CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012061
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
 AAC50289.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38309.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB38310.1; AAB65827.1; EAW67111.1; CAA62603.1; AAC51298.1; AAO26044.1; AAA86520.1; AAI37170.1 
Protein Name
 Serine-protein kinase ATM 
Protein Synonyms/Alias
 Ataxia telangiectasia mutated; A-T mutated 
Gene Name
 ATM 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41IRDPETIKHLDRHSDubiquitination[1]
53HSDSKQGKYLNWDAVubiquitination[1]
66AVFRFLQKYIQKETEubiquitination[1]
70FLQKYIQKETECLRIubiquitination[1]
79TECLRIAKPNVSASTubiquitination[1]
116NRRAPRLKCQELLNYubiquitination[1]
177VYFRLYLKPSQDVHRubiquitination[1]
196RIIHAVTKGCCSQTDubiquitination[1]
208QTDGLNSKFLDFFSKubiquitination[1]
215KFLDFFSKAIQCARQubiquitination[1]
307KGAYESTKWRSILYNubiquitination[1]
331SHIGSRGKYSSGFRNubiquitination[1]
385SDYSVPCKRKKIELGubiquitination[1]
397ELGWEVIKDHLQKSQubiquitination[1]
468EVALCQDKRSNLESSubiquitination[1]
477SNLESSQKSDLLKLWubiquitination[1]
573VNRSFSLKESIMKWLubiquitination[1]
673VRECGIEKHQSSIGFubiquitination[1]
750SELFQKAKSLMQCAGubiquitination[1]
766SITLFKNKTNEEFRIubiquitination[1]
810FLRLLTSKLMNDIADubiquitination[1]
820NDIADICKSLASFIKubiquitination[1]
926RAADIRRKLLMLIDSubiquitination[1]
988RRDQDVCKTILNHVLubiquitination[1]
1057LEADPYSKWAILNVMubiquitination[1]
1101NRLFQDTKGDSSRLLubiquitination[1, 2]
1109GDSSRLLKALPLKLQubiquitination[1, 3]
1114LLKALPLKLQQTAFEubiquitination[1, 3]
1126AFENAYLKAQEGMREubiquitination[1]
1181FALCKSVKENGLEPHubiquitination[1]
1196LVKKVLEKVSETFGYubiquitination[1]
1269RSHFDEVKSIANQIQubiquitination[1]
1317QQRETATKVYDMLKSubiquitination[1]
1323TKVYDMLKSENLLGKubiquitination[1]
1572FPDHVVFKDLRITQQubiquitination[1, 3, 4]
1615LTRLEGLKDLRRQLEubiquitination[1, 4]
1625RRQLELHKDQMVDIMubiquitination[1, 4]
1656VNLLQLSKMAINHTGubiquitination[1]
1698SKDASYTKALKLFEDubiquitination[1]
1738SAAVTCLKNILATKTubiquitination[1, 4]
1744LKNILATKTGHSFWEubiquitination[1]
1772QPFRTSRKKFLEVPRubiquitination[1]
2025LYGCGGGKMLQPITRubiquitination[1, 4]
2148STFYESLKYARVKEVubiquitination[1, 3]
2153SLKYARVKEVEEMCKubiquitination[1]
2160KEVEEMCKRSLESVYubiquitination[1, 4]
2266SILARTFKNTQLPERubiquitination[4]
2385ELRNGKMKAFLSLARubiquitination[1]
2406QRIENYMKSSEFENKubiquitination[1]
2413KSSEFENKQALLKRAubiquitination[1, 4]
2421QALLKRAKEEVGLLRubiquitination[1, 4]
2440QTNRYTVKVQRELELubiquitination[1, 4]
2505SEVNGMMKRDGMKIPubiquitination[1]
2515GMKIPTYKFLPLMYQubiquitination[1]
2589RITKNVPKQSSQLDEubiquitination[1]
2643TQWKTQRKGINIPADmethylation[5]
2643TQWKTQRKGINIPADubiquitination[1]
2657DQPITKLKNLEDVVVubiquitination[1, 4]
2710DCVGSDGKERRQLVKubiquitination[1]
2789NNEDGAHKRYRPNDFubiquitination[1]
2803FSAFQCQKKMMEVQKubiquitination[1]
2848DPAIWFEKRLAYTRSubiquitination[1]
2992NADDQECKRNLSDIDubiquitination[1]
3004DIDQSFNKVAERVLMubiquitination[1]
3016VLMRLQEKLKGVEEGacetylation[6]
3053SRLFPGWKAWV****ubiquitination[1, 2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [6] DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity.
 Sun Y, Xu Y, Roy K, Price BD.
 Mol Cell Biol. 2007 Dec;27(24):8502-9. [PMID: 17923702] 
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. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. 
Sequence Annotation
 DOMAIN 1960 2566 FAT.
 DOMAIN 2712 2962 PI3K/PI4K.
 DOMAIN 3024 3056 FATC.
 REGION 1373 1382 Interaction with ABL1.
 MOD_RES 367 367 Phosphoserine; by autocatalysis.
 MOD_RES 1893 1893 Phosphoserine; by autocatalysis.
 MOD_RES 1981 1981 Phosphoserine; by autocatalysis.
 MOD_RES 1983 1983 Phosphoserine; in variant Ser-1983.
 MOD_RES 2996 2996 Phosphoserine.
 MOD_RES 3016 3016 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Cell cycle; Complete proteome; Cytoplasmic vesicle; Disease mutation; DNA damage; DNA repair; DNA-binding; Kinase; Neurodegeneration; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3056 AA 
Protein Sequence
MSLVLNDLLI CCRQLEHDRA TERKKEVEKF KRLIRDPETI KHLDRHSDSK QGKYLNWDAV 60
FRFLQKYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL VKYFIKCANR RAPRLKCQEL 120
LNYIMDTVKD SSNGAIYGAD CSNILLKDIL SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ 180
DVHRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQCA RQEKSSSGLN HILAALTIFL 240
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK 300
GAYESTKWRS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA DICHQVFNED 360
TRSLEISQSY TTTQRESSDY SVPCKRKKIE LGWEVIKDHL QKSQNDFDLV PWLQIATQLI 420
SKYPASLPNC ELSPLLMILS QLLPQQRHGE RTPYVLRCLT EVALCQDKRS NLESSQKSDL 480
LKLWNKIWCI TFRGISSEQI QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACRPSCPAVC 540
CLTLALTTSI VPGTVKMGIE QNMCEVNRSF SLKESIMKWL LFYQLEGDLE NSTEVPPILH 600
SNFPHLVLEK ILVSLTMKNC KAAMNFFQSV PECEHHQKDK EELSFSEVEE LFLQTTFDKM 660
DFLTIVRECG IEKHQSSIGF SVHQNLKESL DRCLLGLSEQ LLNNYSSEIT NSETLVRCSR 720
LLVGVLGCYC YMGVIAEEEA YKSELFQKAK SLMQCAGESI TLFKNKTNEE FRIGSLRNMM 780
QLCTRCLSNC TKKSPNKIAS GFFLRLLTSK LMNDIADICK SLASFIKKPF DRGEVESMED 840
DTNGNLMEVE DQSSMNLFND YPDSSVSDAN EPGESQSTIG AINPLAEEYL SKQDLLFLDM 900
LKFLCLCVTT AQTNTVSFRA ADIRRKLLML IDSSTLEPTK SLHLHMYLML LKELPGEEYP 960
LPMEDVLELL KPLSNVCSLY RRDQDVCKTI LNHVLHVVKN LGQSNMDSEN TRDAQGQFLT 1020
VIGAFWHLTK ERKYIFSVRM ALVNCLKTLL EADPYSKWAI LNVMGKDFPV NEVFTQFLAD 1080
NHHQVRMLAA ESINRLFQDT KGDSSRLLKA LPLKLQQTAF ENAYLKAQEG MREMSHSAEN 1140
PETLDEIYNR KSVLLTLIAV VLSCSPICEK QALFALCKSV KENGLEPHLV KKVLEKVSET 1200
FGYRRLEDFM ASHLDYLVLE WLNLQDTEYN LSSFPFILLN YTNIEDFYRS CYKVLIPHLV 1260
IRSHFDEVKS IANQIQEDWK SLLTDCFPKI LVNILPYFAY EGTRDSGMAQ QRETATKVYD 1320
MLKSENLLGK QIDHLFISNL PEIVVELLMT LHEPANSSAS QSTDLCDFSG DLDPAPNPPH 1380
FPSHVIKATF AYISNCHKTK LKSILEILSK SPDSYQKILL AICEQAAETN NVYKKHRILK 1440
IYHLFVSLLL KDIKSGLGGA WAFVLRDVIY TLIHYINQRP SCIMDVSLRS FSLCCDLLSQ 1500
VCQTAVTYCK DALENHLHVI VGTLIPLVYE QVEVQKQVLD LLKYLVIDNK DNENLYITIK 1560
LLDPFPDHVV FKDLRITQQK IKYSRGPFSL LEEINHFLSV SVYDALPLTR LEGLKDLRRQ 1620
LELHKDQMVD IMRASQDNPQ DGIMVKLVVN LLQLSKMAIN HTGEKEVLEA VGSCLGEVGP 1680
IDFSTIAIQH SKDASYTKAL KLFEDKELQW TFIMLTYLNN TLVEDCVKVR SAAVTCLKNI 1740
LATKTGHSFW EIYKMTTDPM LAYLQPFRTS RKKFLEVPRF DKENPFEGLD DINLWIPLSE 1800
NHDIWIKTLT CAFLDSGGTK CEILQLLKPM CEVKTDFCQT VLPYLIHDIL LQDTNESWRN 1860
LLSTHVQGFF TSCLRHFSQT SRSTTPANLD SESEHFFRCC LDKKSQRTML AVVDYMRRQK 1920
RPSSGTIFND AFWLDLNYLE VAKVAQSCAA HFTALLYAEI YADKKSMDDQ EKRSLAFEEG 1980
SQNTTISSLS EKSKEETGIS LQDLLLEIYR SIGEPDSLYG CGGGKMLQPI TRLRTYEHEA 2040
MWGKALVTYD LETAIPSSTR QAGIIQALQN LGLCHILSVY LKGLDYENKD WCPELEELHY 2100
QAAWRNMQWD HCTSVSKEVE GTSYHESLYN ALQSLRDREF STFYESLKYA RVKEVEEMCK 2160
RSLESVYSLY PTLSRLQAIG ELESIGELFS RSVTHRQLSE VYIKWQKHSQ LLKDSDFSFQ 2220
EPIMALRTVI LEILMEKEMD NSQRECIKDI LTKHLVELSI LARTFKNTQL PERAIFQIKQ 2280
YNSVSCGVSE WQLEEAQVFW AKKEQSLALS ILKQMIKKLD ASCAANNPSL KLTYTECLRV 2340
CGNWLAETCL ENPAVIMQTY LEKAVEVAGN YDGESSDELR NGKMKAFLSL ARFSDTQYQR 2400
IENYMKSSEF ENKQALLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEL ALRALKEDRK 2460
RFLCKAVENY INCLLSGEEH DMWVFRLCSL WLENSGVSEV NGMMKRDGMK IPTYKFLPLM 2520
YQLAARMGTK MMGGLGFHEV LNNLISRISM DHPHHTLFII LALANANRDE FLTKPEVARR 2580
SRITKNVPKQ SSQLDEDRTE AANRIICTIR SRRPQMVRSV EALCDAYIIL ANLDATQWKT 2640
QRKGINIPAD QPITKLKNLE DVVVPTMEIK VDHTGEYGNL VTIQSFKAEF RLAGGVNLPK 2700
IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL TICTYKVVPL 2760
SQRSGVLEWC TGTVPIGEFL VNNEDGAHKR YRPNDFSAFQ CQKKMMEVQK KSFEEKYEVF 2820
MDVCQNFQPV FRYFCMEKFL DPAIWFEKRL AYTRSVATSS IVGYILGLGD RHVQNILINE 2880
QSAELVHIDL GVAFEQGKIL PTPETVPFRL TRDIVDGMGI TGVEGVFRRC CEKTMEVMRN 2940
SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDETEL HPTLNADDQE CKRNLSDIDQ 3000
SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAI DPKNLSRLFP GWKAWV 3056 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005819; C:spindle; IEA:Compara.
 GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IMP: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; IDA:BHF-UCL.
 GO:0035174; F:histone serine kinase activity; IEA:Compara.
 GO:0032403; F:protein complex binding; IDA:BHF-UCL.
 GO:0046983; F:protein dimerization activity; IDA:BHF-UCL.
 GO:0047485; F:protein N-terminus binding; IDA:UniProtKB.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0007050; P:cell cycle arrest; IMP:BHF-UCL.
 GO:0071480; P:cellular response to gamma radiation; IDA:BHF-UCL.
 GO:0006975; P:DNA damage induced protein phosphorylation; IDA:BHF-UCL.
 GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
 GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
 GO:0007292; P:female gamete generation; IEA:Compara.
 GO:0031572; P:G2 DNA damage checkpoint; IMP:BHF-UCL.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0071044; P:histone mRNA catabolic process; IDA:UniProtKB.
 GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Compara.
 GO:0042159; P:lipoprotein catabolic process; IEA:Compara.
 GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
 GO:0051402; P:neuron apoptotic process; IEA:Compara.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
 GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
 GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
 GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
 GO:0002331; P:pre-B cell allelic exclusion; ISS:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL.
 GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
 GO:0090399; P:replicative senescence; IMP:BHF-UCL.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0001756; P:somitogenesis; IEA:Compara.
 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