Swift M.; RT "Mutations at the ataxia-telangiectasia locus and clinical phenotypes of A- RT T patients."; RL Am. J. Med. Genet. 92:170-177(2000). RN [99] RP VARIANTS AT 35-ARG--VAL-3056 DEL; CYS-49; LEU-292; 393-TRP--VAL-3056 DEL; RP LEU-1082; 1171-GLN--VAL-3056 DEL; 1839-GLN--VAL-3056 DEL; GLU-2063; RP CYS-2227; 2246-CYS--THR-2252 DELINS HIS; 2547-ARG--SER-2549 DEL; GLU-2625 RP AND PRO-2626. RX PubMed=10873394; DOI=10.1006/mgme.2000.2998; RA Becker-Catania S.G., Chen G., Hwang M.J., Wang Z., Sun X., Sanal O., RA Bernatowska-Matuszkiewicz E., Chessa L., Lee E.Y.-H.P., Gatti R.A.; RT "Ataxia-telangiectasia: phenotype/genotype studies of ATM protein RT expression, mutations, and radiosensitivity."; RL Mol. Genet. Metab. 70:122-133(2000). RN [100] RP VARIANTS MCL LYS-2418 INS; GLY-2423 AND CYS-3008. RX PubMed=10706620; DOI=10.1073/pnas.050400997; RA Schaffner C., Idler I., Stilgenbauer S., Doehner H., Lichter P.; RT "Mantle cell lymphoma is characterized by inactivation of the ATM gene."; RL Proc. Natl. Acad. Sci. U.S.A. 97:2773-2778(2000). RN [101] RP VARIANTS TRP-45 AND CYS-49. RX PubMed=11897822; DOI=10.1136/jmg.39.3.192; RA Allinen M., Launonen V., Laake K., Jansen L., Huusko P., Kaeaeriaeinen H., RA Boerresen-Dale A.L., Winqvist R.; RT "ATM mutations in Finnish breast cancer patients."; RL J. Med. Genet. 39:192-196(2002). RN [102] RP VARIANTS [LARGE SCALE ANALYSIS] GLN-23; CYS-49; GLU-126; HIS-140; GLN-250; RP PHE-333; CYS-337; HIS-337; ALA-410; SER-504; ASP-514; TYR-540; VAL-546; RP LEU-582; PRO-707; GLN-848; LEU-858; SER-872; TRP-924; ALA-935; ARG-1054; RP PHE-1179; ILE-1321; TYR-1380; SER-1382; PHE-1420; MET-1469; CYS-1475; RP SER-1650; THR-1739; ASN-1853; VAL-1853; ILE-1916; THR-1945; CYS-1961; RP ASP-1991; PHE-2307; PRO-2332; PHE-2356; LEU-2408; PRO-2442; GLN-2443; RP ARG-2464; ARG-2492; ALA-2666; HIS-2719; ARG-2842 AND ASN-2870. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [103] RP VARIANTS CYS-49; LEU-858; ARG-1054; VAL-1255; ASN-1853; THR-2105; SER-2396 RP AND HIS-2719. RX PubMed=18384426; DOI=10.1111/j.1399-0004.2008.00987.x; RA Brunet J., Gutierrez-Enriquez S., Torres A., Berez V., Sanjose S., RA Galceran J., Izquierdo A., Menendez J.A., Guma J., Borras J.; RT "ATM germline mutations in Spanish early-onset breast cancer patients RT negative for BRCA1/BRCA2 mutations."; RL Clin. Genet. 73:465-473(2008). RN [104] RP FUNCTION, CHARACTERIZATION OF VARIANTS AT LEU-292; PRO-1465; ILE-1743; RP THR-2274; GLY-2424; 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; RP ASP-2554; GLY-2668; CYS-2827; 2855-SER-VAL-2856 DELINS ARG-ILE AND RP CYS-3008, CHARACTERIZATION OF VARIANTS VAL-546; ARG-1054; ILE-1322; RP ARG-1691; CYS-1961 AND SER-2765, VARIANT ILE-1322, AND MUTAGENESIS OF RP LYS-1807; VAL-1941; TYR-2019; GLU-2039; LEU-2338; SER-2394; LEU-2452; RP SER-2685; PRO-2699; ASP-2708 AND GLN-2730. RX PubMed=19431188; DOI=10.1002/humu.21034; RA Barone G., Groom A., Reiman A., Srinivasan V., Byrd P.J., Taylor A.M.; RT "Modeling ATM mutant proteins from missense changes confirms retained RT kinase activity."; RL Hum. Mutat. 30:1222-1230(2009). RN [105] RP VARIANTS ALA-661; PRO-707; LEU-858; TRP-924; ARG-1054; ARG-1691 AND RP VAL-1853. RX PubMed=28202063; DOI=10.1186/s12920-017-0244-7; RA Jalkh N., Chouery E., Haidar Z., Khater C., Atallah D., Ali H., RA Marafie M.J., Al-Mulla M.R., Al-Mulla F., Megarbane A.; RT "Next-generation sequencing in familial breast cancer patients from RT Lebanon."; RL BMC Med. Genomics 10:8-8(2017). RN [106] RP VARIANTS AT VAL-323; PRO-1046; ARG-2023; SER-2068; ASP-2080; HIS-2627; RP LEU-2834 AND ASP-3003, CHARACTERIZATION OF VARIANTS AT VAL-323; PRO-1046; RP ARG-2023; SER-2068; ASP-2080; HIS-2627; LEU-2834 AND ASP-3003, AND RP PHOSPHORYLATION. RX PubMed=27664052; DOI=10.1007/s12017-016-8440-8; RA Carranza D., Vega A.K., Torres-Rusillo S., Montero E., Martinez L.J., RA Santamaria M., Santos J.L., Molina I.J.; RT "Molecular and functional characterization of a cohort of Spanish patients RT with ataxia-telangiectasia."; RL NeuroMolecular Med. 19:161-174(2017). RN [107] RP VARIANTS VAL-68; ILE-341; LEU-597; GLY-699; GLY-759; SER-813; GLY-869; RP ILE-897; ASP-1474; VAL-1488; CYS-1961; ALA-2287; PHE-2307; ARG-2464; RP PRO-2524; THR-2531; GLN-2810; HIS-2832; LEU-2974; ASP-3029 AND LEU-3056. RX PubMed=28726808; DOI=10.1038/gim.2017.85; RA Chaffee K.G., Oberg A.L., McWilliams R.R., Majithia N., Allen B.A., RA Kidd J., Singh N., Hartman A.R., Wenstrup R.J., Petersen G.M.; RT "Prevalence of germ-line mutations in cancer genes among pancreatic cancer RT patients with a positive family history."; RL Genet. Med. 20:119-127(2018). CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint CC signaling upon double strand breaks (DSBs), apoptosis and genotoxic CC stresses such as ionizing ultraviolet A light (UVA), thereby acting as CC a DNA damage sensor (PubMed:9733514, PubMed:10550055, PubMed:10839545, CC PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15456891, CC PubMed:15448695, PubMed:15916964, PubMed:17923702). Recognizes the CC substrate consensus sequence [ST]-Q (PubMed:9733514, PubMed:10550055, CC PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, CC PubMed:15456891, PubMed:15448695, PubMed:15916964, PubMed:17923702). CC Phosphorylates 'Ser-139' of histone variant H2AX at double strand CC breaks (DSBs), thereby regulating DNA damage response mechanism (By CC similarity). Also plays a role in pre-B cell allelic exclusion, a CC process leading to expression of a single immunoglobulin heavy chain CC allele to enforce clonality and monospecific recognition by the B-cell CC antigen receptor (BCR) expressed on individual B-lymphocytes. After the CC introduction of DNA breaks by the RAG complex on one immunoglobulin CC allele, acts by mediating a repositioning of the second allele to CC pericentromeric heterochromatin, preventing accessibility to the RAG CC complex and recombination of the second allele. Also involved in signal CC transduction and cell cycle control. May function as a tumor CC suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates CC DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CTIP, nibrin CC (NBN), TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed:9843217, CC PubMed:9733515, PubMed:10550055, PubMed:10766245, PubMed:10839545, CC PubMed:10910365, PubMed:10802669, PubMed:10973490, PubMed:11375976, CC PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:30612738, CC PubMed:30886146, PubMed:26774286). May play a role in vesicle and/or CC protein transport. Could play a role in T-cell development, gonad and CC neurological function. Plays a role in replication-dependent histone CC mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus CC in response to genotoxic stress prevents its MDM2-mediated CC ubiquitination and subsequent proteasome degradation (PubMed:19965871). CC Phosphorylates ATF2 which stimulates its function in DNA damage CC response (PubMed:15916964). Phosphorylates ERCC6 which is essential for CC its chromatin remodeling activity at DNA double-strand breaks CC (PubMed:29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the CC cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear CC localization (PubMed:15448695). Also involved in pexophagy by mediating CC phosphorylation of PEX5: translocated to peroxisomes in response to CC reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, CC promoting PEX5 ubiquitination and induction of pexophagy CC (PubMed:26344566). {ECO:0000250|UniProtKB:Q62388, CC ECO:0000269|PubMed:10550055, ECO:0000269|PubMed:10766245, CC ECO:0000269|PubMed:10802669, ECO:0000269|PubMed:10839545, CC ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:10973490, CC ECO:0000269|PubMed:11375976, ECO:0000269|PubMed:12086603, CC ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926, CC ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:15456891, CC ECO:0000269|PubMed:15916964, ECO:0000269|PubMed:16086026, CC ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, CC ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:19965871, CC ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:26774286, CC ECO:0000269|PubMed:29203878, ECO:0000269|PubMed:30612738, CC ECO:0000269|PubMed:30886146, ECO:0000269|PubMed:9733514, CC ECO:0000269|PubMed:9733515, ECO:0000269|PubMed:9843217}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:16858402, CC ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:28508083, CC ECO:0000269|PubMed:30886146, ECO:0000269|PubMed:8988033, CC ECO:0000269|PubMed:9843217}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000305|PubMed:15448695}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:28508083, CC ECO:0000269|PubMed:8988033, ECO:0000269|PubMed:9843217}; CC -!- ACTIVITY REGULATION: Inhibited by wortmannin. CC {ECO:0000269|PubMed:9766667}. CC -!- SUBUNIT: Homodimer (PubMed:28508083). Dimers or tetramers in inactive CC state. On DNA damage, autophosphorylation dissociates ATM into monomers CC rendering them catalytically active. Binds p53/TP53, ABL1, BRCA1, CC NBN/nibrin and TERF1. Part of the BRCA1-associated genome surveillance CC complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 CC and the RAD50-MRE11-NBN protein complex. This association could be a CC dynamic process changing throughout the cell cycle and within CC subnuclear domains. Interacts with RAD17; DNA damage promotes the CC association. Interacts with EEF1E1; the interaction, induced on DNA CC damage, up-regulates TP53. Interacts with DCLRE1C, KAT8, KAT5, NABP2, CC ATMIN and CEP164. Interacts with AP2B1 and AP3B2; the interaction CC occurs in cytoplasmic vesicles (By similarity). Interacts with TELO2 CC and TTI1. Interacts with DDX1. Interacts with BRAT1. Interacts with CC CYREN (via XLF motif) (By similarity). Interacts (via microbody CC targeting signal) with PEX5; promoting translocation to peroxisomes in CC response to reactive oxygen species (ROS) (PubMed:26344566). CC {ECO:0000250|UniProtKB:Q62388, ECO:0000269|PubMed:11418864, CC ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:14871926, CC ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15680327, CC ECO:0000269|PubMed:15923642, ECO:0000269|PubMed:16141325, CC ECO:0000269|PubMed:17525732, ECO:0000269|PubMed:18283122, CC ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:18710941, CC ECO:0000269|PubMed:20427287, ECO:0000269|PubMed:20801936, CC ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:22977523, CC ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:28508083, CC ECO:0000269|PubMed:9168117, ECO:0000269|PubMed:9707615, CC ECO:0000269|PubMed:9843217}. CC -!- INTERACTION: CC Q13315; Q9NY61: AATF; NbExp=3; IntAct=EBI-495465, EBI-372428; CC Q13315; P00519: ABL1; NbExp=4; IntAct=EBI-495465, EBI-375543; CC Q13315; O43313: ATMIN; NbExp=5; IntAct=EBI-495465, EBI-7422202; CC Q13315; Q6PJG6: BRAT1; NbExp=3; IntAct=EBI-495465, EBI-10826195; CC Q13315; P62508-3: ESRRG; NbExp=3; IntAct=EBI-495465, EBI-12001340; CC Q13315; Q5XUX0: FBXO31; NbExp=2; IntAct=EBI-495465, EBI-6162477; CC Q13315; Q9Y6K9: IKBKG; NbExp=4; IntAct=EBI-495465, EBI-81279; CC Q13315; Q13007: IL24; NbExp=2; IntAct=EBI-495465, EBI-3915542; CC Q13315; Q14676: MDC1; NbExp=3; IntAct=EBI-495465, EBI-495644; CC Q13315; Q9BQ15: NABP2; NbExp=4; IntAct=EBI-495465, EBI-2120336; CC Q13315; P11245: NAT2; NbExp=2; IntAct=EBI-495465, EBI-9057228; CC Q13315; O60934: NBN; NbExp=2; IntAct=EBI-495465, EBI-494844; CC Q13315; P46531: NOTCH1; NbExp=8; IntAct=EBI-495465, EBI-636374; CC Q13315; Q9BZ95: NSD3; NbExp=3; IntAct=EBI-495465, EBI-3390132; CC Q13315; Q7LG56: RRM2B; NbExp=3; IntAct=EBI-495465, EBI-9009083; CC Q13315; Q9Y4R8: TELO2; NbExp=4; IntAct=EBI-495465, EBI-1043674; CC Q13315; P54274: TERF1; NbExp=3; IntAct=EBI-495465, EBI-710997; CC Q13315; P54274-2: TERF1; NbExp=5; IntAct=EBI-495465, EBI-711018; CC Q13315; Q15554: TERF2; NbExp=2; IntAct=EBI-495465, EBI-706637; CC Q13315; Q12888: TP53BP1; NbExp=2; IntAct=EBI-495465, EBI-396540; CC Q13315; O43156: TTI1; NbExp=5; IntAct=EBI-495465, EBI-1055680; CC Q13315; PRO_0000037577 [P27958]; Xeno; NbExp=3; IntAct=EBI-495465, EBI-6904388; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9050866, CC ECO:0000269|PubMed:9150358}. Cytoplasmic vesicle CC {ECO:0000269|PubMed:9050866, ECO:0000269|PubMed:9150358}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:Q62388}. Peroxisome matrix CC {ECO:0000269|PubMed:26344566}. Note=Primarily nuclear (PubMed:9050866, CC PubMed:9150358). Found also in endocytic vesicles in association with CC beta-adaptin (PubMed:9707615). Translocated to peroxisomes in response CC to reactive oxygen species (ROS) by PEX5 (PubMed:26344566). CC {ECO:0000269|PubMed:26344566, ECO:0000269|PubMed:9050866, CC ECO:0000269|PubMed:9150358, ECO:0000269|PubMed:9707615}. CC -!- TISSUE SPECIFICITY: Found in pancreas, kidney, skeletal muscle, liver, CC lung, placenta, brain, heart, spleen, thymus, testis, ovary, small CC intestine, colon and leukocytes. CC -!- INDUCTION: By ionizing radiation. CC -!- DOMAIN: The FATC domain is required for interaction with KAT5. CC {ECO:0000269|PubMed:16141325}. CC -!- PTM: Phosphorylated by NUAK1/ARK5 (PubMed:12409306). CC Autophosphorylation on Ser-367, Ser-1893, Ser-1981 correlates with DNA CC damage-mediated activation of the kinase (PubMed:12556884, CC PubMed:16141325, PubMed:16858402, PubMed:21144835, PubMed:27664052). CC During the late stages of DNA damage response, dephosphorylated CC following deacetylation by SIRT7, leading to ATM deactivation CC (PubMed:30944854). {ECO:0000269|PubMed:12409306, CC ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:16141325, CC ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:21144835, CC ECO:0000269|PubMed:27664052, ECO:0000269|PubMed:30944854}. CC -!- PTM: Acetylation, on DNA damage, is required for activation of the CC kinase activity, dimer-monomer transition, and subsequent CC autophosphorylation on Ser-1981 (PubMed:12556884, PubMed:16141325, CC PubMed:16858402, PubMed:17923702, PubMed:21144835). Acetylated in vitro CC by KAT5/TIP60 (PubMed:16141325). Deacetylated by SIRT7 during the late CC stages of DNA damage response, promoting ATM dephosphorylation and CC subsequent deactivation (PubMed:30944854). CC {ECO:0000269|PubMed:12556884, ECO:0000269|PubMed:16141325, CC ECO:0000269|PubMed:16858402, ECO:0000269|PubMed:17923702, CC ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:30944854}. CC -!- DISEASE: Ataxia telangiectasia (AT) [MIM:208900]: A rare recessive CC disorder characterized by progressive cerebellar ataxia, dilation of CC the blood vessels in the conjunctiva and eyeballs, immunodeficiency, CC growth retardation and sexual immaturity. Patients have a strong CC predisposition to cancer; about 30% of patients develop tumors, CC particularly lymphomas and leukemias. Cells from affected individuals CC are highly sensitive to damage by ionizing radiation and resistant to CC inhibition of DNA synthesis following irradiation. CC {ECO:0000269|PubMed:10234507, ECO:0000269|PubMed:10425038, CC ECO:0000269|PubMed:10817650, ECO:0000269|PubMed:10873394, CC ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:27664052, CC ECO:0000269|PubMed:7792600, ECO:0000269|PubMed:8589678, CC ECO:0000269|PubMed:8665503, ECO:0000269|PubMed:8698354, CC ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:8789452, CC ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:8808599, CC ECO:0000269|PubMed:8845835, ECO:0000269|PubMed:9043869, CC ECO:0000269|PubMed:9150358, ECO:0000269|PubMed:9443866, CC ECO:0000269|PubMed:9450874, ECO:0000269|PubMed:9463314, CC ECO:0000269|PubMed:9497252, ECO:0000269|PubMed:9521587, CC ECO:0000269|PubMed:9711876, ECO:0000269|PubMed:9792409, CC ECO:0000269|PubMed:9792410, ECO:0000269|PubMed:9872980, CC ECO:0000269|PubMed:9887333}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Note=Defects in ATM may contribute to T-cell acute CC lymphoblastic leukemia (TALL) and T-prolymphocytic leukemia (TPLL). CC TPLL is characterized by a high white blood cell count, with a CC predominance of prolymphocytes, marked splenomegaly, lymphadenopathy, CC skin lesions and serous effusion. The clinical course is highly CC aggressive, with poor response to chemotherapy and short survival time. CC TPLL occurs both in adults as a sporadic disease and in younger AT CC patients. {ECO:0000269|PubMed:9288106, ECO:0000269|PubMed:9334731, CC ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9488043, CC ECO:0000269|PubMed:9573030}. CC -!- DISEASE: Note=Defects in ATM may contribute to B-cell non-Hodgkin CC lymphomas (BNHL), including mantle cell lymphoma (MCL). CC {ECO:0000269|PubMed:10397742, ECO:0000269|PubMed:10706620, CC ECO:0000269|PubMed:9288106}. CC -!- DISEASE: Note=Defects in ATM may contribute to B-cell chronic CC lymphocytic leukemia (BCLL). BCLL is the commonest form of leukemia in CC the elderly. It is characterized by the accumulation of mature CD5+ B- CC lymphocytes, lymphadenopathy, immunodeficiency and bone marrow failure. CC {ECO:0000269|PubMed:10023947, ECO:0000269|PubMed:10397742, CC ECO:0000269|PubMed:9892178}. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA86520.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAA86520.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=AAI37170.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI37170.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=EAW67111.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/123/ATM"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/atm/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ataxia telangiectasia mutated entry; CC URL="https://en.wikipedia.org/wiki/Ataxia_telangiectasia_mutated"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U33841; AAC50289.1; -; mRNA. DR EMBL; U55757; AAB38309.1; -; Genomic_DNA. DR EMBL; U55704; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55705; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55707; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55708; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55709; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55710; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55711; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55712; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55713; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55714; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55715; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55716; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55717; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55718; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55719; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55720; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55721; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55722; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55723; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55724; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55725; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55726; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55727; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55728; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55729; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55730; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55731; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55732; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55733; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55734; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55735; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55736; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55737; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55738; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55739; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55740; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55741; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55742; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55743; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55744; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55745; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55746; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55747; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55748; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55749; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55750; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55751; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55752; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55753; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55754; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55755; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55756; AAB38309.1; JOINED; Genomic_DNA. DR EMBL; U55757; AAB38310.1; -; Genomic_DNA. DR EMBL; U55726; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55727; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55728; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55729; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55730; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55731; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55732; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55733; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55734; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55735; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55736; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55737; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55738; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55739; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55740; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55741; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55742; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55743; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55744; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55745; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55746; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55747; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55748; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55749; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55750; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55751; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55752; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55753; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55754; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55755; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U55756; AAB38310.1; JOINED; Genomic_DNA. DR EMBL; U82828; AAB65827.1; -; Genomic_DNA. DR EMBL; AP001925; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005718; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455499; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67111.1; ALT_SEQ; Genomic_DNA. DR EMBL; X91196; CAA62603.1; -; mRNA. DR EMBL; U67092; AAC51298.1; -; Genomic_DNA. DR EMBL; AY220758; AAO26044.1; -; Genomic_DNA. DR EMBL; U26455; AAA86520.1; ALT_SEQ; mRNA. DR EMBL; BC137169; AAI37170.1; ALT_SEQ; mRNA. DR CCDS; CCDS31669.1; -. DR PIR; A43100; A43100. DR RefSeq; NP_000042.3; NM_000051.3. DR RefSeq; XP_005271618.2; XM_005271561.4. DR RefSeq; XP_005271619.2; XM_005271562.4. DR RefSeq; XP_006718906.1; XM_006718843.3. DR RefSeq; XP_006718908.1; XM_006718845.1. DR RefSeq; XP_011541142.1; XM_011542840.2. DR RefSeq; XP_016873278.1; XM_017017789.1. DR RefSeq; XP_016873279.1; XM_017017790.1. DR PDB; 5NP0; EM; 5.70 A; A/B=1-3056. DR PDB; 5NP1; EM; 5.70 A; A=1-3056. DR PDB; 6HKA; NMR; -; A=3024-3056. DR PDB; 6K9K; EM; 7.82 A; A=1-3056. DR PDB; 6K9L; EM; 4.27 A; A/B=1-3056. DR PDB; 7NI4; EM; 3.00 A; A/B=1-3056. DR PDB; 7NI5; EM; 2.78 A; A/B=1-3056. DR PDB; 7NI6; EM; 2.80 A; A/B=1-3056. DR PDB; 7SIC; EM; 2.51 A; A/B=1-3056. DR PDB; 7SID; EM; 2.53 A; A/C=1-3056. DR PDB; 8OXM; EM; 3.30 A; A/B=1-3056. DR PDB; 8OXO; EM; 3.00 A; A/B=1-3056. DR PDB; 8OXP; EM; 2.60 A; A/B=1-3056. DR PDB; 8OXQ; EM; 2.50 A; A/B=1-3056. DR PDBsum; 5NP0; -. DR PDBsum; 5NP1; -. DR PDBsum; 6HKA; -. DR PDBsum; 6K9K; -. DR PDBsum; 6K9L; -. DR PDBsum; 7NI4; -. DR PDBsum; 7NI5; -. DR PDBsum; 7NI6; -. DR PDBsum; 7SIC; -. DR PDBsum; 7SID; -. DR PDBsum; 8OXM; -. DR PDBsum; 8OXO; -. DR PDBsum; 8OXP; -. DR PDBsum; 8OXQ; -. DR EMDB; EMD-12350; -. DR EMDB; EMD-12351; -. DR EMDB; EMD-12352; -. DR EMDB; EMD-17265; -. DR EMDB; EMD-17266; -. DR EMDB; EMD-17267; -. DR EMDB; EMD-17268; -. DR EMDB; EMD-25140; -. DR EMDB; EMD-25141; -. DR EMDB; EMD-3669; -. DR EMDB; EMD-3672; -. DR EMDB; EMD-9949; -. DR EMDB; EMD-9950; -. DR SMR; Q13315; -. DR BioGRID; 106962; 306. DR CORUM; Q13315; -. DR DIP; DIP-182N; -. DR IntAct; Q13315; 103. DR MINT; Q13315; -. DR STRING; 9606.ENSP00000278616; -. DR BindingDB; Q13315; -. DR ChEMBL; CHEMBL3797; -. DR DrugBank; DB00201; Caffeine. DR GuidetoPHARMACOLOGY; 1934; -. DR GlyCosmos; Q13315; 4 sites, 2 glycans. DR GlyGen; Q13315; 5 sites, 2 O-linked glycans (5 sites). DR iPTMnet; Q13315; -. DR PhosphoSitePlus; Q13315; -. DR BioMuta; ATM; -. DR DMDM; 317373479; -. DR CPTAC; CPTAC-2874; -. DR CPTAC; CPTAC-2875; -. DR CPTAC; CPTAC-2876; -. DR CPTAC; CPTAC-3210; -. DR CPTAC; CPTAC-3211; -. DR CPTAC; CPTAC-3212; -. DR CPTAC; CPTAC-3213; -. DR CPTAC; CPTAC-5976; -. DR CPTAC; CPTAC-5977; -. DR CPTAC; CPTAC-5978; -. DR CPTAC; CPTAC-5979; -. DR CPTAC; CPTAC-912; -. DR CPTAC; CPTAC-913; -. DR EPD; Q13315; -. DR jPOST; Q13315; -. DR MassIVE; Q13315; -. DR MaxQB; Q13315; -. DR PaxDb; 9606-ENSP00000278616; -. DR PeptideAtlas; Q13315; -. DR ProteomicsDB; 59303; -. DR Pumba; Q13315; -. DR Antibodypedia; 3596; 1753 antibodies from 48 providers. DR CPTC; Q13315; 4 antibodies. DR DNASU; 472; -. DR Ensembl; ENST00000278616.9; ENSP00000278616.4; ENSG00000149311.20. DR Ensembl; ENST00000452508.6; ENSP00000388058.2; ENSG00000149311.20. DR Ensembl; ENST00000675843.1; ENSP00000501606.1; ENSG00000149311.20. DR GeneID; 472; -. DR KEGG; hsa:472; -. DR MANE-Select; ENST00000675843.1; ENSP00000501606.1; NM_000051.4; NP_000042.3. DR UCSC; uc001pkb.1; human. DR AGR; HGNC:795; -. DR CTD; 472; -. DR DisGeNET; 472; -. DR GeneCards; ATM; -. DR GeneReviews; ATM; -. DR HGNC; HGNC:795; ATM. DR HPA; ENSG00000149311; Low tissue specificity. DR MalaCards; ATM; -. DR MIM; 208900; phenotype. DR MIM; 607585; gene. DR neXtProt; NX_Q13315; -. DR OpenTargets; ENSG00000149311; -. DR Orphanet; 100; Ataxia-telangiectasia. DR Orphanet; 370109; Ataxia-telangiectasia variant. DR Orphanet; 67038; B-cell chronic lymphocytic leukemia. DR Orphanet; 440437; Familial colorectal cancer Type X. DR Orphanet; 1331; Familial prostate cancer. DR Orphanet; 52416; Mantle cell lymphoma. DR PharmGKB; PA61; -. DR VEuPathDB; HostDB:ENSG00000149311; -. DR eggNOG; KOG0892; Eukaryota. DR GeneTree; ENSGT00670000098061; -. DR HOGENOM; CLU_000178_3_1_1; -. DR InParanoid; Q13315; -. DR OMA; VVTKGCC; -. DR OrthoDB; 8448at2759; -. DR PhylomeDB; Q13315; -. DR TreeFam; TF101182; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; Q13315; -. DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks. DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA). DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange. DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release. DR Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation. DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation. DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint. DR Reactome; R-HSA-69541; Stabilization of p53. DR Reactome; R-HSA-912446; Meiotic recombination. DR Reactome; R-HSA-9664873; Pexophagy. DR Reactome; R-HSA-9701192; Defective homologous recombination repair (HRR) due to BRCA1 loss of function. DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function. DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function. DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51. DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2. DR SignaLink; Q13315; -. DR SIGNOR; Q13315; -. DR BioGRID-ORCS; 472; 54 hits in 1215 CRISPR screens. DR ChiTaRS; ATM; human. DR GeneWiki; Ataxia_telangiectasia_mutated; -. DR GenomeRNAi; 472; -. DR Pharos; Q13315; Tchem. DR PRO; PR:Q13315; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q13315; Protein. DR Bgee; ENSG00000149311; Expressed in calcaneal tendon and 207 other cell types or tissues. DR ExpressionAtlas; Q13315; baseline and differential. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:1990391; C:DNA repair complex; IDA:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IEA:Ensembl. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IMP:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004677; F:DNA-dependent protein kinase activity; IDA:BHF-UCL. DR GO; GO:0035979; F:histone H2AXS139 kinase activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:BHF-UCL. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:CAFA. DR GO; GO:0071500; P:cellular response to nitrosative stress; IDA:ParkinsonsUK-UCL. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProt. DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:ARUK-UCL. DR GO; GO:0071481; P:cellular response to X-ray; IDA:ParkinsonsUK-UCL. DR GO; GO:0090398; P:cellular senescence; TAS:Reactome. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0000077; P:DNA damage checkpoint signaling; IDA:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IDA:CAFA. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome. DR GO; GO:0006302; P:double-strand break repair; TAS:Reactome. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome. DR GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IMP:BHF-UCL. DR GO; GO:0097694; P:establishment of RNA localization to telomere; IMP:BHF-UCL. DR GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0071044; P:histone mRNA catabolic process; IDA:UniProtKB. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central. DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl. DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl. DR GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:BHF-UCL. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB. DR GO; GO:1904354; P:negative regulation of telomere capping; IMP:BHF-UCL. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:ParkinsonsUK-UCL. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0048599; P:oocyte development; IEA:Ensembl. DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl. DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IMP:MGI. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL. DR GO; GO:0000425; P:pexophagy; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:ARUK-UCL. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL. DR GO; GO:1903626; P:positive regulation of DNA catabolic process; IEA:Ensembl. DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:1904884; P:positive regulation of telomerase catalytic core complex assembly; IMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISS:BHF-UCL. DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ARUK-UCL. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0002331; P:pre-B cell allelic exclusion; ISS:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:0010506; P:regulation of autophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0051726; P:regulation of cell cycle; IMP:BHF-UCL. DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome. DR GO; GO:1903978; P:regulation of microglial cell activation; IEA:Ensembl. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IGI:BHF-UCL. DR GO; GO:0090399; P:replicative senescence; IMP:BHF-UCL. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB. DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl. DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central. DR GO; GO:0048538; P:thymus development; IEA:Ensembl. DR GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl. DR CDD; cd05171; PIKKc_ATM; 1. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR038980; ATM_plant. DR InterPro; IPR003152; FATC_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000403; PI3/4_kinase_cat_dom. DR InterPro; IPR036940; PI3/4_kinase_cat_sf. DR InterPro; IPR018936; PI3/4_kinase_CS. DR InterPro; IPR003151; PIK-rel_kinase_FAT. DR InterPro; IPR014009; PIK_FAT. DR InterPro; IPR044107; PIKKc_ATM. DR InterPro; IPR021668; TAN. DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1. DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1. DR Pfam; PF02259; FAT; 1. DR Pfam; PF02260; FATC; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF11640; TAN; 1. DR SMART; SM01343; FATC; 1. DR SMART; SM00146; PI3Kc; 1. DR SMART; SM01342; TAN; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51189; FAT; 1. DR PROSITE; PS51190; FATC; 1. DR PROSITE; PS00915; PI3_4_KINASE_1; 1. DR PROSITE; PS00916; PI3_4_KINASE_2; 1. DR PROSITE; PS50290; PI3_4_KINASE_3; 1. DR Genevisible; Q13315; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Disease variant; DNA damage; KW DNA-binding; Kinase; Neurodegeneration; Nucleotide-binding; Nucleus; KW Peroxisome; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Tumor suppressor. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..3056 FT /note="Serine-protein kinase ATM" FT /id="PRO_0000088840" FT DOMAIN 1940..2566 FT /note="FAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534" FT DOMAIN 2686..2998 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT DOMAIN 3024..3056 FT /note="FATC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534, FT ECO:0000255|PROSITE-ProRule:PRU00535" FT REGION 1373..1382 FT /note="Interaction with ABL1" FT /evidence="ECO:0000269|PubMed:9168117" FT REGION 2692..2698 FT /note="G-loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 2867..2875 FT /note="Catalytic loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 2887..2911 FT /note="Activation loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT MOTIF 3046..3048 FT /note="Microbody targeting signal; atypical" FT /evidence="ECO:0000269|PubMed:26344566" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 367 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:16858402" FT MOD_RES 1893 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:16858402" FT MOD_RES 1981 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:12556884, FT ECO:0000269|PubMed:16141325, ECO:0000269|PubMed:16858402, FT ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:30944854, FT ECO:0007744|PubMed:17525332" FT MOD_RES 1983 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 2996 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195" FT MOD_RES 3016 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:17923702, FT ECO:0000269|PubMed:30944854" FT VARIANT 23 FT /note="R -> Q (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs587779858)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041545" FT VARIANT 35..3056 FT /note="Missing (in AT; dbSNP:rs55861249)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085060" FT VARIANT 45 FT /note="R -> W (found in a patient with breast cancer; FT uncertain significance; dbSNP:rs3218684)" FT /evidence="ECO:0000269|PubMed:11897822" FT /id="VAR_056678" FT VARIANT 49 FT /note="S -> C (in AT; increases protein abundance; FT dbSNP:rs1800054)" FT /evidence="ECO:0000269|PubMed:10425038, FT ECO:0000269|PubMed:10534763, ECO:0000269|PubMed:10873394, FT ECO:0000269|PubMed:11897822, ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:18384426, ECO:0000269|PubMed:8665503, FT ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:9887333" FT /id="VAR_010798" FT VARIANT 68 FT /note="I -> V (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083373" FT VARIANT 126 FT /note="D -> E (in dbSNP:rs2234997)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:9711876" FT /id="VAR_010799" FT VARIANT 140 FT /note="D -> H (in dbSNP:rs55633650)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041546" FT VARIANT 182 FT /note="V -> L (in dbSNP:rs3218707)" FT /evidence="ECO:0000269|PubMed:10534763" FT /id="VAR_010800" FT VARIANT 224 FT /note="K -> E (in AT; uncertain significance; FT dbSNP:rs145053092)" FT /evidence="ECO:0000269|PubMed:10817650" FT /id="VAR_010801" FT VARIANT 250 FT /note="R -> Q (in dbSNP:rs56123940)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041547" FT VARIANT 292 FT /note="P -> L (in AT; decrease phosphorylation of target FT proteins; increases protein abundance; dbSNP:rs747727055)" FT /evidence="ECO:0000269|PubMed:10873394, FT ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:9463314" FT /id="VAR_010802" FT VARIANT 323 FT /note="I -> V (in AT; loss of protein expression; FT dbSNP:rs587781511)" FT /evidence="ECO:0000269|PubMed:10817650, FT ECO:0000269|PubMed:27664052" FT /id="VAR_010803" FT VARIANT 332 FT /note="Y -> C (in B-cell chronic lymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9892178" FT /id="VAR_010804" FT VARIANT 333 FT /note="S -> F (in dbSNP:rs28904919)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041548" FT VARIANT 337 FT /note="R -> C (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs138398778)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041549" FT VARIANT 337 FT /note="R -> H (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs202160435)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041550" FT VARIANT 341 FT /note="V -> I (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083374" FT VARIANT 350 FT /note="A -> T (in B-cell chronic lymphocytic leukemia; FT dbSNP:rs371713984)" FT /evidence="ECO:0000269|PubMed:10023947" FT /id="VAR_010805" FT VARIANT 352 FT /note="I -> T (in B-cell chronic lymphocytic leukemia; FT dbSNP:rs369203092)" FT /evidence="ECO:0000269|PubMed:10023947" FT /id="VAR_010806" FT VARIANT 374..3056 FT /note="Missing (in AT; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_085061" FT VARIANT 393..3056 FT /note="Missing (in AT; uncertain significance; FT dbSNP:rs587776547)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085062" FT VARIANT 410 FT /note="V -> A (in dbSNP:rs56128736)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041551" FT VARIANT 504 FT /note="N -> S (in dbSNP:rs56365018)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041552" FT VARIANT 514 FT /note="G -> D (in dbSNP:rs2235000)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:9711876" FT /id="VAR_010807" FT VARIANT 540 FT /note="C -> Y (in a colorectal adenocarcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041553" FT VARIANT 546 FT /note="L -> V (no effect on phosphorylation of target FT proteins; dbSNP:rs2227924)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:19431188" FT /id="VAR_041554" FT VARIANT 570 FT /note="F -> S (in AT; dbSNP:rs777301065)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010808" FT VARIANT 582 FT /note="F -> L (in dbSNP:rs2235006)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041555" FT VARIANT 597 FT /note="P -> L (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083375" FT VARIANT 661 FT /note="D -> A (found in a patient with familial breast FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28202063" FT /id="VAR_083376" FT VARIANT 699 FT /note="E -> G (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083377" FT VARIANT 705..707 FT /note="YSS -> FIP (in AT)" FT /evidence="ECO:0000269|PubMed:8797579, FT ECO:0000269|PubMed:9043869" FT /id="VAR_010809" FT VARIANT 707 FT /note="S -> P (in dbSNP:rs4986761)" FT /evidence="ECO:0000269|PubMed:10534763, FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:28202063" FT /id="VAR_010810" FT VARIANT 759 FT /note="S -> G (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083378" FT VARIANT 761 FT /note="T -> S (in dbSNP:rs2235011)" FT /id="VAR_056679" FT VARIANT 768 FT /note="N -> D (in AT)" FT /evidence="ECO:0000269|PubMed:9463314" FT /id="VAR_010812" FT VARIANT 785 FT /note="R -> C (in AT; dbSNP:rs587778065)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010813" FT VARIANT 788 FT /note="S -> R (in dbSNP:rs641252)" FT /id="VAR_056680" FT VARIANT 813 FT /note="N -> S (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083379" FT VARIANT 814 FT /note="D -> E (in dbSNP:rs3218695)" FT /id="VAR_056681" FT VARIANT 848 FT /note="E -> Q (in a lung adenocarcinoma sample; somatic FT mutation; dbSNP:rs879254046)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041556" FT VARIANT 858 FT /note="F -> L (in dbSNP:rs1800056)" FT /evidence="ECO:0000269|PubMed:10534763, FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:18384426, FT ECO:0000269|PubMed:28202063, ECO:0000269|PubMed:8797579, FT ECO:0000269|PubMed:9043869, ECO:0000269|PubMed:9792409, FT ECO:0000269|PubMed:9887333" FT /id="VAR_010814" FT VARIANT 869 FT /note="A -> G (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083380" FT VARIANT 872 FT /note="P -> S (in dbSNP:rs3218673)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041557" FT VARIANT 897 FT /note="F -> I (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083381" FT VARIANT 924 FT /note="R -> W (found in a patient with familial breast FT cancer; uncertain significance; dbSNP:rs55723361)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:28202063" FT /id="VAR_041558" FT VARIANT 935 FT /note="T -> A (in dbSNP:rs35813135)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041559" FT VARIANT 935 FT /note="T -> M (in dbSNP:rs3218708)" FT /id="VAR_056682" FT VARIANT 942 FT /note="L -> F (in dbSNP:rs3218688)" FT /id="VAR_056683" FT VARIANT 950 FT /note="L -> R (in AT; dbSNP:rs786203054)" FT /id="VAR_010815" FT VARIANT 1001 FT /note="L -> Q (in AT; risk factor for T-cell acute FT lymphoblastic leukemia)" FT /evidence="ECO:0000269|PubMed:9463314" FT /id="VAR_010816" FT VARIANT 1040 FT /note="M -> V (found in B-cell non-Hodgkin lymphoma; FT uncertain significance; dbSNP:rs3092857)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010817" FT VARIANT 1046 FT /note="L -> P (in AT; loss of protein expression; FT dbSNP:rs568461905)" FT /evidence="ECO:0000269|PubMed:27664052" FT /id="VAR_077237" FT VARIANT 1054 FT /note="P -> R (in AT; likely benign; no effect on FT phosphorylation of target proteins; dbSNP:rs1800057)" FT /evidence="ECO:0000269|PubMed:10023947, FT ECO:0000269|PubMed:10217116, ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:18384426, ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:28202063, ECO:0000269|PubMed:8665503, FT ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:9043869, FT ECO:0000269|PubMed:9792409, ECO:0000269|PubMed:9887333" FT /id="VAR_010818" FT VARIANT 1082 FT /note="H -> L (in AT; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_010819" FT VARIANT 1091 FT /note="E -> D (in AT)" FT /evidence="ECO:0000269|PubMed:9792409" FT /id="VAR_010820" FT VARIANT 1171..3056 FT /note="Missing (in AT; uncertain significance; increases FT protein abundance)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085063" FT VARIANT 1179 FT /note="S -> F (in a gastric adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041560" FT VARIANT 1255 FT /note="L -> V (found in a patient with early-onset breast FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:18384426" FT /id="VAR_083382" FT VARIANT 1313 FT /note="E -> Q (in dbSNP:rs3092841)" FT /id="VAR_056684" FT VARIANT 1321 FT /note="M -> I (in dbSNP:rs35184530)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041561" FT VARIANT 1322 FT /note="L -> I (no effect on phosphorylation of target FT proteins; dbSNP:rs144535256)" FT /evidence="ECO:0000269|PubMed:19431188" FT /id="VAR_080300" FT VARIANT 1380 FT /note="H -> Y (in dbSNP:rs3092856)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041562" FT VARIANT 1382 FT /note="P -> S (in dbSNP:rs55859590)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041563" FT VARIANT 1407 FT /note="I -> T (in T-prolymphocytic leukemia; FT dbSNP:rs1234250980)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010821" FT VARIANT 1420 FT /note="L -> F (in dbSNP:rs1800058)" FT /evidence="ECO:0000269|PubMed:10534763, FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:8665503, FT ECO:0000269|PubMed:8797579" FT /id="VAR_010822" FT VARIANT 1420 FT /note="L -> P (in AT)" FT /evidence="ECO:0000269|PubMed:10817650" FT /id="VAR_010823" FT VARIANT 1427 FT /note="A -> T (in dbSNP:rs2229021)" FT /id="VAR_056685" FT VARIANT 1463 FT /note="F -> S (found in B-cell non-Hodgkin lymphoma; FT uncertain significance)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010825" FT VARIANT 1465 FT /note="L -> P (in AT; decreased phosphorylation of target FT proteins; dbSNP:rs730881391)" FT /evidence="ECO:0000269|PubMed:10234507, FT ECO:0000269|PubMed:19431188" FT /id="VAR_010826" FT VARIANT 1466..3056 FT /note="Missing (in AT; uncertain significance; FT dbSNP:rs730881369)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_085064" FT VARIANT 1469 FT /note="I -> M (in a renal papillary cancer sample; somatic FT mutation; dbSNP:rs775047783)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041564" FT VARIANT 1474 FT /note="H -> D (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083383" FT VARIANT 1475 FT /note="Y -> C (in dbSNP:rs34640941)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041565" FT VARIANT 1488 FT /note="L -> V (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083384" FT VARIANT 1541 FT /note="L -> F (in dbSNP:rs3092849)" FT /id="VAR_056686" FT VARIANT 1566 FT /note="P -> R (in AT)" FT /evidence="ECO:0000269|PubMed:9792409" FT /id="VAR_010827" FT VARIANT 1570 FT /note="V -> A (in dbSNP:rs140856217)" FT /evidence="ECO:0000269|PubMed:10534763" FT /id="VAR_010828" FT VARIANT 1650 FT /note="N -> S (in dbSNP:rs55870064)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041566" FT VARIANT 1682 FT /note="D -> H (in T-prolymphocytic leukemia; FT dbSNP:rs121434217)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010829" FT VARIANT 1691 FT /note="S -> R (in AT, B-cell chronic lymphocytic leukemia FT and familial cancer patients; no effect on phosphorylation FT of target proteins; dbSNP:rs1800059)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:28202063, ECO:0000269|PubMed:8797579, FT ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9892178" FT /id="VAR_010830" FT VARIANT 1729 FT /note="V -> L (in dbSNP:rs3092907)" FT /id="VAR_056687" FT VARIANT 1730..3056 FT /note="Missing (in AT; uncertain significance; FT dbSNP:rs764389018)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_085065" FT VARIANT 1739 FT /note="N -> T (in a colorectal adenocarcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041567" FT VARIANT 1743 FT /note="T -> I (in AT; decreased phosphorylation of target FT proteins; dbSNP:rs587779844)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:9463314" FT /id="VAR_010831" FT VARIANT 1812..1813 FT /note="AF -> V (in AT)" FT /evidence="ECO:0000269|PubMed:9497252" FT /id="VAR_010832" FT VARIANT 1839..3056 FT /note="Missing (in AT; uncertain significance; reduces FT protein abundance)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085066" FT VARIANT 1853 FT /note="D -> N (in dbSNP:rs1801516)" FT /evidence="ECO:0000269|PubMed:10397742, FT ECO:0000269|PubMed:10425038, ECO:0000269|PubMed:10534763, FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:18384426, FT ECO:0000269|PubMed:9711876, ECO:0000269|PubMed:9887333" FT /id="VAR_010833" FT VARIANT 1853 FT /note="D -> V (might contribute to B-cell chronic FT lymphocytic leukemia; dbSNP:rs1801673)" FT /evidence="ECO:0000269|PubMed:10397742, FT ECO:0000269|PubMed:10817650, ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:28202063, ECO:0000269|PubMed:9872980, FT ECO:0000269|PubMed:9887333" FT /id="VAR_010834" FT VARIANT 1910 FT /note="L -> H (in T-prolymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010835" FT VARIANT 1913 FT /note="V -> G (in AT; dbSNP:rs1060501688)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010836" FT VARIANT 1916 FT /note="M -> I (in a breast pleomorphic lobular carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041568" FT VARIANT 1945 FT /note="A -> T (in a colorectal adenocarcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041569" FT VARIANT 1953 FT /note="T -> R (in B-cell chronic lymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:10397742" FT /id="VAR_010837" FT VARIANT 1961 FT /note="Y -> C (found in a patient with familial pancreatic FT cancer; uncertain significance; also found in a lung FT adenocarcinoma sample; uncertain significance; decreased FT phosphorylation of target proteins; dbSNP:rs56399311)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:28726808" FT /id="VAR_041570" FT VARIANT 1983 FT /note="S -> N (in dbSNP:rs659243)" FT /evidence="ECO:0000269|PubMed:16554811" FT /id="VAR_041571" FT VARIANT 1991 FT /note="E -> D (in a renal clear cell carcinoma sample; FT somatic mutation; dbSNP:rs587782274)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041572" FT VARIANT 2016 FT /note="D -> G (in AT; uncertain significance; FT dbSNP:rs587781302)" FT /evidence="ECO:0000269|PubMed:10425038, FT ECO:0000269|PubMed:9887333" FT /id="VAR_010838" FT VARIANT 2023 FT /note="G -> R (in AT; loss of protein expression; FT dbSNP:rs11212587)" FT /evidence="ECO:0000269|PubMed:27664052" FT /id="VAR_077238" FT VARIANT 2034 FT /note="R -> Q (in dbSNP:rs3218670)" FT /id="VAR_056688" FT VARIANT 2063 FT /note="G -> E (in AT; uncertain significance; reduces FT protein abundance; dbSNP:rs866290641)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_010839" FT VARIANT 2067 FT /note="A -> D (in AT; dbSNP:rs397514577)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010840" FT VARIANT 2068 FT /note="L -> S (in AT; decreased protein abundance; loss of FT DNA damage induced protein autophosphorylation; FT dbSNP:rs1555114558)" FT /evidence="ECO:0000269|PubMed:27664052" FT /id="VAR_077239" FT VARIANT 2079 FT /note="V -> I (in dbSNP:rs1800060)" FT /evidence="ECO:0000269|PubMed:8665503" FT /id="VAR_010841" FT VARIANT 2080 FT /note="Y -> D (in AT; loss of DNA damage induced protein FT autophosphorylation; dbSNP:rs1064795467)" FT /evidence="ECO:0000269|PubMed:27664052" FT /id="VAR_077240" FT VARIANT 2105 FT /note="R -> T (found in a patient with early-onset breast FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:18384426" FT /id="VAR_083385" FT VARIANT 2139 FT /note="E -> G (in T-prolymphocytic leukemia; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:9488043" FT /id="VAR_010842" FT VARIANT 2164 FT /note="E -> K (in T-prolymphocytic leukemia; FT dbSNP:rs1317619286)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010843" FT VARIANT 2218 FT /note="S -> C (in AT)" FT /evidence="ECO:0000269|PubMed:10817650" FT /id="VAR_010844" FT VARIANT 2224..2227 FT /note="MALR -> IS (in AT; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_010845" FT VARIANT 2227 FT /note="R -> C (in AT; uncertain significance; reduces FT protein abundance; dbSNP:rs564652222)" FT /evidence="ECO:0000269|PubMed:10873394, FT ECO:0000269|PubMed:9887333" FT /id="VAR_010846" FT VARIANT 2246..2252 FT /note="CIKDILT -> H (in AT; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10425038, FT ECO:0000269|PubMed:10873394" FT /id="VAR_010847" FT VARIANT 2274 FT /note="A -> T (in B-cell chronic lymphocytic leukemia; FT uncertain significance; no effect on phosphorylation of FT target proteins; dbSNP:rs567060474)" FT /evidence="ECO:0000269|PubMed:10023947, FT ECO:0000269|PubMed:19431188" FT /id="VAR_010848" FT VARIANT 2287 FT /note="G -> A (found in a patient with familial pancreatic FT cancer; uncertain significance; dbSNP:rs1800061)" FT /evidence="ECO:0000269|PubMed:28726808, FT ECO:0000269|PubMed:8665503" FT /id="VAR_010849" FT VARIANT 2307 FT /note="L -> F (found in patients with familial pancreatic FT cancer; uncertain significance; also found in a lung FT adenocarcinoma sample; uncertain significance; FT dbSNP:rs56009889)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:28726808" FT /id="VAR_041573" FT VARIANT 2332 FT /note="L -> P (in dbSNP:rs4988111)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041574" FT VARIANT 2335 FT /note="T -> K (in dbSNP:rs3092831)" FT /id="VAR_056689" FT VARIANT 2356 FT /note="I -> F (in a renal clear cell carcinoma sample; FT somatic mutation; dbSNP:rs876658517)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041575" FT VARIANT 2396 FT /note="T -> S (found in a patient with T-prolymphocytic FT leukemia; uncertain significance; also found in a patient FT with early-onset breast cancer; uncertain significance; FT dbSNP:rs370559102)" FT /evidence="ECO:0000269|PubMed:18384426, FT ECO:0000269|PubMed:9288106" FT /id="VAR_010850" FT VARIANT 2408 FT /note="S -> L (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs730881315)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041576" FT VARIANT 2418 FT /note="K -> KK (in mantle cell lymphoma)" FT /evidence="ECO:0000269|PubMed:10397742, FT ECO:0000269|PubMed:10706620" FT /id="VAR_010851" FT VARIANT 2420 FT /note="A -> P (in B-cell chronic lymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:10397742" FT /id="VAR_010852" FT VARIANT 2423 FT /note="E -> G (in mantle cell lymphoma; dbSNP:rs121434221)" FT /evidence="ECO:0000269|PubMed:10397742, FT ECO:0000269|PubMed:10706620" FT /id="VAR_010853" FT VARIANT 2424 FT /note="V -> G (in AT; also found in B-cell chronic FT lymphocytic leukemia and T-prolymphocytic leukemia; FT probable risk factor for breast cancer; decreased FT phosphorylation of target proteins; dbSNP:rs28904921)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:9288106, FT ECO:0000269|PubMed:9463314, ECO:0000269|PubMed:9892178" FT /id="VAR_010854" FT VARIANT 2427..2428 FT /note="Missing (in AT; also found in T-prolymphocytic FT leukemia; lack of phosphorylation of target proteins)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:7792600, ECO:0000269|PubMed:8845835, FT ECO:0000269|PubMed:9463314" FT /id="VAR_010855" FT VARIANT 2438 FT /note="T -> I (in dbSNP:rs147604227)" FT /evidence="ECO:0000269|PubMed:10817650, FT ECO:0000269|PubMed:8808599" FT /id="VAR_010856" FT VARIANT 2442 FT /note="Q -> P (in T-prolymphocytic leukemia; also in a lung FT adenocarcinoma sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:9288106" FT /id="VAR_010857" FT VARIANT 2443 FT /note="R -> Q (in a colorectal adenocarcinoma sample; FT somatic mutation; dbSNP:rs587782310)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041577" FT VARIANT 2464 FT /note="C -> R (found in patients with familial pancreatic FT cancer; uncertain significance; also found in a small cell FT lung cancer sample; uncertain significance; FT dbSNP:rs55801750)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:28726808" FT /id="VAR_041578" FT VARIANT 2470 FT /note="Y -> D (in AT; dbSNP:rs876659365)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010858" FT VARIANT 2486 FT /note="R -> G (in T-prolymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9573030" FT /id="VAR_010859" FT VARIANT 2491 FT /note="W -> R (in AT)" FT /evidence="ECO:0000269|PubMed:9792410" FT /id="VAR_010860" FT VARIANT 2492 FT /note="L -> R (in dbSNP:rs56399857)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041579" FT VARIANT 2524 FT /note="A -> P (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083386" FT VARIANT 2531 FT /note="M -> T (found in patients with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083387" FT VARIANT 2546..2548 FT /note="Missing (in AT; also found in T-prolymphocytic FT leukemia and T-cell acute lymphoblastic leukemia; lack of FT phosphorylation of target proteins)" FT /evidence="ECO:0000269|PubMed:10817650, FT ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:7792600, FT ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:8789452, FT ECO:0000269|PubMed:8797579, ECO:0000269|PubMed:8808599, FT ECO:0000269|PubMed:8845835, ECO:0000269|PubMed:9150358, FT ECO:0000269|PubMed:9288106, ECO:0000269|PubMed:9463314" FT /id="VAR_010861" FT VARIANT 2547..2549 FT /note="Missing (in AT; dbSNP:rs587776547)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085067" FT VARIANT 2554 FT /note="H -> D (in AT; lack of phosphorylation of target FT proteins)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:9463314" FT /id="VAR_010862" FT VARIANT 2570 FT /note="E -> G (in dbSNP:rs28904920)" FT /id="VAR_056690" FT VARIANT 2625..2626 FT /note="DA -> EP (in AT; dbSNP:rs267606668)" FT /evidence="ECO:0000269|PubMed:9521587" FT /id="VAR_010864" FT VARIANT 2625 FT /note="D -> E (in AT; uncertain significance; FT dbSNP:rs1196903858)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085068" FT VARIANT 2625 FT /note="D -> Q (in AT; requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:10817650" FT /id="VAR_010863" FT VARIANT 2626 FT /note="A -> P (in AT; uncertain significance; FT dbSNP:rs267606669)" FT /evidence="ECO:0000269|PubMed:10873394" FT /id="VAR_085069" FT VARIANT 2627 FT /note="Y -> H (in AT; loss of protein expression)" FT /evidence="ECO:0000269|PubMed:27664052" FT /id="VAR_077241" FT VARIANT 2640 FT /note="T -> I (in dbSNP:rs4988125)" FT /id="VAR_056691" FT VARIANT 2656 FT /note="L -> P (in AT; dbSNP:rs121434218)" FT /evidence="ECO:0000269|PubMed:9450874" FT /id="VAR_010865" FT VARIANT 2662 FT /note="Missing (in AT)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010866" FT VARIANT 2664 FT /note="Missing (in AT; uncertain significance; FT dbSNP:rs1471563800)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_085070" FT VARIANT 2666 FT /note="T -> A (in a lung adenocarcinoma sample; somatic FT mutation; dbSNP:rs745775382)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041580" FT VARIANT 2668 FT /note="E -> G (in AT; uncertain significance; no effect on FT phosphorylation of target proteins)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:9463314" FT /id="VAR_010868" FT VARIANT 2695 FT /note="G -> A (in T-prolymphocytic leukemia and B-cell FT chronic lymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:10023947, FT ECO:0000269|PubMed:9288106" FT /id="VAR_010869" FT VARIANT 2702 FT /note="I -> R (in AT; dbSNP:rs876659735)" FT /id="VAR_010870" FT VARIANT 2709 FT /note="G -> S (in dbSNP:rs3218680)" FT /id="VAR_056692" FT VARIANT 2719 FT /note="R -> H (found in a patient with early-onset breast FT cancer; uncertain significance; dbSNP:rs55982963)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:18384426" FT /id="VAR_041581" FT VARIANT 2722 FT /note="L -> R (in T-prolymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010871" FT VARIANT 2725 FT /note="D -> G (found in T-prolymphocytic leukemia; FT uncertain significance; dbSNP:rs1555128314)" FT /evidence="ECO:0000269|PubMed:9334731" FT /id="VAR_010872" FT VARIANT 2725 FT /note="D -> V (in T-prolymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010873" FT VARIANT 2726 FT /note="A -> V (in AT; uncertain significance)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_010874" FT VARIANT 2732 FT /note="F -> L (in T-prolymphocytic leukemia; FT dbSNP:rs876659619)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010875" FT VARIANT 2765 FT /note="G -> S (may contribute to breast cancer; lack of FT phosphorylation of target proteins; dbSNP:rs748634900)" FT /evidence="ECO:0000269|PubMed:10534763, FT ECO:0000269|PubMed:19431188" FT /id="VAR_010876" FT VARIANT 2810 FT /note="K -> Q (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083388" FT VARIANT 2810 FT /note="Missing (in T-prolymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010877" FT VARIANT 2824 FT /note="C -> Y (in AT; dbSNP:rs876660927)" FT /evidence="ECO:0000269|PubMed:9150358" FT /id="VAR_010878" FT VARIANT 2827 FT /note="F -> C (in AT; mild; decreased phosphorylation of FT target proteins; dbSNP:rs121434216)" FT /evidence="ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:8755918, ECO:0000269|PubMed:9463314" FT /id="VAR_010879" FT VARIANT 2829 FT /note="P -> L (in AT; dbSNP:rs938431501)" FT /evidence="ECO:0000269|PubMed:9711876" FT /id="VAR_010880" FT VARIANT 2832 FT /note="R -> C (in AT; also found in B-cell non-Hodgkin FT lymphoma; increases protein abundance; dbSNP:rs587779872)" FT /evidence="ECO:0000269|PubMed:10817650, FT ECO:0000269|PubMed:10873394, ECO:0000269|PubMed:9288106, FT ECO:0000269|PubMed:9443866" FT /id="VAR_010881" FT VARIANT 2832 FT /note="R -> H (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083389" FT VARIANT 2834 FT /note="F -> L (in AT; decreased protein abundance)" FT /evidence="ECO:0000269|PubMed:27664052" FT /id="VAR_077242" FT VARIANT 2842 FT /note="P -> R (in a lung adenocarcinoma sample; somatic FT mutation; dbSNP:rs879254065)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041582" FT VARIANT 2849..3056 FT /note="Missing (in AT; uncertain significance; FT dbSNP:rs587778080)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_085071" FT VARIANT 2849 FT /note="R -> P (in AT; dbSNP:rs587782202)" FT /evidence="ECO:0000269|PubMed:9887333" FT /id="VAR_010882" FT VARIANT 2855..2856 FT /note="SV -> RI (in AT; lack of phosphorylation of target FT proteins; dbSNP:rs587781353)" FT /evidence="ECO:0000269|PubMed:10817650, FT ECO:0000269|PubMed:19431188, ECO:0000269|PubMed:9872980" FT /id="VAR_010884" FT VARIANT 2855 FT /note="S -> R (in AT; uncertain significance; FT dbSNP:rs780905851)" FT /evidence="ECO:0000269|PubMed:10425038" FT /id="VAR_010883" FT VARIANT 2860 FT /note="Missing (in AT)" FT /evidence="ECO:0000269|PubMed:7792600, FT ECO:0000269|PubMed:8845835" FT /id="VAR_010885" FT VARIANT 2867 FT /note="G -> R (in AT)" FT /evidence="ECO:0000269|PubMed:8698354, FT ECO:0000269|PubMed:9887333" FT /id="VAR_010886" FT VARIANT 2870 FT /note="D -> N (in dbSNP:rs55798854)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041583" FT VARIANT 2871..2872 FT /note="RH -> S (in T-prolymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:9288106" FT /id="VAR_010887" FT VARIANT 2890 FT /note="L -> V (in T-prolymphocytic leukemia; FT dbSNP:rs587779874)" FT /evidence="ECO:0000269|PubMed:9288106, FT ECO:0000269|PubMed:9488043" FT /id="VAR_010888" FT VARIANT 2904 FT /note="E -> G (in AT; dbSNP:rs786202826)" FT /evidence="ECO:0000269|PubMed:8845835" FT /id="VAR_010889" FT VARIANT 2909 FT /note="R -> G (in AT)" FT /evidence="ECO:0000269|PubMed:9792410" FT /id="VAR_010890" FT VARIANT 2974 FT /note="P -> L (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083390" FT VARIANT 3003 FT /note="N -> D (in AT; decreased protein abundance; FT dbSNP:rs1137889)" FT /evidence="ECO:0000269|PubMed:27664052, FT ECO:0000269|PubMed:7792600, ECO:0000269|PubMed:8589678, FT ECO:0000269|PubMed:8665503" FT /id="VAR_077243" FT VARIANT 3006 FT /note="A -> P (found in T-prolymphocytic leukemia; FT uncertain significance; dbSNP:rs876658767)" FT /evidence="ECO:0000269|PubMed:9334731" FT /id="VAR_010892" FT VARIANT 3008 FT /note="R -> C (in AT; also found in T-prolymphocytic FT leukemia and mantle cell lymphoma; lack of phosphorylation FT of target proteins; dbSNP:rs587782292)" FT /evidence="ECO:0000269|PubMed:10706620, FT ECO:0000269|PubMed:10817650, ECO:0000269|PubMed:19431188, FT ECO:0000269|PubMed:9334731, ECO:0000269|PubMed:9488043, FT ECO:0000269|PubMed:9872980" FT /id="VAR_010893" FT VARIANT 3008 FT /note="R -> H (in B-cell chronic lymphocytic leukemia; FT dbSNP:rs587781894)" FT /evidence="ECO:0000269|PubMed:10397742" FT /id="VAR_010894" FT VARIANT 3018 FT /note="K -> N (in B-cell chronic lymphocytic leukemia)" FT /evidence="ECO:0000269|PubMed:10397742" FT /id="VAR_010895" FT VARIANT 3029 FT /note="G -> D (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083391" FT VARIANT 3056 FT /note="V -> L (found in a patient with familial pancreatic FT cancer; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28726808" FT /id="VAR_083392" FT MUTAGEN 367 FT /note="S->A: Loss of IR-induced S-367 autophosphorylation. FT Reduced correction of cell cycle checkpoint defects and FT DNA-repair activity. No effect on S-1893 nor S-1981 FT autophosphorylation." FT /evidence="ECO:0000269|PubMed:16858402" FT MUTAGEN 1807 FT /note="K->E: Decreased phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 1893 FT /note="S->A: Loss of IR-induced S-1893 autophosphorylation. FT Reduced correction of cell cycle checkpoint defects and FT DNA-repair activity. No effect on S-367 nor S-1981 FT autophosphorylation." FT /evidence="ECO:0000269|PubMed:16858402" FT MUTAGEN 1941 FT /note="V->L: Decreased phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 1981 FT /note="S->A: Loss of IR-induced S-1981 autophosphorylation. FT Reduced correction of cell cycle checkpoint defects and FT DNA-repair activity. No effect on S-367 nor S-1893 FT autophosphorylation. No dimer disruption." FT /evidence="ECO:0000269|PubMed:12556884, FT ECO:0000269|PubMed:16858402" FT MUTAGEN 1981 FT /note="S->D,E: Disrupts the dimer." FT /evidence="ECO:0000269|PubMed:12556884, FT ECO:0000269|PubMed:16858402" FT MUTAGEN 2019 FT /note="Y->C: Loss of phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2039 FT /note="E->K: Decreased phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2338 FT /note="L->P: Loss of phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2394 FT /note="S->L: Loss of phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2452 FT /note="L->P: Loss of phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2685 FT /note="S->T: No effect on phosphorylation of target FT proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2699 FT /note="P->L: Loss of phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2708 FT /note="D->N: Decreased phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2730 FT /note="Q->P: Loss of phosphorylation of target proteins." FT /evidence="ECO:0000269|PubMed:19431188" FT MUTAGEN 2870 FT /note="D->A: Loss of kinase activity." FT /evidence="ECO:0000269|PubMed:9733515" FT MUTAGEN 2875 FT /note="N->K: Loss of kinase activity." FT /evidence="ECO:0000269|PubMed:9733515" FT MUTAGEN 3016 FT /note="K->Q: Mimics acetylation, preventing FT dephosphorylation and subsequent ATM deactivation during FT the late stage of DNA damage response." FT /evidence="ECO:0000269|PubMed:30944854" FT MUTAGEN 3016 FT /note="K->R: Loss of DNA damage-inducible acetylation. FT Retains constitutive kinase activity, but blocks DNA FT damage-induced kinase activation. Disrupts dimer and FT abolishes S-1981 autophosphorylation." FT /evidence="ECO:0000269|PubMed:17923702" FT MUTAGEN 3018 FT /note="K->R: Retains DNA damage-inducible acetylation and FT S-1981 autophosphorylation." FT /evidence="ECO:0000269|PubMed:17923702" FT MUTAGEN 3047 FT /note="R->Q: Abolished interaction with PEX5 and FT translocation to peroxisomes in response to reactive oxygen FT species (ROS)." FT /evidence="ECO:0000269|PubMed:26344566" FT CONFLICT 46 FT /note="H -> N (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 56 FT /note="N -> I (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="Y -> N (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 488 FT /note="W -> G (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 554 FT /note="T -> A (in Ref. 1; AAC50289)" FT /evidence="ECO:0000305" FT CONFLICT 750 FT /note="K -> N (in Ref. 1; AAC50289)" FT /evidence="ECO:0000305" FT CONFLICT 754 FT /note="Q -> K (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 887 FT /note="E -> G (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 1003 FT /note="Q -> L (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 1049 FT /note="L -> W (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT CONFLICT 1089 FT /note="A -> V (in Ref. 7; CAA62603)" FT /evidence="ECO:0000305" FT HELIX 6..17 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 20..33 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 36..41 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 57..73 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 90..108 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 109..112 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 117..129 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 135..148 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 149..151 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 161..176 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 183..201 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 210..222 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 229..242 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 248..268 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 273..290 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 306..323 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 343..356 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 393..402 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 407..409 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 410..422 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 424..426 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:7SID" FT HELIX 432..442 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 452..466 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 474..492 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 493..496 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 498..500 FT /evidence="ECO:0007829|PDB:7SID" FT HELIX 501..513 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 521..524 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 525..527 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 528..530 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 536..548 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 572..580 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 597..600 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 605..607 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 608..615 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 617..619 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 620..628 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 634..636 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 646..655 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 684..704 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 707..709 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 713..731 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 732..735 FT /evidence="ECO:0007829|PDB:8OXP" FT HELIX 737..741 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 744..765 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 771..786 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 792..794 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 795..806 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 809..822 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 887..889 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 892..911 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 920..930 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 933..935 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 941..953 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 957..959 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 963..970 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 973..979 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 980..982 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 984..994 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 995..997 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 998..1002 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1009..1030 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 1031..1033 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 1036..1052 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 1060..1063 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 1066..1069 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1070..1076 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1077..1079 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1083..1092 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1093..1096 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1113..1132 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 1136..1138 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 1144..1164 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1169..1181 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1187..1201 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1206..1212 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1214..1223 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1227..1229 FT /evidence="ECO:0007829|PDB:7NI5" FT TURN 1231..1233 FT /evidence="ECO:0007829|PDB:7SID" FT HELIX 1236..1238 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1244..1261 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1265..1275 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1279..1285 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1287..1294 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1295..1297 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 1299..1303 FT /evidence="ECO:0007829|PDB:8OXM" FT HELIX 1306..1322 FT /evidence="ECO:0007829|PDB:7SIC" FT TURN 1325..1327 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1328..1330 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1332..1338 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1340..1348 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1383..1396 FT /evidence="ECO:0007829|PDB:7SIC" FT STRAND 1397..1399 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1404..1408 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1413..1428 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1432..1450 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1453..1455 FT /evidence="ECO:0007829|PDB:7SID" FT TURN 1456..1460 FT /evidence="ECO:0007829|PDB:7NI5" FT HELIX 1461..1477 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1485..1508 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1513..1515 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1517..1527 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 1528..1530 FT /evidence="ECO:0007829|PDB:7SID" FT HELIX 1532..1545 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 1546..1551 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1553..1560 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 1567..1569 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1572..1582 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 1583..1585 FT /evidence="ECO:0007829|PDB:7NI6" FT HELIX 1590..1601 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1607..1610 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1611..1623 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1625..1634 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 1635..1637 FT /evidence="ECO:0007829|PDB:8OXP" FT HELIX 1639..1641 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 1643..1658 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 1661..1663 FT /evidence="ECO:0007829|PDB:8OXM" FT HELIX 1664..1677 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1694..1702 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1706..1721 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 1723..1725 FT /evidence="ECO:0007829|PDB:8OXO" FT HELIX 1727..1742 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1744..1753 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 1754..1756 FT /evidence="ECO:0007829|PDB:7NI4" FT HELIX 1759..1763 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 1764..1767 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 1785..1789 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1792..1795 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1802..1815 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1822..1825 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1828..1831 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1835..1851 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1857..1874 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1903..1917 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 1922..1924 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1927..1930 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1938..1947 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1951..1973 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 1986..1997 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2001..2012 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2016..2019 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2023..2028 FT /evidence="ECO:0007829|PDB:7SIC" FT HELIX 2029..2038 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2042..2051 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2057..2070 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2074..2087 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2093..2105 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2124..2136 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2140..2159 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2166..2168 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2170..2190 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2195..2210 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2211..2214 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2217..2236 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2240..2242 FT /evidence="ECO:0007829|PDB:8OXP" FT HELIX 2245..2264 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2269..2281 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2290..2301 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2305..2322 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2328..2348 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2353..2359 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2361..2370 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2377..2406 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2408..2421 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2437..2475 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2481..2483 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2484..2493 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2494..2496 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2498..2507 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2508..2510 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2513..2516 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2520..2525 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2529..2531 FT /evidence="ECO:0007829|PDB:7SID" FT STRAND 2533..2535 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2537..2551 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2553..2564 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2565..2567 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2568..2572 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2593..2612 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2614..2632 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2637..2640 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2652..2655 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2659..2663 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2665..2667 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2673..2675 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2682..2686 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2688..2692 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2695..2697 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2700..2706 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2707..2709 FT /evidence="ECO:0007829|PDB:7NI4" FT STRAND 2711..2717 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2723..2740 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2743..2748 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2757..2759 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2761..2763 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2765..2768 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2773..2775 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2776..2780 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2783..2785 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2787..2791 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2798..2807 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2808..2810 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2813..2825 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2833..2838 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2842..2866 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2873..2875 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2876..2879 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2880..2882 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2885..2887 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2894..2899 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2900..2902 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 2906..2908 FT /evidence="ECO:0007829|PDB:8OXP" FT HELIX 2912..2916 FT /evidence="ECO:0007829|PDB:8OXQ" FT TURN 2920..2925 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2926..2940 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2942..2953 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 2964..2970 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 3002..3017 FT /evidence="ECO:0007829|PDB:8OXQ" FT STRAND 3020..3025 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 3028..3040 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 3042..3047 FT /evidence="ECO:0007829|PDB:8OXQ" FT HELIX 3050..3052 FT /evidence="ECO:0007829|PDB:8OXQ" SQ 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 //