CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014428
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine-protein kinase ATM 
Protein Synonyms/Alias
 Ataxia telangiectasia mutated homolog; A-T mutated homolog 
Gene Name
 Atm 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1326TKVYDTLKGEDFLGKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. 
Sequence Annotation
 DOMAIN 1966 2576 FAT.
 DOMAIN 2722 2972 PI3K/PI4K.
 DOMAIN 3034 3066 FATC.
 REGION 1380 1389 Interaction with ABL1 (By similarity).
 MOD_RES 367 367 Phosphoserine; by autocatalysis.
 MOD_RES 1899 1899 Phosphoserine; by autocatalysis.
 MOD_RES 1987 1987 Phosphoserine; by autocatalysis.
 MOD_RES 3006 3006 Phosphoserine (By similarity).
 MOD_RES 3026 3026 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; ATP-binding; Cell cycle; Complete proteome; Cytoplasmic vesicle; DNA damage; DNA repair; DNA-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3066 AA 
Protein Sequence
MSLALNDLLI CCRQLEHDRA TERRKEVDKF KRLIQDPETV QHLDRHSDSK QGKYLNWDAV 60
FRFLQKYIQK EMESLRTAKS NVSATTQSSR QKKMQEISSL VRYFIKCANK RAPRLKCQDL 120
LNYVMDTVKD SSNGLTYGAD CSNILLKDIL SVRKYWCEVS QQQWLELFSL YFRLYLKPSQ 180
DINRVLVARI IHAVTRGCCS QTDGLPSKFL DLFSKAIQYA RQEKSSPGLS HILAALNIFL 240
KSLAVNFRKR VCEAGDEILP TLLYIWTQHR LNDSLKEVII ELIQLQIYIH HPQGARAPEE 300
GAYESMKWKS ILYNLYDLLV NEISHIGSRG KYSSGSRNIA VKENLIDLMA DICYQLFDAD 360
TRSVEISQSY VTQRESTDYS VPCKRRKIDV GWEVIKDYLQ KSQSDFDLVP WLQITTRLIS 420
KYPSSLPNCE LSPLILILYQ LLPQQRRGER IPYVLRCLKE VALCQGKKSN LESSQKSDLL 480
KLWIKIWSIT FRGISSGQTQ TENFGLLEAI IQGSLVELDR EFWKLFTGSA CKPSSPSVCC 540
LTLALSICVV PDAIKMGTEQ SVCEANRSFS VKESIMRWLL FYQLEDDLED STELPPILQS 600
NFPHLVVEKI LVSLTMKNSK AAMKFFQSVP ECEQHCEDKE EPSFSEVEEL FLQTTFDKMD 660
FLTTVKEYAV EKFQSSVGFS VQQNLKESLD HYLLGLSEQL LSNYSSEITS SETLVRCSSL 720
LVGVLGCYCY MGIITEDEAH KSELFQKAKS LMQCAGESIS LFKNKTNEES RIGSLRNVMH 780
LCTSCLCIHT KHTPNKIASG FFLRLLTSKL MNDIADICKS LASCTKKPLD HGVHPGEDDE 840
DGGGCDSLME AEGPSSTGLS TAYPASSVSD ANDYGENQNA VGAMSPLAAD YLSKQDHLLL 900
DMLRFLGRSV TASQSHTVSF RGADIRRKLL LLLDSSILDL MKPLHLHMYL VLLKDLPGNE 960
HSLPMEDVVE LLQPLSLVCS LHRRDQDVCK TILSNVLHIV TNLGQGSVDM ESTRIAQGHF 1020
LTVMGAFWHL TKEKKCVFSV RMALVKCLQT LLEADPYSEW AILNVKGQDF PVNEAFSQFL 1080
ADDHHQVRML AAGSVNRLFQ DMRQGDFSRS LKALPLKFQQ TSFNNAYTTA EAGIRGLLCD 1140
SQNPDLLDEI YNRKSVLLMM IAVVLHCSPV CEKQALFALC KSVKENRLEP HLVKKVLEKV 1200
SESFGCRSLE DFMISHLDYL VLEWLNLQDT EYSLSSFPFM LLNYTSIEDF YRSCYKILIP 1260
HLVIRSHFDE VKSIANQIQK CWKSLLVDCF PKILVHILPY FAYEGTRDSY VSQKRETATK 1320
VYDTLKGEDF LGKQIDQVFI SNLPEIVVEL LMTLHETADS ADSDASQSAT ALCDFSGDLD 1380
PAPNPPYFPS HVIQATFAYI SNCHKTKFKS ILEILSKIPD SYQKILLAIC EQAAETNNVF 1440
KKHRILKIYH LFVSLLLKDI QSGLGGAWAF VLRDVIYTLI HYINKRSSHF TDVSLRSFSL 1500
CCDLLSRVCH TAVTQCKDAL ESHLHVIVGT LIPLVDYQEV QEQVLDLLKY LVIDNKDNKN 1560
LSVTIKLLDP FPDHVIFKDL RLTQQKIKYS GGPFSLLEEI NHFLSVSAYN PLPLTRLEGL 1620
KDLRRQLEQH KDQMLDLLRA SQDNPQDGIV VKLVVSLLQL SKMAVNQTGE REVLEAVGRC 1680
LGEIGPLDFS TIAVQHNKDV SYTKAYGLPE DRELQWTLIM LTALNNTLVE DSVKIRSAAA 1740
TCLKNILATK IGHIFWENYK TSADPMLTYL QPFRTSRKKF LEVPRSVKED VLEGLDAVNL 1800
WVPQSESHDI WIKTLTCAFL DSGGINSEIL QLLKPMCEVK TDFCQMLLPY LIHDVLLQDT 1860
HESWRTLLSA HVRGFFTSCF KHSSQASRSA TPANSDSESE NFLRCCLDKK SQRTMLAVVD 1920
YLRRQKRPSS GTAFDDAFWL DLNYLEVAKV AQSCSAHFTA LLYAEIYSDK KSTDEQEKRS 1980
PTFEEGSQGT TISSLSEKSK EETGISLQDL LLEIYRSIGE PDSLYGCGGG KMLQPLTRIR 2040
TYEHEATWEK ALVTYDLETS ISSSTRQSGI IQALQNLGLS HILSVYLKGL DYERREWCAE 2100
LQELRYQAAW RNMQWGLCAS AGQEVEGTSY HESLYNALQC LRNREFSTFY ESLRYASLFR 2160
VKEVEELSKG SLESVYSLYP TLSRLQAIGE LENSGELFSR SVTDRERSEA YWKWQKHSQL 2220
LKDSDFSFQE PLMALRTVIL ETLVQKEMER SQGACSKDIL TKHLVEFSVL ARTFKNTQLP 2280
ERAIFKIKQY NSAICGISEW HLEEAQVFWA KKEQSLALSI LKQMIKKLDS SFKDKENDAG 2340
LKVIYAECLR VCGSWLAETC LENPAVIMQT YLEKAVKVAG SYDGNSRELR NGQMKAFLSL 2400
ARFSDTQYQR IENYMKSSEF ENKQTLLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEC 2460
ALRALREDRK RFLCKAVENY INCLLSGEEH DLWVFRLCSL WLENSGVSEV NGMMKKDGMK 2520
ISSYKFLPLM YQLAARMGTK MTGGLGFHEV LNNLISRISL DHPHHTLFII LALANANKDE 2580
FLSKPETTRR SRITKSTSKE NSHLDEDRTE AATRIIHSIR SKRCKMVKDM EALCDAYIIL 2640
ANMDASQWRA QRKGINIPAN QPITKLKNLE DVVVPTMEIK VDPTGEYENL VTIKSFKTEF 2700
RLAGGLNLPK IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL 2760
TICTYKVVPL SQRSGVLEWC TGTVPIGEYL VNSEDGAHRR YRPNDFSANQ CQKKMMEVQK 2820
KSFEEKYDTF MTICQNFEPV FRYFCMEKFL DPAVWFEKRL AYTRSVATSS IVGYILGLGD 2880
RHVQNILINE QSAELVHIDL GVAFEQGKIL PTPETVPFRL SRDIVDGMGI TGVEGVFRRC 2940
CEKTMEVMRS SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDESDL HSTPNADDQE 3000
CKQSLSDTDQ SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAM DPKNLSRLFP 3060
GWKAWV 3066 
Gene Ontology
 GO:0000781; C:chromosome, telomeric region; IEA:Compara.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005819; C:spindle; IDA:MGI.
 GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004677; F:DNA-dependent protein kinase activity; IEA:Compara.
 GO:0035174; F:histone serine kinase activity; IEA:Compara.
 GO:0047485; F:protein N-terminus binding; ISS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
 GO:0007420; P:brain development; IGI:MGI.
 GO:0007050; P:cell cycle arrest; IEA:Compara.
 GO:0071480; P:cellular response to gamma radiation; IEA:Compara.
 GO:0000077; P:DNA damage checkpoint; IMP:MGI.
 GO:0006975; P:DNA damage induced protein phosphorylation; IEA:Compara.
 GO:0006281; P:DNA repair; IDA:MGI.
 GO:0031572; P:G2 DNA damage checkpoint; IEA:Compara.
 GO:0007507; P:heart development; IGI:MGI.
 GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
 GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
 GO:0042159; P:lipoprotein catabolic process; IGI:MGI.
 GO:0007094; P:mitotic spindle assembly checkpoint; ISS:UniProtKB.
 GO:0030889; P:negative regulation of B cell proliferation; IEA:Compara.
 GO:0051402; P:neuron apoptotic process; IGI:MGI.
 GO:0048599; P:oocyte development; IMP:MGI.
 GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Compara.
 GO:0043525; P:positive regulation of neuron apoptotic process; IGI:MGI.
 GO:0002331; P:pre-B cell allelic exclusion; IMP:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IEA:Compara.
 GO:0090399; P:replicative senescence; IEA:InterPro.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
 GO:0001756; P:somitogenesis; IGI:MGI.
 GO:0000723; P:telomere maintenance; IEA:InterPro. 
Interpro
 IPR016024; ARM-type_fold.
 IPR015519; ATM/Tel1.
 IPR003152; FATC.
 IPR011009; Kinase-like_dom.
 IPR000403; PI3/4_kinase_cat_dom.
 IPR018936; PI3/4_kinase_CS.
 IPR003151; PIK-rel_kinase_FAT.
 IPR014009; PIK_FAT.
 IPR021668; TAN. 
Pfam
 PF02259; FAT
 PF02260; FATC
 PF00454; PI3_PI4_kinase
 PF11640; TAN 
SMART
 SM00146; PI3Kc 
PROSITE
 PS51189; FAT
 PS51190; FATC
 PS00915; PI3_4_KINASE_1
 PS00916; PI3_4_KINASE_2
 PS50290; PI3_4_KINASE_3 
PRINTS