Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ATR (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ATR a ser/thr kinase of the PIKK family most closely related to ATM. Activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]Q. Phosphorylates BRCA1, Chk1, MCM2, RAD17, RPA2, SMC1 and p53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Kinase, lipid; Protein kinase, ATYPICAL; Protein kinase, Ser/Thr (non-receptor); Membrane protein, integral; EC 2.7.11.1; ATYPICAL group; PIKK family; ATR subfamily
Cellular Component: XY body; nucleoplasm; PML body; chromosome
Molecular Function: protein serine/threonine kinase activity; protein binding; DNA binding; MutLalpha complex binding; MutSalpha complex binding; ATP binding; protein kinase activity
Biological Process: peptidyl-serine phosphorylation; negative regulation of DNA replication; regulation of protein binding; protein amino acid autophosphorylation; multicellular organismal development; DNA damage checkpoint; positive regulation of DNA damage response, signal transduction by p53 class mediator; cell cycle; DNA repair; DNA replication; cell cycle checkpoint; response to DNA damage stimulus
Reference #:  Q13535 (UniProtKB)
Alt. Names/Synonyms: ataxia telangiectasia and Rad3 related; Ataxia telangiectasia and Rad3-related protein; ATR; FRAP-related protein 1; FRAP-related protein-1; FRP1; MEC1; MEC1, mitosis entry checkpoint 1, homolog; protein kinase ATR; Rad3 related protein; SCKL; SCKL1; Serine/threonine-protein kinase ATR
Gene Symbols: ATR
Molecular weight: 301,367 Da
Basal Isoelectric point: 7.17  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis  |  Cell Cycle: G1/S Checkpoint  |  Cell Cycle: G2/M DNA Damage Checkpoint  |  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ATR

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
cell growth, altered: S428‑p
enzymatic activity, induced: S428‑p, T1989‑p
molecular association, regulation: T1989‑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 Y26-p GSATPEEyNTVVQkP
0 1 K32-u EyNTVVQkPRQILCQ
0 1 S61-p ELVKKTDsQPTSVML
1 0 Y291-p DTDQLKLyEEPLSKL
1 0 Y310-p FPFEAEAyRNIEPVy
0 1 Y317-p yRNIEPVyLNMLLEK
8 4 S428-p SSNSDGIsPKRRRLs
0 78 S435-p sPKRRRLsssLNPsk
0 46 S436-p PKRRRLsssLNPskR
0 5 S437-p KRRRLsssLNPskRA
0 2 S441-p LsssLNPskRAPKQT
0 1 K442-u sssLNPskRAPKQTE
0 1 T533-p KKPSVVItWMSLDFY
0 1 S580 LIYMQVNSSFEDHIL
0 1 S581 IYMQVNSSFEDHILE
0 1 K866-u ISRNNELkDTLILTT
0 2 K1005-u LLPDLAAkAsPAASA
0 1 S1007-p PDLAAkAsPAASALI
0 1 N1024 LGKQLNVNRREILIN
0 1 Y1122-p SPELMADyLQPKLLG
0 1 S1140-p FFNMQLLsSSVGIED
0 1 K1173-a HVSSVRVkMMTTLRT
0 1 T1275-p LQEYRKEtSESTDLQ
0 1 Y1312 TSLKETLYKNQEKLI
1 0 T1566-p DDQHTINtQDIASDL
1 0 T1578-p SDLCQLStQTVFSML
1 0 T1589-p FSMLDHLtQWARHKF
0 1 K1613-u HSKSNRNkVDSMVST
0 4 S1645-p QDTLAVAsFRSKAYT
0 1 K1703-u RKAEPSLkEQILEHE
0 2 K1824-u TAFYDSLkLVRAEQI
0 1 S1871-p IKPLFQHsPGDSsQE
0 1 S1876-p QHsPGDSsQEDSLNW
2 27 T1989-p LCFPENEtPPEGKNM
0 1 S2186-p MTAVSKSsyPMRVNR
0 1 Y2187-p TAVSKSsyPMRVNRC
0 1 T2219 VGDATRLTDKLLELC
0 1 S2313-p LQKPKKIsLKGSDGK
0 1 K2587-u TGEVVNEkAKTHVLD
0 1 K2604-u QRLQGVIkTRNRVTG
2853 : Phospho-ATR (Ser428) Antibody
  mouse

 
Y26 GSATPEEYNTVVQKP
K32 EYNTVVQKPRQILCQ
A61 ELVKKTDAQPTSVML
Y294 DADQLKLYEEPLSKL
Y313 FPFEAEAYRNIEPVY
Y320 YRNIEPVYLNVLLEK
S431-p SGNNDEVsPKRRKLs
S438-p sPKRRKLsSSLSSYK
S439 PKRRKLsSSLSSYKK
S440 KRRKLsSSLSSYKKP
Y444 LsSSLSSYKKPSRQP
K445 sSSLSSYKKPSRQPE
T536 KKPPVVVTWMSLDFY
S583-p LMYMQVKssFKDHVL
S584-p MYMQVKssFKDHVLE
K866 IARNNELKDTLILTT
K1005 LLPDLAAKASPAASA
S1007 PDLAAKASPAASALI
S1024-p LGKQLNVsRREILIN
Y1122 SPELMADYLQPKLLG
S1140 FFNMQLLSSSVGIED
K1173 HVSSVRVKMMTTLRT
T1275 LQEYRKETSETTDLQ
Y1312-p TSLKETLyKNQEKLI
T1566 DEQHAISTQDSASDL
T1578 SDLCQLSTQTVFSVL
T1589 FSVLDHLTQWARHKF
- gap
S1639 QDTLAVASFRSKAYT
K1697 RKAEPSLKEQILEHE
K1818 TTFYDTLKLVRAEQI
S1865 LKPLFRKSPGDSCNE
C1870 RKSPGDSCNEDSLNW
S1983 LCFPENKSPSESKHM
S2180 MTAVSKSSYPMRVNR
Y2181 TAVSKSSYPMRVNRC
T2213-p VGDATRLtDKLLELC
S2304 LQKPKKISLKGSDGK
K2578 TGEVVNEKAKTHVLD
K2595 QRLQGVIKTRNRVTG
2853 : Phospho-ATR (Ser428) Antibody
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.