Q13535 (ATR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ATR
Synonyms:	FRP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2644 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Manganese. Ref.11
Enzyme regulation	Activated by DNA and inhibited by BCR-ABL oncogene. Slightly activated by ATRIP. Inhibited by caffeine, wortmannin and LY294002. Ref.6 Ref.12 Ref.30
Subunit structure	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. Ref.9 Ref.16 Ref.17 Ref.22 Ref.23 Ref.24 Ref.25 Ref.30 Ref.32 Ref.33 Ref.34 Ref.38 Ref.39 Ref.40
Subcellular location	Nucleus. Nucleus › PML body By similarity. Chromosome By similarity. Note: Depending on the cell type, it can also be found in PML nuclear bodies. Recruited to chromatin during S-phase. Redistributes to discrete nuclear foci upon DNA damage, hypoxia or replication fork stalling. Ref.5 Ref.14 Ref.17 Ref.19 Ref.21 Ref.27 Ref.34
Tissue specificity	Ubiquitous, with highest expression in testis. Isoform 2 is found in pancreas, placenta and liver but not in heart, testis and ovary. Ref.2 Ref.3 Ref.5
Post-translational modification	Phosphorylated; autophosphorylates in vitro. Ref.7 Ref.12
Involvement in disease	Seckel syndrome 1 (SCKL1) [MIM:210600]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35 Cutaneous telangiectasia and cancer syndrome, familial (FCTCS) [MIM:614564]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.44
Sequence similarities	Belongs to the PI3/PI4-kinase family. ATM subfamily. Contains 1 FAT domain. Contains 1 FATC domain. Contains 2 HEAT repeats. Contains 1 PI3K/PI4K domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dwarfism Mental retardation
Domain	Repeat
Ligand	ATP-binding DNA-binding Manganese Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from direct assay Ref.23. Source: UniProtKB DNA repair Traceable author statement. Source: Reactome DNA replication Traceable author statement. Source: Reactome cellular response to UV Inferred from mutant phenotype Ref.10. Source: BHF-UCL cellular response to gamma radiation Inferred from direct assay Ref.10. Source: BHF-UCL multicellular organismal development Traceable author statement PubMed 9590286. Source: ProtInc negative regulation of DNA replication Inferred from mutant phenotype Ref.23. Source: UniProtKB peptidyl-serine phosphorylation Inferred from direct assay PubMed 9733515. Source: BHF-UCL positive regulation of DNA damage response, signal transduction by p53 class mediator Inferred from mutant phenotype Ref.10. Source: BHF-UCL protein autophosphorylation Inferred from direct assay PubMed 9733515. Source: BHF-UCL regulation of protein binding Inferred from electronic annotation. Source: Compara replicative senescence Inferred from mutant phenotype PubMed 15149599. Source: BHF-UCL
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell XY body Inferred from electronic annotation. Source: Compara chromosome Inferred from sequence or structural similarity. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW MutLalpha complex binding Inferred from direct assay PubMed 16713580. Source: MGI MutSalpha complex binding Inferred from direct assay PubMed 16713580. Source: MGI protein serine/threonine kinase activity Inferred from direct assay PubMed 9733515Ref.10. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TTI1	O43156	2	EBI-968983,EBI-1055680

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13535-1)

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.

Isoform 2 (identifier: Q13535-2)

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

Isoform 3 (identifier: Q13535-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2644	2644	Serine/threonine-protein kinase ATR		PRO_0000088844
Regions
	Repeat	799 – 835	37	HEAT 1
	Repeat	1329 – 1365	37	HEAT 2
	Domain	1640 – 2185	546	FAT
	Domain	2322 – 2567	246	PI3K/PI4K
	Domain	2612 – 2644	33	FATC
Amino acid modifications
	Modified residue	428	1	Phosphoserine Ref.36
	Modified residue	1989	1	Phosphothreonine Ref.36
Natural variations
	Alternative sequence	450	1	E → D in isoform 2.		VSP_013305
	Alternative sequence	451 – 514	64	Missing in isoform 2.		VSP_013304
	Alternative sequence	2588 – 2610	23	AKTHV…RNRVT → VSRRYSLIWAVVLISTNELD MQL in isoform 3.		VSP_036907
	Alternative sequence	2611 – 2644	34	Missing in isoform 3.		VSP_036908
	Natural variant	64	1	T → A. Ref.43 Corresponds to variant rs35306038 [ dbSNP | Ensembl ].		VAR_041584
	Natural variant	90	1	H → Y. Ref.43 Corresponds to variant rs28897763 [ dbSNP | Ensembl ].		VAR_041585
	Natural variant	211	1	M → T. Corresponds to variant rs2227928 [ dbSNP | Ensembl ].		VAR_050532
	Natural variant	297	1	K → N. Ref.43 Corresponds to variant rs2229033 [ dbSNP | Ensembl ].		VAR_041586
	Natural variant	316	1	V → I. Ref.43 Corresponds to variant rs28897764 [ dbSNP | Ensembl ].		VAR_041587
	Natural variant	959	1	V → M. Ref.43 Corresponds to variant rs28910271 [ dbSNP | Ensembl ].		VAR_041588
	Natural variant	1087	1	Y → H. Ref.43 Corresponds to variant rs34253059 [ dbSNP | Ensembl ].		VAR_041589
	Natural variant	1213	1	S → G. Ref.43 Corresponds to variant rs34766606 [ dbSNP | Ensembl ].		VAR_041590
	Natural variant	1488	1	A → P in a lung squamous cell carcinoma sample; somatic mutation. Ref.43		VAR_041591
	Natural variant	1526	1	I → V. Corresponds to variant rs34124242 [ dbSNP | Ensembl ].		VAR_050533
	Natural variant	1607	1	S → N. Ref.43 Corresponds to variant rs55724025 [ dbSNP | Ensembl ].		VAR_041592
	Natural variant	1612	1	N → S. Ref.43 Corresponds to variant rs55894265 [ dbSNP | Ensembl ].		VAR_041593
	Natural variant	2002	1	A → G in a lung adenocarcinoma sample; somatic mutation. Ref.43		VAR_041594
	Natural variant	2120	1	G → A. Ref.43 Corresponds to variant rs35134774 [ dbSNP | Ensembl ].		VAR_041595
	Natural variant	2132	1	Y → D. Ref.43 Corresponds to variant rs28910273 [ dbSNP | Ensembl ].		VAR_041596
	Natural variant	2144	1	Q → R in FCTCS. Ref.44		VAR_067919
	Natural variant	2233	1	S → I in a lung large cell carcinoma sample; somatic mutation. Ref.43		VAR_041597
	Natural variant	2425	1	R → Q. Ref.43 Corresponds to variant rs2229032 [ dbSNP | Ensembl ].		VAR_041598
	Natural variant	2434	1	P → A. Ref.43 Corresponds to variant rs33972295 [ dbSNP | Ensembl ].		VAR_041599
	Natural variant	2438	1	E → K in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.43		VAR_041600
	Natural variant	2537	1	E → Q in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.43		VAR_041601
Experimental info
	Mutagenesis	2327	1	K → R: Abolishes kinase activity. Ref.10 Ref.14 Ref.20
	Mutagenesis	2475	1	D → A: Abolishes kinase activity; increases sensitivity to IR and impairs translocation to nuclear foci upon DNA damage. Ref.7 Ref.10 Ref.21
	Mutagenesis	2494	1	D → E: Abolishes kinase activity; reduces cell viability, augments sensitivity to IR and UV. Ref.8 Ref.12
	Sequence conflict	92	1	A → R in CAA70298. Ref.1
	Sequence conflict	92	1	A → R in AAC50929. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 3. Checksum: 11BC22297FB9A802	FASTA	2,644	301,367
	10 20 30 40 50 60 MGEHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV VAVELVKKTD 70 80 90 100 110 120 SQPTSVMLLD FIQHIMKSSP LMFVNVSGSH EAKGSCIEFS NWIITRLLRI AATPSCHLLH 130 140 150 160 170 180 KKICEVICSL LFLFKSKSPA IFGVLTKELL QLFEDLVYLH RRNVMGHAVE WPVVMSRFLS 190 200 210 220 230 240 QLDEHMGYLQ SAPLQLMSMQ NLEFIEVTLL MVLTRIIAIV FFRRQELLLW QIGCVLLEYG 250 260 270 280 290 300 SPKIKSLAIS FLTELFQLGG LPAQPASTFF SSFLELLKHL VEMDTDQLKL YEEPLSKLIK 310 320 330 340 350 360 TLFPFEAEAY RNIEPVYLNM LLEKLCVMFE DGVLMRLKSD LLKAALCHLL QYFLKFVPAG 370 380 390 400 410 420 YESALQVRKV YVRNICKALL DVLGIEVDAE YLLGPLYAAL KMESMEIIEE IQCQTQQENL 430 440 450 460 470 480 SSNSDGISPK RRRLSSSLNP SKRAPKQTEE IKHVDMNQKS ILWSALKQKA ESLQISLEYS 490 500 510 520 530 540 GLKNPVIEML EGIAVVLQLT ALCTVHCSHQ NMNCRTFKDC QHKSKKKPSV VITWMSLDFY 550 560 570 580 590 600 TKVLKSCRSL LESVQKLDLE ATIDKVVKIY DALIYMQVNS SFEDHILEDL CGMLSLPWIY 610 620 630 640 650 660 SHSDDGCLKL TTFAANLLTL SCRISDSYSP QAQSRCVFLL TLFPRRIFLE WRTAVYNWAL 670 680 690 700 710 720 QSSHEVIRAS CVSGFFILLQ QQNSCNRVPK ILIDKVKDDS DIVKKEFASI LGQLVCTLHG 730 740 750 760 770 780 MFYLTSSLTE PFSEHGHVDL FCRNLKATSQ HECSSSQLKA SVCKPFLFLL KKKIPSPVKL 790 800 810 820 830 840 AFIDNLHHLC KHLDFREDET DVKAVLGTLL NLMEDPDKDV RVAFSGNIKH ILESLDSEDG 850 860 870 880 890 900 FIKELFVLRM KEAYTHAQIS RNNELKDTLI LTTGDIGRAA KGDLVPFALL HLLHCLLSKS 910 920 930 940 950 960 ASVSGAAYTE IRALVAAKSV KLQSFFSQYK KPICQFLVES LHSSQMTALP NTPCQNADVR 970 980 990 1000 1010 1020 KQDVAHQREM ALNTLSEIAN VFDFPDLNRF LTRTLQVLLP DLAAKASPAA SALIRTLGKQ 1030 1040 1050 1060 1070 1080 LNVNRREILI NNFKYIFSHL VCSCSKDELE RALHYLKNET EIELGSLLRQ DFQGLHNELL 1090 1100 1110 1120 1130 1140 LRIGEHYQQV FNGLSILASF ASSDDPYQGP RDIISPELMA DYLQPKLLGI LAFFNMQLLS 1150 1160 1170 1180 1190 1200 SSVGIEDKKM ALNSLMSLMK LMGPKHVSSV RVKMMTTLRT GLRFKDDFPE LCCRAWDCFV 1210 1220 1230 1240 1250 1260 RCLDHACLGS LLSHVIVALL PLIHIQPKET AAIFHYLIIE NRDAVQDFLH EIYFLPDHPE 1270 1280 1290 1300 1310 1320 LKKIKAVLQE YRKETSESTD LQTTLQLSMK AIQHENVDVR IHALTSLKET LYKNQEKLIK 1330 1340 1350 1360 1370 1380 YATDSETVEP IISQLVTVLL KGCQDANSQA RLLCGECLGE LGAIDPGRLD FSTTETQGKD 1390 1400 1410 1420 1430 1440 FTFVTGVEDS SFAYGLLMEL TRAYLAYADN SRAQDSAAYA IQELLSIYDC REMETNGPGH 1450 1460 1470 1480 1490 1500 QLWRRFPEHV REILEPHLNT RYKSSQKSTD WSGVKKPIYL SKLGSNFAEW SASWAGYLIT 1510 1520 1530 1540 1550 1560 KVRHDLASKI FTCCSIMMKH DFKVTIYLLP HILVYVLLGC NQEDQQEVYA EIMAVLKHDD 1570 1580 1590 1600 1610 1620 QHTINTQDIA SDLCQLSTQT VFSMLDHLTQ WARHKFQALK AEKCPHSKSN RNKVDSMVST 1630 1640 1650 1660 1670 1680 VDYEDYQSVT RFLDLIPQDT LAVASFRSKA YTRAVMHFES FITEKKQNIQ EHLGFLQKLY 1690 1700 1710 1720 1730 1740 AAMHEPDGVA GVSAIRKAEP SLKEQILEHE SLGLLRDATA CYDRAIQLEP DQIIHYHGVV 1750 1760 1770 1780 1790 1800 KSMLGLGQLS TVITQVNGVH ANRSEWTDEL NTYRVEAAWK LSQWDLVENY LAADGKSTTW 1810 1820 1830 1840 1850 1860 SVRLGQLLLS AKKRDITAFY DSLKLVRAEQ IVPLSAASFE RGSYQRGYEY IVRLHMLCEL 1870 1880 1890 1900 1910 1920 EHSIKPLFQH SPGDSSQEDS LNWVARLEMT QNSYRAKEPI LALRRALLSL NKRPDYNEMV 1930 1940 1950 1960 1970 1980 GECWLQSARV ARKAGHHQTA YNALLNAGES RLAELYVERA KWLWSKGDVH QALIVLQKGV 1990 2000 2010 2020 2030 2040 ELCFPENETP PEGKNMLIHG RAMLLVGRFM EETANFESNA IMKKYKDVTA CLPEWEDGHF 2050 2060 2070 2080 2090 2100 YLAKYYDKLM PMVTDNKMEK QGDLIRYIVL HFGRSLQYGN QFIYQSMPRM LTLWLDYGTK 2110 2120 2130 2140 2150 2160 AYEWEKAGRS DRVQMRNDLG KINKVITEHT NYLAPYQFLT AFSQLISRIC HSHDEVFVVL 2170 2180 2190 2200 2210 2220 MEIIAKVFLA YPQQAMWMMT AVSKSSYPMR VNRCKEILNK AIHMKKSLEK FVGDATRLTD 2230 2240 2250 2260 2270 2280 KLLELCNKPV DGSSSTLSMS THFKMLKKLV EEATFSEILI PLQSVMIPTL PSILGTHANH 2290 2300 2310 2320 2330 2340 ASHEPFPGHW AYIAGFDDMV EILASLQKPK KISLKGSDGK FYIMMCKPKD DLRKDCRLME 2350 2360 2370 2380 2390 2400 FNSLINKCLR KDAESRRREL HIRTYAVIPL NDECGIIEWV NNTAGLRPIL TKLYKEKGVY 2410 2420 2430 2440 2450 2460 MTGKELRQCM LPKSAALSEK LKVFREFLLP RHPPIFHEWF LRTFPDPTSW YSSRSAYCRS 2470 2480 2490 2500 2510 2520 TAVMSMVGYI LGLGDRHGEN ILFDSLTGEC VHVDFNCLFN KGETFEVPEI VPFRLTHNMV 2530 2540 2550 2560 2570 2580 NGMGPMGTEG LFRRACEVTM RLMRDQREPL MSVLKTFLHD PLVEWSKPVK GHSKAPLNET 2590 2600 2610 2620 2630 2640 GEVVNEKAKT HVLDIEQRLQ GVIKTRNRVT GLPLSIEGHV HYLIQEATDE NLLCQMYLGW TPYM
	Isoform 2 [UniParc]. Checksum: A7C5CED46708FC16	FASTA	2,580	294,219
	10 20 30 40 50 60 MGEHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV VAVELVKKTD 70 80 90 100 110 120 SQPTSVMLLD FIQHIMKSSP LMFVNVSGSH EAKGSCIEFS NWIITRLLRI AATPSCHLLH 130 140 150 160 170 180 KKICEVICSL LFLFKSKSPA IFGVLTKELL QLFEDLVYLH RRNVMGHAVE WPVVMSRFLS 190 200 210 220 230 240 QLDEHMGYLQ SAPLQLMSMQ NLEFIEVTLL MVLTRIIAIV FFRRQELLLW QIGCVLLEYG 250 260 270 280 290 300 SPKIKSLAIS FLTELFQLGG LPAQPASTFF SSFLELLKHL VEMDTDQLKL YEEPLSKLIK 310 320 330 340 350 360 TLFPFEAEAY RNIEPVYLNM LLEKLCVMFE DGVLMRLKSD LLKAALCHLL QYFLKFVPAG 370 380 390 400 410 420 YESALQVRKV YVRNICKALL DVLGIEVDAE YLLGPLYAAL KMESMEIIEE IQCQTQQENL 430 440 450 460 470 480 SSNSDGISPK RRRLSSSLNP SKRAPKQTED RTFKDCQHKS KKKPSVVITW MSLDFYTKVL 490 500 510 520 530 540 KSCRSLLESV QKLDLEATID KVVKIYDALI YMQVNSSFED HILEDLCGML SLPWIYSHSD 550 560 570 580 590 600 DGCLKLTTFA ANLLTLSCRI SDSYSPQAQS RCVFLLTLFP RRIFLEWRTA VYNWALQSSH 610 620 630 640 650 660 EVIRASCVSG FFILLQQQNS CNRVPKILID KVKDDSDIVK KEFASILGQL VCTLHGMFYL 670 680 690 700 710 720 TSSLTEPFSE HGHVDLFCRN LKATSQHECS SSQLKASVCK PFLFLLKKKI PSPVKLAFID 730 740 750 760 770 780 NLHHLCKHLD FREDETDVKA VLGTLLNLME DPDKDVRVAF SGNIKHILES LDSEDGFIKE 790 800 810 820 830 840 LFVLRMKEAY THAQISRNNE LKDTLILTTG DIGRAAKGDL VPFALLHLLH CLLSKSASVS 850 860 870 880 890 900 GAAYTEIRAL VAAKSVKLQS FFSQYKKPIC QFLVESLHSS QMTALPNTPC QNADVRKQDV 910 920 930 940 950 960 AHQREMALNT LSEIANVFDF PDLNRFLTRT LQVLLPDLAA KASPAASALI RTLGKQLNVN 970 980 990 1000 1010 1020 RREILINNFK YIFSHLVCSC SKDELERALH YLKNETEIEL GSLLRQDFQG LHNELLLRIG 1030 1040 1050 1060 1070 1080 EHYQQVFNGL SILASFASSD DPYQGPRDII SPELMADYLQ PKLLGILAFF NMQLLSSSVG 1090 1100 1110 1120 1130 1140 IEDKKMALNS LMSLMKLMGP KHVSSVRVKM MTTLRTGLRF KDDFPELCCR AWDCFVRCLD 1150 1160 1170 1180 1190 1200 HACLGSLLSH VIVALLPLIH IQPKETAAIF HYLIIENRDA VQDFLHEIYF LPDHPELKKI 1210 1220 1230 1240 1250 1260 KAVLQEYRKE TSESTDLQTT LQLSMKAIQH ENVDVRIHAL TSLKETLYKN QEKLIKYATD 1270 1280 1290 1300 1310 1320 SETVEPIISQ LVTVLLKGCQ DANSQARLLC GECLGELGAI DPGRLDFSTT ETQGKDFTFV 1330 1340 1350 1360 1370 1380 TGVEDSSFAY GLLMELTRAY LAYADNSRAQ DSAAYAIQEL LSIYDCREME TNGPGHQLWR 1390 1400 1410 1420 1430 1440 RFPEHVREIL EPHLNTRYKS SQKSTDWSGV KKPIYLSKLG SNFAEWSASW AGYLITKVRH 1450 1460 1470 1480 1490 1500 DLASKIFTCC SIMMKHDFKV TIYLLPHILV YVLLGCNQED QQEVYAEIMA VLKHDDQHTI 1510 1520 1530 1540 1550 1560 NTQDIASDLC QLSTQTVFSM LDHLTQWARH KFQALKAEKC PHSKSNRNKV DSMVSTVDYE 1570 1580 1590 1600 1610 1620 DYQSVTRFLD LIPQDTLAVA SFRSKAYTRA VMHFESFITE KKQNIQEHLG FLQKLYAAMH 1630 1640 1650 1660 1670 1680 EPDGVAGVSA IRKAEPSLKE QILEHESLGL LRDATACYDR AIQLEPDQII HYHGVVKSML 1690 1700 1710 1720 1730 1740 GLGQLSTVIT QVNGVHANRS EWTDELNTYR VEAAWKLSQW DLVENYLAAD GKSTTWSVRL 1750 1760 1770 1780 1790 1800 GQLLLSAKKR DITAFYDSLK LVRAEQIVPL SAASFERGSY QRGYEYIVRL HMLCELEHSI 1810 1820 1830 1840 1850 1860 KPLFQHSPGD SSQEDSLNWV ARLEMTQNSY RAKEPILALR RALLSLNKRP DYNEMVGECW 1870 1880 1890 1900 1910 1920 LQSARVARKA GHHQTAYNAL LNAGESRLAE LYVERAKWLW SKGDVHQALI VLQKGVELCF 1930 1940 1950 1960 1970 1980 PENETPPEGK NMLIHGRAML LVGRFMEETA NFESNAIMKK YKDVTACLPE WEDGHFYLAK 1990 2000 2010 2020 2030 2040 YYDKLMPMVT DNKMEKQGDL IRYIVLHFGR SLQYGNQFIY QSMPRMLTLW LDYGTKAYEW 2050 2060 2070 2080 2090 2100 EKAGRSDRVQ MRNDLGKINK VITEHTNYLA PYQFLTAFSQ LISRICHSHD EVFVVLMEII 2110 2120 2130 2140 2150 2160 AKVFLAYPQQ AMWMMTAVSK SSYPMRVNRC KEILNKAIHM KKSLEKFVGD ATRLTDKLLE 2170 2180 2190 2200 2210 2220 LCNKPVDGSS STLSMSTHFK MLKKLVEEAT FSEILIPLQS VMIPTLPSIL GTHANHASHE 2230 2240 2250 2260 2270 2280 PFPGHWAYIA GFDDMVEILA SLQKPKKISL KGSDGKFYIM MCKPKDDLRK DCRLMEFNSL 2290 2300 2310 2320 2330 2340 INKCLRKDAE SRRRELHIRT YAVIPLNDEC GIIEWVNNTA GLRPILTKLY KEKGVYMTGK 2350 2360 2370 2380 2390 2400 ELRQCMLPKS AALSEKLKVF REFLLPRHPP IFHEWFLRTF PDPTSWYSSR SAYCRSTAVM 2410 2420 2430 2440 2450 2460 SMVGYILGLG DRHGENILFD SLTGECVHVD FNCLFNKGET FEVPEIVPFR LTHNMVNGMG 2470 2480 2490 2500 2510 2520 PMGTEGLFRR ACEVTMRLMR DQREPLMSVL KTFLHDPLVE WSKPVKGHSK APLNETGEVV 2530 2540 2550 2560 2570 2580 NEKAKTHVLD IEQRLQGVIK TRNRVTGLPL SIEGHVHYLI QEATDENLLC QMYLGWTPYM
	Isoform 3 [UniParc]. Checksum: 44281024A65D73B1	FASTA	2,610	297,479
	10 20 30 40 50 60 MGEHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV VAVELVKKTD 70 80 90 100 110 120 SQPTSVMLLD FIQHIMKSSP LMFVNVSGSH EAKGSCIEFS NWIITRLLRI AATPSCHLLH 130 140 150 160 170 180 KKICEVICSL LFLFKSKSPA IFGVLTKELL QLFEDLVYLH RRNVMGHAVE WPVVMSRFLS 190 200 210 220 230 240 QLDEHMGYLQ SAPLQLMSMQ NLEFIEVTLL MVLTRIIAIV FFRRQELLLW QIGCVLLEYG 250 260 270 280 290 300 SPKIKSLAIS FLTELFQLGG LPAQPASTFF SSFLELLKHL VEMDTDQLKL YEEPLSKLIK 310 320 330 340 350 360 TLFPFEAEAY RNIEPVYLNM LLEKLCVMFE DGVLMRLKSD LLKAALCHLL QYFLKFVPAG 370 380 390 400 410 420 YESALQVRKV YVRNICKALL DVLGIEVDAE YLLGPLYAAL KMESMEIIEE IQCQTQQENL 430 440 450 460 470 480 SSNSDGISPK RRRLSSSLNP SKRAPKQTEE IKHVDMNQKS ILWSALKQKA ESLQISLEYS 490 500 510 520 530 540 GLKNPVIEML EGIAVVLQLT ALCTVHCSHQ NMNCRTFKDC QHKSKKKPSV VITWMSLDFY 550 560 570 580 590 600 TKVLKSCRSL LESVQKLDLE ATIDKVVKIY DALIYMQVNS SFEDHILEDL CGMLSLPWIY 610 620 630 640 650 660 SHSDDGCLKL TTFAANLLTL SCRISDSYSP QAQSRCVFLL TLFPRRIFLE WRTAVYNWAL 670 680 690 700 710 720 QSSHEVIRAS CVSGFFILLQ QQNSCNRVPK ILIDKVKDDS DIVKKEFASI LGQLVCTLHG 730 740 750 760 770 780 MFYLTSSLTE PFSEHGHVDL FCRNLKATSQ HECSSSQLKA SVCKPFLFLL KKKIPSPVKL 790 800 810 820 830 840 AFIDNLHHLC KHLDFREDET DVKAVLGTLL NLMEDPDKDV RVAFSGNIKH ILESLDSEDG 850 860 870 880 890 900 FIKELFVLRM KEAYTHAQIS RNNELKDTLI LTTGDIGRAA KGDLVPFALL HLLHCLLSKS 910 920 930 940 950 960 ASVSGAAYTE IRALVAAKSV KLQSFFSQYK KPICQFLVES LHSSQMTALP NTPCQNADVR 970 980 990 1000 1010 1020 KQDVAHQREM ALNTLSEIAN VFDFPDLNRF LTRTLQVLLP DLAAKASPAA SALIRTLGKQ 1030 1040 1050 1060 1070 1080 LNVNRREILI NNFKYIFSHL VCSCSKDELE RALHYLKNET EIELGSLLRQ DFQGLHNELL 1090 1100 1110 1120 1130 1140 LRIGEHYQQV FNGLSILASF ASSDDPYQGP RDIISPELMA DYLQPKLLGI LAFFNMQLLS 1150 1160 1170 1180 1190 1200 SSVGIEDKKM ALNSLMSLMK LMGPKHVSSV RVKMMTTLRT GLRFKDDFPE LCCRAWDCFV 1210 1220 1230 1240 1250 1260 RCLDHACLGS LLSHVIVALL PLIHIQPKET AAIFHYLIIE NRDAVQDFLH EIYFLPDHPE 1270 1280 1290 1300 1310 1320 LKKIKAVLQE YRKETSESTD LQTTLQLSMK AIQHENVDVR IHALTSLKET LYKNQEKLIK 1330 1340 1350 1360 1370 1380 YATDSETVEP IISQLVTVLL KGCQDANSQA RLLCGECLGE LGAIDPGRLD FSTTETQGKD 1390 1400 1410 1420 1430 1440 FTFVTGVEDS SFAYGLLMEL TRAYLAYADN SRAQDSAAYA IQELLSIYDC REMETNGPGH 1450 1460 1470 1480 1490 1500 QLWRRFPEHV REILEPHLNT RYKSSQKSTD WSGVKKPIYL SKLGSNFAEW SASWAGYLIT 1510 1520 1530 1540 1550 1560 KVRHDLASKI FTCCSIMMKH DFKVTIYLLP HILVYVLLGC NQEDQQEVYA EIMAVLKHDD 1570 1580 1590 1600 1610 1620 QHTINTQDIA SDLCQLSTQT VFSMLDHLTQ WARHKFQALK AEKCPHSKSN RNKVDSMVST 1630 1640 1650 1660 1670 1680 VDYEDYQSVT RFLDLIPQDT LAVASFRSKA YTRAVMHFES FITEKKQNIQ EHLGFLQKLY 1690 1700 1710 1720 1730 1740 AAMHEPDGVA GVSAIRKAEP SLKEQILEHE SLGLLRDATA CYDRAIQLEP DQIIHYHGVV 1750 1760 1770 1780 1790 1800 KSMLGLGQLS TVITQVNGVH ANRSEWTDEL NTYRVEAAWK LSQWDLVENY LAADGKSTTW 1810 1820 1830 1840 1850 1860 SVRLGQLLLS AKKRDITAFY DSLKLVRAEQ IVPLSAASFE RGSYQRGYEY IVRLHMLCEL 1870 1880 1890 1900 1910 1920 EHSIKPLFQH SPGDSSQEDS LNWVARLEMT QNSYRAKEPI LALRRALLSL NKRPDYNEMV 1930 1940 1950 1960 1970 1980 GECWLQSARV ARKAGHHQTA YNALLNAGES RLAELYVERA KWLWSKGDVH QALIVLQKGV 1990 2000 2010 2020 2030 2040 ELCFPENETP PEGKNMLIHG RAMLLVGRFM EETANFESNA IMKKYKDVTA CLPEWEDGHF 2050 2060 2070 2080 2090 2100 YLAKYYDKLM PMVTDNKMEK QGDLIRYIVL HFGRSLQYGN QFIYQSMPRM LTLWLDYGTK 2110 2120 2130 2140 2150 2160 AYEWEKAGRS DRVQMRNDLG KINKVITEHT NYLAPYQFLT AFSQLISRIC HSHDEVFVVL 2170 2180 2190 2200 2210 2220 MEIIAKVFLA YPQQAMWMMT AVSKSSYPMR VNRCKEILNK AIHMKKSLEK FVGDATRLTD 2230 2240 2250 2260 2270 2280 KLLELCNKPV DGSSSTLSMS THFKMLKKLV EEATFSEILI PLQSVMIPTL PSILGTHANH 2290 2300 2310 2320 2330 2340 ASHEPFPGHW AYIAGFDDMV EILASLQKPK KISLKGSDGK FYIMMCKPKD DLRKDCRLME 2350 2360 2370 2380 2390 2400 FNSLINKCLR KDAESRRREL HIRTYAVIPL NDECGIIEWV NNTAGLRPIL TKLYKEKGVY 2410 2420 2430 2440 2450 2460 MTGKELRQCM LPKSAALSEK LKVFREFLLP RHPPIFHEWF LRTFPDPTSW YSSRSAYCRS 2470 2480 2490 2500 2510 2520 TAVMSMVGYI LGLGDRHGEN ILFDSLTGEC VHVDFNCLFN KGETFEVPEI VPFRLTHNMV 2530 2540 2550 2560 2570 2580 NGMGPMGTEG LFRRACEVTM RLMRDQREPL MSVLKTFLHD PLVEWSKPVK GHSKAPLNET 2590 2600 2610 GEVVNEKVSR RYSLIWAVVL ISTNELDMQL

References

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[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2155-2644 (ISOFORM 3). Tissue: Brain.
[5]	"The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes." Keegan K.S., Holtzman D.A., Plug A.W., Christenson E.R., Brainerd E.E., Flaggs G., Bentley N.J., Taylor E.M., Meyn M.S., Moss S.B., Carr A.M., Ashley T., Hoekstra M.F. Genes Dev. 10:2423-2437(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
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[8]	"Protein kinase mutants of human ATR increase sensitivity to UV and ionizing radiation and abrogate cell cycle checkpoint control." Wright J.A., Keegan K.S., Herendeen D.R., Bentley N.J., Carr A.M., Hoekstra M.F., Concannon P. Proc. Natl. Acad. Sci. U.S.A. 95:7445-7450(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-2494.
[9]	"Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4." Schmidt D.R., Schreiber S.L. Biochemistry 38:14711-14717(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HDAC2, IDENTIFICATION IN A COMPLEX CONTAINING HDAC2 AND CHD4.
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[11]	"Substrate specificities and identification of putative substrates of ATM kinase family members." Kim S.-T., Lim D.-S., Canman C.E., Kastan M.B. J. Biol. Chem. 274:37538-37543(1999) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR, FUNCTION.
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[13]	"Chk1 is an essential kinase that is regulated by Atr and required for the G(2)/M DNA damage checkpoint." Liu Q., Guntuku S., Cui X.-S., Matsuoka S., Cortez D., Tamai K., Luo G., Carattini-Rivera S., DeMayo F., Bradley A., Donehower L.A., Elledge S.J. Genes Dev. 14:1448-1459(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
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[16]	"ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses." Bao S., Tibbetts R.S., Brumbaugh K.M., Fang Y., Richardson D.A., Ali A., Chen S.M., Abraham R.T., Wang X.-F. Nature 411:969-974(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAD17.
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[19]	"Hypoxia links ATR and p53 through replication arrest." Hammond E.M., Denko N.C., Dorie M.J., Abraham R.T., Giaccia A.J. Mol. Cell. Biol. 22:1834-1843(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]	"Preferential binding of ATR protein to UV-damaged DNA." Uensal-Kacmaz K., Makhov A.M., Griffith J.D., Sancar A. Proc. Natl. Acad. Sci. U.S.A. 99:6673-6678(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, MUTAGENESIS OF LYS-2327.
[21]	"ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation." Barr S.M., Leung C.G., Chang E.E., Cimprich K.A. Curr. Biol. 13:1047-1051(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-2475.
[22]	"Human claspin is required for replication checkpoint control." Chini C.C.S., Chen J. J. Biol. Chem. 278:30057-30062(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CLSPN.
[23]	"MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation." Wang Y., Qin J. Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MSH2, MASS SPECTROMETRY.
[24]	"Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes." Zou L., Elledge S.J. Science 300:1542-1548(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH RPA AND ATRIP.
[25]	"BCR/ABL translocates to the nucleus and disrupts an ATR-dependent intra-S phase checkpoint." Dierov J., Dierova R., Carroll M. Cancer Cell 5:275-285(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BCR-ABL.
[26]	"UV-induced ataxia-telangiectasia-mutated and Rad3-related (ATR) activation requires replication stress." Ward I.M., Minn K., Chen J. J. Biol. Chem. 279:9677-9680(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[27]	"Recruitment of the cell cycle checkpoint kinase ATR to chromatin during S-phase." Dart D.A., Adams K.E., Akerman I., Lakin N.D. J. Biol. Chem. 279:16433-16440(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, SUBCELLULAR LOCATION.
[28]	"ATR couples FANCD2 monoubiquitination to the DNA-damage response." Andreassen P.R., D'Andrea A.D., Taniguchi T. Genes Dev. 18:1958-1963(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[29]	"Seckel syndrome exhibits cellular features demonstrating defects in the ATR-signalling pathway." Alderton G.K., Joenje H., Varon R., Borglum A.D., Jeggo P.A., O'Driscoll M. Hum. Mol. Genet. 13:3127-3138(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[30]	"Quaternary structure of ATR and effects of ATRIP and replication protein A on its DNA binding and kinase activities." Uensal-Kacmaz K., Sancar A. Mol. Cell. Biol. 24:1292-1300(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH ATRIP AND RPA1, DNA-BINDING, ENZYME REGULATION.
[31]	"Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases." Cortez D., Glick G., Elledge S.J. Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[32]	"The haploinsufficient tumor suppressor p18 upregulates p53 via interactions with ATM/ATR." Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H., Choi Y.H., Choi D., Lee K.S., Kim S. Cell 120:209-221(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EEF1E1.
[33]	"Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage." Falck J., Coates J., Jackson S.P. Nature 434:605-611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATRIP.
[34]	"Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1." Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y. Genes Dev. 22:587-600(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CEP164, SUBCELLULAR LOCATION.
[35]	"A splicing mutation affecting expression of ataxia-telangiectasia and Rad3-related protein (ATR) results in Seckel syndrome." O'Driscoll M., Ruiz-Perez V.L., Woods C.G., Jeggo P.A., Goodship J.A. Nat. Genet. 33:497-501(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SCKL1.
[36]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND THR-1989, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[38]	"A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability." Hurov K.E., Cotta-Ramusino C., Elledge S.J. Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TTI1.
[39]	"Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes." Takai H., Xie Y., de Lange T., Pavletich N.P. Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TELO2.
[40]	"Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly." Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N. J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TELO2 AND TTI1.
[41]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-64; TYR-90; ASN-297; ILE-316; MET-959; HIS-1087; GLY-1213; PRO-1488; ASN-1607; SER-1612; GLY-2002; ALA-2120; ASP-2132; ILE-2233; GLN-2425; ALA-2434; LYS-2438 AND GLN-2537.
[44]	"Germline mutation in ATR in autosomal- dominant oropharyngeal cancer syndrome." Tanaka A., Weinel S., Nagy N., O'Driscoll M., Lai-Cheong J.E., Kulp-Shorten C.L., Knable A., Carpenter G., Fisher S.A., Hiragun M., Yanase Y., Hide M., Callen J., McGrath J.A. Am. J. Hum. Genet. 90:511-517(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FCTCS ARG-2144.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00412298. IPI00554573. IPI00926461.
RefSeq	NP_001175.2. NM_001184.3.
UniGene	Hs.271791.
3D structure databases
ProteinModelPortal	Q13535.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35308N.
IntAct	Q13535. 10 interactions.
MINT	MINT-194575.
STRING	9606.ENSP00000343741.
PTM databases
PhosphoSite	Q13535.
Polymorphism databases
DMDM	62286460.
Proteomic databases
PaxDb	Q13535.
PRIDE	Q13535.
Protocols and materials databases
DNASU	545.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000350721; ENSP00000343741; ENSG00000175054. ENST00000383101; ENSP00000372581; ENSG00000175054.
GeneID	545.
KEGG	hsa:545.
UCSC	uc003eux.4. human.
Organism-specific databases
CTD	545.
GeneCards	GC03M142168.
H-InvDB	HIX0030886.
HGNC	HGNC:882. ATR.
HPA	HPA028264.
MIM	210600. phenotype. 601215. gene. 614564. phenotype.
neXtProt	NX_Q13535.
Orphanet	808. Seckel syndrome.
PharmGKB	PA74.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5032.
HOGENOM	HOG000034221.
HOVERGEN	HBG050619.
InParanoid	Q13535.
KO	K06640.
OMA	AIQHENV.
OrthoDB	EOG48GW2C.
PhylomeDB	Q13535.
Enzyme and pathway databases
Pathway_Interaction_DB	bard1pathway. BARD1 signaling events. circadianpathway. Circadian rhythm pathway.
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q13535.
Bgee	Q13535.
CleanEx	HS_ATR.
Genevestigator	Q13535.
GermOnline	ENSG00000175054. Homo sapiens.
Family and domain databases
Gene3D	1.10.1070.11. 2 hits. 1.25.10.10. 4 hits. 1.25.40.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR003152. FATC. 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. IPR012993. UME. [Graphical view]
Pfam	PF02259. FAT. 1 hit. PF02260. FATC. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. PF08064. UME. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. SM00802. UME. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS50077. HEAT_REPEAT. 1 hit. PS00915. PI3_4_KINASE_1. False negative. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q13535.
ChEMBL	CHEMBL5024.
ChiTaRS	ATR. human.
GenomeRNAi	545.
NextBio	2253.
SOURCE	Search...

Entry information

Entry name

ATR_HUMAN

Accession

Primary (citable) accession number: Q13535
Secondary accession number(s): Q59HB2 , Q7KYL3, Q93051, Q9BXK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.