CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037549
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Serine-protein kinase ATM 
Protein Synonyms/Alias
  
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, 2]
116NRRAPRLKCQELLNYubiquitination[1]
177VYFRLYLKPSQDVHRubiquitination[1]
196RIIHAVTKGCCSQTDubiquitination[1]
208QTDGLNSKFLDFFSKubiquitination[1]
215KFLDFFSKAIQCARQubiquitination[1]
307KGAYESTKWRSILYNubiquitination[1]
331SHIGSRGKYSSGFRNubiquitination[1]
385SDYSVPCKRKKIELGubiquitination[1, 2]
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, 3]
1109GDSSRLLKALPLKLQubiquitination[1, 2, 4, 5]
1114LLKALPLKLQQTAFEubiquitination[1, 2, 4, 5]
1126AFENAYLKAQEGMREubiquitination[1]
1181FALCKSVKENGLEPHubiquitination[1]
1196LVKKVLEKVSETFGYubiquitination[1]
1269RSHFDEVKSIANQIQubiquitination[1]
1317QQRETATKVYDMLKSubiquitination[1]
1323TKVYDMLKSENLLGKubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1369 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 QSTDLCDFS 1369 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005819; C:spindle; IEA:Compara.
 GO:0035174; F:histone serine kinase activity; IEA:Compara.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0000077; P:DNA damage checkpoint; IEA:Compara.
 GO:0006281; P:DNA repair; IEA:Compara.
 GO:0007292; P:female gamete generation; IEA:Compara.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Compara.
 GO:0042159; P:lipoprotein catabolic process; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0051402; P:neuron apoptotic process; IEA:Compara.
 GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
 GO:0002331; P:pre-B cell allelic exclusion; IEA:Compara.
 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; IEA:InterPro.
 GO:0001756; P:somitogenesis; IEA:Compara.
 GO:0000723; P:telomere maintenance; IEA:InterPro. 
Interpro
 IPR016024; ARM-type_fold.
 IPR015519; ATM/Tel1.
 IPR021668; TAN. 
Pfam
 PF11640; TAN 
SMART
  
PROSITE
  
PRINTS