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Protein Page:
ATM (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ATM an atypical kinase of the PIKK family. Regulates cell cycle checkpoints and DNA repair . May function as a tumor suppressor. 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. Involved in the activation of ABL1 and SAPK. Binds DNA ends and is part of the BRCA1- associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. DNA damage promotes association with RAD17. LOF mutations associated with ataxia telangiectasia, causing progressive loss of motor control (ataxia), dilation of superficial blood vessels (telangiectasia), cancer and immune deficiency. Approximately 30% of cases develop tumors, mostly lymphomas and leukemias, due to defects in DNA damage repair. Somatic mutations seen in leukemias and lymphomas. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Protein kinase, atypical; EC 2.7.11.1; ATYPICAL group; PIKK family
Cellular Component: nucleoplasm; chromosome, telomeric region; cytoplasmic membrane-bound vesicle; spindle
Molecular Function: protein dimerization activity; protein serine/threonine kinase activity; protein binding; DNA binding; 1-phosphatidylinositol-3-kinase activity; protein complex binding; DNA-dependent protein kinase activity; protein N-terminus binding; histone serine kinase activity; ATP binding
Biological Process: lipoprotein catabolic process; DNA damage induced protein phosphorylation; positive regulation of apoptosis; heart development; protein amino acid autophosphorylation; pre-B cell allelic exclusion; negative regulation of B cell proliferation; signal transduction; protein amino acid phosphorylation; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; positive regulation of neuron apoptosis; double-strand break repair; mitotic cell cycle spindle assembly checkpoint; cell cycle arrest; somitogenesis; DNA repair; double-strand break repair via homologous recombination; peptidyl-serine phosphorylation; neuron apoptosis; DNA damage response, signal transduction resulting in induction of apoptosis; meiotic recombination; response to hypoxia; response to ionizing radiation; brain development; positive regulation of DNA damage response, signal transduction by p53 class mediator; response to DNA damage stimulus; oocyte development
Reference #:  Q13315 (UniProtKB)
Alt. Names/Synonyms: A-T mutated; AT mutated; AT1; ATA; Ataxia telangiectasia mutated; ataxia telangiectasia mutated (includes complementation groups A, C and D); ATC; ATD; ATDC; ATE; ATM; DKFZp781A0353; human phosphatidylinositol 3-kinase homolog; MGC74674; Serine-protein kinase ATM; TEL1; TEL1, telomere maintenance 1, homolog; TELO1
Gene Symbols: ATM
Molecular weight: 350,687 Da
Basal Isoelectric point: 6.39  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  G1/S Checkpoint  |  G2/M DNA Damage Checkpoint  |  Mitochondrial Control of Apoptosis  |  NF-kB Signaling  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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ATM

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

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Sites Implicated In
apoptosis, altered: S1981‑p
apoptosis, induced: S794‑p
cell cycle regulation: S794‑p, S1403‑p, S1981‑p
chromatin organization, altered: S1981‑p
activity, induced: S1981‑p
enzymatic activity, induced: S367‑p, S794‑p, S1403‑p, S1981‑p, S2996‑p, K3016‑a
intracellular localization: S1981‑p
molecular association, regulation: S1981‑p
phosphorylation: S794‑p
protein stabilization: S1981‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T72-p QKYIQKEtECLRIAK
0 1 S85-p AKPNVSAstQASRQK
0 1 T86-p KPNVSAstQASRQKK
0 4 T237-p NHILAALtIFLKTLA
2 6 S367-p DTRSLEIsQSYTTtQ
0 1 T373-p IsQSYTTtQRESSDY
1 0 S440-p SPLLMILsQLLPQQR
2 0 S794-p LSNCTKKsPNKIASG
0 1 K1109-u GDSSRLLkALPLkLQ
0 1 K1114-u LLkALPLkLQQTAFE
0 1 K1126-m1 AFENAYLkAQEGMRE
0 1 K1323 TKVYDMLKSENLLGK
1 0 S1403-p CHKTKLKsILEILSK
0 1 S1414 ILSKSPDSYQKILLA
0 1 Y1415 LSKSPDSYQKILLAI
0 1 K1572-u FPDHVVFkDLRITQQ
0 1 S1655-p VVNLLQLskMAINHt
0 1 K1656-m1 VNLLQLskMAINHtG
0 1 T1662-p skMAINHtGEKEVLE
0 1 Y1717-p WTFIMLTyLNNTLVE
0 2 Y1753-p GHSFWEIyKMTTDPM
0 3 Y1763-p TTDPMLAyLQPFRTS
0 2 S1878-p TSCLRHFsQTSRsTt
0 1 S1883-p HFsQTSRsTtPANLD
0 3 T1885-p sQTSRsTtPANLDsE
2 1 S1891-p TtPANLDsEsEHFFR
3 2 S1893-p PANLDsEsEHFFRCC
128 17 S1981-p SLAFEEGsQSTtISS
0 1 T1985-p EEGsQSTtISSLSEK
0 9 Y2019-p IGEPDSLyGCGGGKM
0 1 T2031-p GKMLQPItRLRTYEH
0 1 K2148-u STFYESLkYARVKEV
0 1 S2165-p MCKRSLEsVYsLYPT
0 1 S2168-p RSLEsVYsLYPTLSR
0 1 K2643-m1 TQWKTQRkGINIPAD
0 81 Y2969-p MNPLKALyLQQRPED
1 5 S2996-p QECKRNLsDIDQSFN
1 0 K3016-a VLMRLQEkLKGVEEG
4526 : Phospho-ATM (Ser1981) (10H11.E12) Mouse mAb
5883 : Phospho-ATM (Ser1981) (D6H9) Rabbit mAb
13050 : Phospho-ATM (Ser1981) (D25E5) Rabbit mAb
  mouse

 
M72 QKYIQKEMESLRTAK
T85 AKSNVSATTQSSRQK
T86 KSNVSATTQSSRQKK
N237 SHILAALNIFLKSLA
S367-p DTRSVEIsQSYVTQR
T372 EIsQSYVTQRESTDY
Y439 SPLILILYQLLPQQR
T793 LCIHTKHTPNKIASG
K1112 GDFSRSLKALPLKFQ
K1117 SLKALPLKFQQTSFN
T1129 SFNNAYTTAEAGIRG
K1326-u TKVYDTLkGEDFLGK
S1410 CHKTKFKSILEILSK
S1421-p ILSKIPDsyQKILLA
Y1422-p LSKIPDsyQKILLAI
K1578 FPDHVIFKDLRLTQQ
S1661 VVSLLQLSKMAVNQT
K1662 VSLLQLSKMAVNQTG
T1668 SKMAVNQTGEREVLE
A1723 WTLIMLTALNNTLVE
Y1759 GHIFWENYKTSADPM
Y1769 SADPMLTYLQPFRTS
S1884 TSCFKHSSQASRSAt
S1889 HSSQASRSAtPANSD
T1891-p SQASRSAtPANSDsE
S1897-p AtPANSDsEsENFLR
S1899-p PANSDsEsENFLRCC
S1987-p SPTFEEGsQGTTISS
T1991 EEGsQGTTISSLSEK
Y2025 IGEPDSLYGCGGGKM
T2037 GKMLQPLTRIRTYEH
R2154 STFYESLRYASLFRV
S2174 LSKGSLESVYSLYPT
S2177 GSLESVYSLYPTLSR
K2653 SQWRAQRKGINIPAN
Y2979 MNPLKALYLQQRPED
S3006-p QECKQSLsDTDQSFN
K3026 VLMRLQEKLKGVEEG
  rat

 
T72 QKYIQKETESLRTAK
S85 AKSNVSASTQTSRQK
T86 KSNVSASTQTSRQKK
N237 SHILAALNIFLKTLA
S367 DTRSVEISQSYATQR
T372 EISQSYATQRESTDY
Y439 SPLILILYQLLPQQR
T793 LCRHTKHTLNKIASG
K1117 GDSSRSLKALPLKFQ
K1122 SLKALPLKFQQTSFN
I1134 SFNSAYMIAEAGIRE
K1331 TEVYDTLKGEDFLGK
S1411 CHKTKFKSILEILSK
S1422 ILSKIPDSYQKILLA
Y1423 LSKIPDSYQKILLAI
K1579 FPDHVVFKDLRLTQQ
S1662 VVSLLQLSKMAVNQT
K1663 VSLLQLSKMAVNQTG
T1669 SKMAVNQTGEREVLE
A1724 WTLIMLTALNNTLVE
H1760 GHIFWENHKTSADPM
Y1770 SADPMLTYLQPFRAS
S1885 TNCFKHSSQASRSAT
S1890 HSSQASRSATPANSD
T1892 SQASRSATPANSDSE
S1898 ATPANSDSESENFLR
S1900 PANSDSESENFLRCC
S1988-p SPTFEEGsQGTTISS
T1992 EEGsQGTTISSLSEK
Y2026 IGEPDSLYGCGGGKV
T2038 GKVLQPLTRIRTYEH
R2155 STFYDSLRHARVKEV
S2172 LSKGSLESVYSLYPT
S2175 GSLESVYSLYPTLSR
K2651 SQWRNQRKGISIPAN
Y2977 MNPLKALYLQQRPED
S3004 QECKRSLSDTDQSFN
K3024 VLMRLQEKLKGVEEG
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