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Protein

Serine/threonine-protein kinase ATR

Gene

ATR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine protein kinase which 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, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, 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.22 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mn2+1 Publication

Enzyme regulationi

Activated by DNA and inhibited by BCR-ABL oncogene. Slightly activated by ATRIP. Inhibited by caffeine, wortmannin and LY294002.3 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • MutLalpha complex binding Source: MGI
  • MutSalpha complex binding Source: MGI
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: BHF-UCL

GO - Biological processi

  • cell cycle Source: ProtInc
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to gamma radiation Source: BHF-UCL
  • cellular response to UV Source: BHF-UCL
  • DNA damage checkpoint Source: UniProtKB
  • DNA repair Source: ProtInc
  • DNA replication Source: Reactome
  • establishment of macromolecular complex localization to telomere Source: BHF-UCL
  • establishment of RNA localization to telomere Source: BHF-UCL
  • interstrand cross-link repair Source: Reactome
  • multicellular organism development Source: ProtInc
  • negative regulation of DNA replication Source: UniProtKB
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • positive regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  • positive regulation of telomerase catalytic core complex assembly Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein autophosphorylation Source: BHF-UCL
  • protein localization to chromosome, telomeric region Source: BHF-UCL
  • regulation of cellular response to heat Source: Reactome
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • replicative senescence Source: BHF-UCL
  • response to drug Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Manganese, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169604-MONOMER.
ZFISH:HS10870-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6783310. Fanconi Anemia Pathway.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ13535.
SIGNORiQ13535.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase ATR (EC:2.7.11.1)
Alternative name(s):
Ataxia telangiectasia and Rad3-related protein
FRAP-related protein 1
Gene namesi
Name:ATR
Synonyms:FRP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:882. ATR.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • nucleoplasm Source: HPA
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Seckel syndrome 1 (SCKL1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation.
See also OMIM:210600
Cutaneous telangiectasia and cancer syndrome, familial (FCTCS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by cutaneous telangiectases in infancy with patchy alopecia over areas of affected skin, thinning of the lateral eyebrows, and mild dental and nail anomalies. Affected individuals are at increased risk of developing oropharyngeal cancer, and other malignancies have been reported as well.
See also OMIM:614564
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0679192144Q → R in FCTCS. 1 PublicationCorresponds to variant rs387906797dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2327K → R: Abolishes kinase activity. 3 Publications1
Mutagenesisi2475D → A: Abolishes kinase activity; increases sensitivity to IR and impairs translocation to nuclear foci upon DNA damage. 3 Publications1
Mutagenesisi2494D → E: Abolishes kinase activity; reduces cell viability, augments sensitivity to IR and UV. 2 Publications1

Keywords - Diseasei

Disease mutation, Dwarfism, Mental retardation

Organism-specific databases

DisGeNETi545.
MalaCardsiATR.
MIMi210600. phenotype.
614564. phenotype.
OpenTargetsiENSG00000175054.
Orphaneti313846. Familial cutaneous telangiectasia and oropharyngeal predisposition cancer syndrome.
808. Seckel syndrome.
PharmGKBiPA74.

Chemistry databases

ChEMBLiCHEMBL5024.
GuidetoPHARMACOLOGYi1935.

Polymorphism and mutation databases

BioMutaiATR.
DMDMi62286460.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888441 – 2644Serine/threonine-protein kinase ATRAdd BLAST2644

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei428PhosphoserineCombined sources1 Publication1
Modified residuei435PhosphoserineCombined sources1
Modified residuei436PhosphoserineCombined sources1
Modified residuei1989PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated; autophosphorylates in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13535.
MaxQBiQ13535.
PaxDbiQ13535.
PeptideAtlasiQ13535.
PRIDEiQ13535.

PTM databases

iPTMnetiQ13535.
PhosphoSitePlusiQ13535.

Expressioni

Tissue specificityi

Ubiquitous, with highest expression in testis. Isoform 2 is found in pancreas, placenta and liver but not in heart, testis and ovary.3 Publications

Gene expression databases

BgeeiENSG00000175054.
CleanExiHS_ATR.
ExpressionAtlasiQ13535. baseline and differential.
GenevisibleiQ13535. HS.

Organism-specific databases

HPAiHPA028264.
HPA054320.

Interactioni

Subunit structurei

Interacts with ATRIP (By similarity). Forms a heterodimer with ATRIP. Binds to DNA, and to UV-damaged DNA with higher affinity. Interacts with RAD17, MSH2 and HDAC2. Present in a complex containing ATRIP and RPA-coated single-stranded DNA. Present in a complex containing CHD4 and HDAC2. Interacts with BCR-ABL after genotoxic stress. Interacts with EEF1E1. This interaction is enhanced by UV irradiation. Interacts with CLSPN and CEP164. Interacts with TELO2 and TTI1.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC5LQ994593EBI-968983,EBI-374880
CDK9P507503EBI-968983,EBI-1383449
IKBKGQ9Y6K92EBI-968983,EBI-81279
TTI1O431562EBI-968983,EBI-1055680

GO - Molecular functioni

  • MutLalpha complex binding Source: MGI
  • MutSalpha complex binding Source: MGI

Protein-protein interaction databases

BioGridi107027. 111 interactors.
DIPiDIP-35308N.
IntActiQ13535. 19 interactors.
MINTiMINT-194575.
STRINGi9606.ENSP00000343741.

Chemistry databases

BindingDBiQ13535.

Structurei

3D structure databases

ProteinModelPortaliQ13535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati799 – 835HEAT 1Add BLAST37
Repeati1329 – 1365HEAT 2Add BLAST37
Domaini1640 – 2185FATPROSITE-ProRule annotationAdd BLAST546
Domaini2322 – 2567PI3K/PI4KPROSITE-ProRule annotationAdd BLAST246
Domaini2612 – 2644FATCPROSITE-ProRule annotationAdd BLAST33

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family. ATM subfamily.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 2 HEAT repeats.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0890. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00830000128321.
HOGENOMiHOG000034221.
HOVERGENiHBG050619.
InParanoidiQ13535.
KOiK06640.
OMAiWRRFPEH.
OrthoDBiEOG091G013Q.
PhylomeDBiQ13535.
TreeFamiTF101183.

Family and domain databases

Gene3Di1.10.1070.11. 2 hits.
1.25.10.10. 4 hits.
1.25.40.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC_dom.
IPR021133. HEAT_type_2.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical_dom.
IPR012993. UME.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08064. UME. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00802. UME. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 7 hits.
SSF48452. SSF48452. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50077. HEAT_REPEAT. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13535-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGEHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV
60 70 80 90 100
VAVELVKKTD SQPTSVMLLD FIQHIMKSSP LMFVNVSGSH EAKGSCIEFS
110 120 130 140 150
NWIITRLLRI AATPSCHLLH KKICEVICSL LFLFKSKSPA IFGVLTKELL
160 170 180 190 200
QLFEDLVYLH RRNVMGHAVE WPVVMSRFLS QLDEHMGYLQ SAPLQLMSMQ
210 220 230 240 250
NLEFIEVTLL MVLTRIIAIV FFRRQELLLW QIGCVLLEYG SPKIKSLAIS
260 270 280 290 300
FLTELFQLGG LPAQPASTFF SSFLELLKHL VEMDTDQLKL YEEPLSKLIK
310 320 330 340 350
TLFPFEAEAY RNIEPVYLNM LLEKLCVMFE DGVLMRLKSD LLKAALCHLL
360 370 380 390 400
QYFLKFVPAG YESALQVRKV YVRNICKALL DVLGIEVDAE YLLGPLYAAL
410 420 430 440 450
KMESMEIIEE IQCQTQQENL SSNSDGISPK RRRLSSSLNP SKRAPKQTEE
460 470 480 490 500
IKHVDMNQKS ILWSALKQKA ESLQISLEYS GLKNPVIEML EGIAVVLQLT
510 520 530 540 550
ALCTVHCSHQ NMNCRTFKDC QHKSKKKPSV VITWMSLDFY TKVLKSCRSL
560 570 580 590 600
LESVQKLDLE ATIDKVVKIY DALIYMQVNS SFEDHILEDL CGMLSLPWIY
610 620 630 640 650
SHSDDGCLKL TTFAANLLTL SCRISDSYSP QAQSRCVFLL TLFPRRIFLE
660 670 680 690 700
WRTAVYNWAL QSSHEVIRAS CVSGFFILLQ QQNSCNRVPK ILIDKVKDDS
710 720 730 740 750
DIVKKEFASI LGQLVCTLHG MFYLTSSLTE PFSEHGHVDL FCRNLKATSQ
760 770 780 790 800
HECSSSQLKA SVCKPFLFLL KKKIPSPVKL AFIDNLHHLC KHLDFREDET
810 820 830 840 850
DVKAVLGTLL NLMEDPDKDV RVAFSGNIKH ILESLDSEDG FIKELFVLRM
860 870 880 890 900
KEAYTHAQIS RNNELKDTLI LTTGDIGRAA KGDLVPFALL HLLHCLLSKS
910 920 930 940 950
ASVSGAAYTE IRALVAAKSV KLQSFFSQYK KPICQFLVES LHSSQMTALP
960 970 980 990 1000
NTPCQNADVR KQDVAHQREM ALNTLSEIAN VFDFPDLNRF LTRTLQVLLP
1010 1020 1030 1040 1050
DLAAKASPAA SALIRTLGKQ LNVNRREILI NNFKYIFSHL VCSCSKDELE
1060 1070 1080 1090 1100
RALHYLKNET EIELGSLLRQ DFQGLHNELL LRIGEHYQQV FNGLSILASF
1110 1120 1130 1140 1150
ASSDDPYQGP RDIISPELMA DYLQPKLLGI LAFFNMQLLS SSVGIEDKKM
1160 1170 1180 1190 1200
ALNSLMSLMK LMGPKHVSSV RVKMMTTLRT GLRFKDDFPE LCCRAWDCFV
1210 1220 1230 1240 1250
RCLDHACLGS LLSHVIVALL PLIHIQPKET AAIFHYLIIE NRDAVQDFLH
1260 1270 1280 1290 1300
EIYFLPDHPE LKKIKAVLQE YRKETSESTD LQTTLQLSMK AIQHENVDVR
1310 1320 1330 1340 1350
IHALTSLKET LYKNQEKLIK YATDSETVEP IISQLVTVLL KGCQDANSQA
1360 1370 1380 1390 1400
RLLCGECLGE LGAIDPGRLD FSTTETQGKD FTFVTGVEDS SFAYGLLMEL
1410 1420 1430 1440 1450
TRAYLAYADN SRAQDSAAYA IQELLSIYDC REMETNGPGH QLWRRFPEHV
1460 1470 1480 1490 1500
REILEPHLNT RYKSSQKSTD WSGVKKPIYL SKLGSNFAEW SASWAGYLIT
1510 1520 1530 1540 1550
KVRHDLASKI FTCCSIMMKH DFKVTIYLLP HILVYVLLGC NQEDQQEVYA
1560 1570 1580 1590 1600
EIMAVLKHDD QHTINTQDIA SDLCQLSTQT VFSMLDHLTQ WARHKFQALK
1610 1620 1630 1640 1650
AEKCPHSKSN RNKVDSMVST VDYEDYQSVT RFLDLIPQDT LAVASFRSKA
1660 1670 1680 1690 1700
YTRAVMHFES FITEKKQNIQ EHLGFLQKLY AAMHEPDGVA GVSAIRKAEP
1710 1720 1730 1740 1750
SLKEQILEHE SLGLLRDATA CYDRAIQLEP DQIIHYHGVV KSMLGLGQLS
1760 1770 1780 1790 1800
TVITQVNGVH ANRSEWTDEL NTYRVEAAWK LSQWDLVENY LAADGKSTTW
1810 1820 1830 1840 1850
SVRLGQLLLS AKKRDITAFY DSLKLVRAEQ IVPLSAASFE RGSYQRGYEY
1860 1870 1880 1890 1900
IVRLHMLCEL EHSIKPLFQH SPGDSSQEDS LNWVARLEMT QNSYRAKEPI
1910 1920 1930 1940 1950
LALRRALLSL NKRPDYNEMV GECWLQSARV ARKAGHHQTA YNALLNAGES
1960 1970 1980 1990 2000
RLAELYVERA KWLWSKGDVH QALIVLQKGV ELCFPENETP PEGKNMLIHG
2010 2020 2030 2040 2050
RAMLLVGRFM EETANFESNA IMKKYKDVTA CLPEWEDGHF YLAKYYDKLM
2060 2070 2080 2090 2100
PMVTDNKMEK QGDLIRYIVL HFGRSLQYGN QFIYQSMPRM LTLWLDYGTK
2110 2120 2130 2140 2150
AYEWEKAGRS DRVQMRNDLG KINKVITEHT NYLAPYQFLT AFSQLISRIC
2160 2170 2180 2190 2200
HSHDEVFVVL MEIIAKVFLA YPQQAMWMMT AVSKSSYPMR VNRCKEILNK
2210 2220 2230 2240 2250
AIHMKKSLEK FVGDATRLTD KLLELCNKPV DGSSSTLSMS THFKMLKKLV
2260 2270 2280 2290 2300
EEATFSEILI PLQSVMIPTL PSILGTHANH ASHEPFPGHW AYIAGFDDMV
2310 2320 2330 2340 2350
EILASLQKPK KISLKGSDGK FYIMMCKPKD DLRKDCRLME FNSLINKCLR
2360 2370 2380 2390 2400
KDAESRRREL HIRTYAVIPL NDECGIIEWV NNTAGLRPIL TKLYKEKGVY
2410 2420 2430 2440 2450
MTGKELRQCM LPKSAALSEK LKVFREFLLP RHPPIFHEWF LRTFPDPTSW
2460 2470 2480 2490 2500
YSSRSAYCRS TAVMSMVGYI LGLGDRHGEN ILFDSLTGEC VHVDFNCLFN
2510 2520 2530 2540 2550
KGETFEVPEI VPFRLTHNMV NGMGPMGTEG LFRRACEVTM RLMRDQREPL
2560 2570 2580 2590 2600
MSVLKTFLHD PLVEWSKPVK GHSKAPLNET GEVVNEKAKT HVLDIEQRLQ
2610 2620 2630 2640
GVIKTRNRVT GLPLSIEGHV HYLIQEATDE NLLCQMYLGW TPYM
Length:2,644
Mass (Da):301,367
Last modified:July 5, 2004 - v3
Checksum:i11BC22297FB9A802
GO
Isoform 2 (identifier: Q13535-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     450-450: E → D
     451-514: Missing.

Show »
Length:2,580
Mass (Da):294,219
Checksum:iA7C5CED46708FC16
GO
Isoform 3 (identifier: Q13535-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2588-2610: AKTHVLDIEQRLQGVIKTRNRVT → VSRRYSLIWAVVLISTNELDMQL
     2611-2644: Missing.

Note: No experimental confirmation available.
Show »
Length:2,610
Mass (Da):297,479
Checksum:i44281024A65D73B1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti92A → R in CAA70298 (PubMed:8978690).Curated1
Sequence conflicti92A → R in AAC50929 (PubMed:8978690).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04158464T → A.1 PublicationCorresponds to variant rs35306038dbSNPEnsembl.1
Natural variantiVAR_04158590H → Y.1 PublicationCorresponds to variant rs28897763dbSNPEnsembl.1
Natural variantiVAR_050532211M → T.Corresponds to variant rs2227928dbSNPEnsembl.1
Natural variantiVAR_041586297K → N.1 PublicationCorresponds to variant rs2229033dbSNPEnsembl.1
Natural variantiVAR_041587316V → I.1 PublicationCorresponds to variant rs28897764dbSNPEnsembl.1
Natural variantiVAR_041588959V → M.1 PublicationCorresponds to variant rs28910271dbSNPEnsembl.1
Natural variantiVAR_0415891087Y → H.1 PublicationCorresponds to variant rs34253059dbSNPEnsembl.1
Natural variantiVAR_0415901213S → G.1 PublicationCorresponds to variant rs34766606dbSNPEnsembl.1
Natural variantiVAR_0415911488A → P in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0505331526I → V.Corresponds to variant rs34124242dbSNPEnsembl.1
Natural variantiVAR_0415921607S → N.1 PublicationCorresponds to variant rs55724025dbSNPEnsembl.1
Natural variantiVAR_0415931612N → S.1 PublicationCorresponds to variant rs55894265dbSNPEnsembl.1
Natural variantiVAR_0415942002A → G in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0415952120G → A.1 PublicationCorresponds to variant rs35134774dbSNPEnsembl.1
Natural variantiVAR_0415962132Y → D.1 PublicationCorresponds to variant rs28910273dbSNPEnsembl.1
Natural variantiVAR_0679192144Q → R in FCTCS. 1 PublicationCorresponds to variant rs387906797dbSNPEnsembl.1
Natural variantiVAR_0415972233S → I in a lung large cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0415982425R → Q.1 PublicationCorresponds to variant rs2229032dbSNPEnsembl.1
Natural variantiVAR_0415992434P → A.1 PublicationCorresponds to variant rs33972295dbSNPEnsembl.1
Natural variantiVAR_0416002438E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0416012537E → Q in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_013305450E → D in isoform 2. 1 Publication1
Alternative sequenceiVSP_013304451 – 514Missing in isoform 2. 1 PublicationAdd BLAST64
Alternative sequenceiVSP_0369072588 – 2610AKTHV…RNRVT → VSRRYSLIWAVVLISTNELD MQL in isoform 3. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_0369082611 – 2644Missing in isoform 3. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09077 mRNA. Translation: CAA70298.1.
U76308 mRNA. Translation: AAC50929.1.
U49844 mRNA. Translation: AAC50405.1.
AF325699 Genomic DNA. Translation: AAK26749.1.
AB208847 mRNA. Translation: BAD92084.1.
CCDSiCCDS3124.1. [Q13535-1]
RefSeqiNP_001175.2. NM_001184.3. [Q13535-1]
XP_016862132.1. XM_017006643.1. [Q13535-2]
UniGeneiHs.271791.

Genome annotation databases

EnsembliENST00000350721; ENSP00000343741; ENSG00000175054. [Q13535-1]
GeneIDi545.
KEGGihsa:545.
UCSCiuc003eux.5. human. [Q13535-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09077 mRNA. Translation: CAA70298.1.
U76308 mRNA. Translation: AAC50929.1.
U49844 mRNA. Translation: AAC50405.1.
AF325699 Genomic DNA. Translation: AAK26749.1.
AB208847 mRNA. Translation: BAD92084.1.
CCDSiCCDS3124.1. [Q13535-1]
RefSeqiNP_001175.2. NM_001184.3. [Q13535-1]
XP_016862132.1. XM_017006643.1. [Q13535-2]
UniGeneiHs.271791.

3D structure databases

ProteinModelPortaliQ13535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107027. 111 interactors.
DIPiDIP-35308N.
IntActiQ13535. 19 interactors.
MINTiMINT-194575.
STRINGi9606.ENSP00000343741.

Chemistry databases

BindingDBiQ13535.
ChEMBLiCHEMBL5024.
GuidetoPHARMACOLOGYi1935.

PTM databases

iPTMnetiQ13535.
PhosphoSitePlusiQ13535.

Polymorphism and mutation databases

BioMutaiATR.
DMDMi62286460.

Proteomic databases

EPDiQ13535.
MaxQBiQ13535.
PaxDbiQ13535.
PeptideAtlasiQ13535.
PRIDEiQ13535.

Protocols and materials databases

DNASUi545.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000350721; ENSP00000343741; ENSG00000175054. [Q13535-1]
GeneIDi545.
KEGGihsa:545.
UCSCiuc003eux.5. human. [Q13535-1]

Organism-specific databases

CTDi545.
DisGeNETi545.
GeneCardsiATR.
GeneReviewsiATR.
H-InvDBHIX0030886.
HGNCiHGNC:882. ATR.
HPAiHPA028264.
HPA054320.
MalaCardsiATR.
MIMi210600. phenotype.
601215. gene.
614564. phenotype.
neXtProtiNX_Q13535.
OpenTargetsiENSG00000175054.
Orphaneti313846. Familial cutaneous telangiectasia and oropharyngeal predisposition cancer syndrome.
808. Seckel syndrome.
PharmGKBiPA74.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0890. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00830000128321.
HOGENOMiHOG000034221.
HOVERGENiHBG050619.
InParanoidiQ13535.
KOiK06640.
OMAiWRRFPEH.
OrthoDBiEOG091G013Q.
PhylomeDBiQ13535.
TreeFamiTF101183.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169604-MONOMER.
ZFISH:HS10870-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6783310. Fanconi Anemia Pathway.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ13535.
SIGNORiQ13535.

Miscellaneous databases

ChiTaRSiATR. human.
GeneWikiiAtaxia_telangiectasia_and_Rad3_related.
GenomeRNAii545.
PROiQ13535.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175054.
CleanExiHS_ATR.
ExpressionAtlasiQ13535. baseline and differential.
GenevisibleiQ13535. HS.

Family and domain databases

Gene3Di1.10.1070.11. 2 hits.
1.25.10.10. 4 hits.
1.25.40.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR003152. FATC_dom.
IPR021133. HEAT_type_2.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR011990. TPR-like_helical_dom.
IPR012993. UME.
[Graphical view]
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08064. UME. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM00802. UME. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 7 hits.
SSF48452. SSF48452. 2 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50077. HEAT_REPEAT. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATR_HUMAN
AccessioniPrimary (citable) accession number: Q13535
Secondary accession number(s): Q59HB2
, Q7KYL3, Q93051, Q9BXK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.