Q62388 (ATM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine-protein kinase ATM
EC=2.7.11.1

Alternative name(s):
Ataxia telangiectasia mutated homolog
Short name=A-T mutated homolog

Gene names

Name:

Atm

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	3066 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine protein kinase which 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. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Ref.6 Ref.7 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Inhibited by wortmannin By similarity.
Subunit structure	Dimers or tetramers in inactive state. On DNA damage, autophosphorylation dissociates ATM into monomers rendering them catalytically active. Binds DNA ends, p53/TP53, ABL1, BRCA1, NBN/nibrin and TERF1. 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. Interacts with EEF1E1; the interaction, induced on DNA damage, up-regulates TP53. Interacts with DCLRE1C, MYST1, KAT5, NABP2, ATMIN and CEP164 By similarity. Interacts with AP2B1 AND AP3B2; the interaction occurs in cytoplasmic vesicles. Interacts with TELO2 AND TTI1. Interacts with DDX1 By similarity. Ref.5
Subcellular location	Nucleus By similarity. Cytoplasmic vesicle By similarity. Note: Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin By similarity. Ref.3
Tissue specificity	Expressed in brain, skeletal muscle, testis, followed by spleen, lung, kidney, heart, liver and thymus. Ubiquitously expressed in embryonal tissues.
Developmental stage	Highest expression in embryonic central nervous system, from E13.5 day and during the whole cerebellar development. Decreased expression when maturation occurs. Ref.4
Domain	The FATC domain is required for interaction with KAT5 By similarity.
Post-translational modification	Phosphorylated by NUAK1/ARK5 By similarity. Autophosphorylation on Ser-367, Ser-1899, Ser-1987 correlates with DNA damage-mediated activation of the kinase. Ref.7 Acetylated by KAT5 upon DNA damage; which is required for autophosphorylation and subsequent activation By similarity.
Involvement in disease	Atm-deficient mice show a phenotype similar to human ataxia telangiectasia (AT) and consistently develop immature T-cells malignancies. Ref.7
Sequence similarities	Belongs to the PI3/PI4-kinase family. ATM subfamily. Contains 1 FAT domain. Contains 1 FATC domain. Contains 1 PI3K/PI4K domain.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Cytoplasmic vesicle Nucleus
Disease	Tumor suppressor
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from mutant phenotype PubMed 12937170. Source: MGI DNA damage induced protein phosphorylation Inferred from electronic annotation. Source: Compara DNA repair Inferred from direct assay PubMed 15364958. Source: MGI G2 DNA damage checkpoint Inferred from electronic annotation. Source: Compara brain development Inferred from genetic interaction PubMed 16687486. Source: MGI cell cycle arrest Inferred from electronic annotation. Source: Compara cellular response to gamma radiation Inferred from electronic annotation. Source: Compara female gamete generation Inferred from mutant phenotype PubMed 15640358. Source: MGI heart development Inferred from genetic interaction PubMed 16687486. Source: MGI histone mRNA catabolic process Inferred from sequence or structural similarity. Source: UniProtKB intrinsic apoptotic signaling pathway in response to DNA damage Inferred from mutant phenotype PubMed 11040211PubMed 16777961. Source: MGI lipoprotein catabolic process Inferred from genetic interaction PubMed 15863839. Source: MGI mitotic spindle assembly checkpoint Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of B cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from mutant phenotype PubMed 11536012. Source: MGI neuron apoptotic process Inferred from genetic interaction PubMed 11248063. Source: MGI positive regulation of DNA damage response, signal transduction by p53 class mediator Inferred from electronic annotation. Source: Compara positive regulation of neuron apoptotic process Inferred from genetic interaction PubMed 10639175PubMed 16777961. Source: MGI pre-B cell allelic exclusion Inferred from mutant phenotype Ref.8. Source: UniProtKB protein autophosphorylation Inferred from electronic annotation. Source: Compara replicative senescence Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from sequence or structural similarity. Source: UniProtKB somitogenesis Inferred from genetic interaction PubMed 16687486. Source: MGI telomere maintenance Inferred from electronic annotation. Source: InterPro
Cellular_component	chromosome, telomeric region Inferred from electronic annotation. Source: Compara cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome spindle Inferred from direct assay PubMed 15509711. Source: MGI
Molecular_function	1-phosphatidylinositol-3-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-dependent protein kinase activity Inferred from electronic annotation. Source: Compara histone serine kinase activity Inferred from electronic annotation. Source: Compara protein N-terminus binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3066	3066	Serine-protein kinase ATM		PRO_0000088841
Regions
	Domain	1966 – 2576	611	FAT
	Domain	2722 – 2972	251	PI3K/PI4K
	Domain	3034 – 3066	33	FATC
	Region	1380 – 1389	10	Interaction with ABL1 By similarity
Amino acid modifications
	Modified residue	367	1	Phosphoserine; by autocatalysis Ref.7
	Modified residue	1899	1	Phosphoserine; by autocatalysis Ref.7
	Modified residue	1987	1	Phosphoserine; by autocatalysis Ref.7
	Modified residue	3006	1	Phosphoserine By similarity
	Modified residue	3026	1	N6-acetyllysine By similarity
Experimental info
	Mutagenesis	367	1	S → A: Retains genomic stability and cell cycle checkpoint correction and kinase activity towards downstream targets; when associated with A-1987. Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-1899 and A-1987. Ref.7
	Mutagenesis	1899	1	S → A: Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987. Ref.7
	Mutagenesis	1987	1	S → A: Retains genomic stability and cell cycle checkpoint correction and kinase activity towards downstream targets; when associated with A-367. Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987. Ref.7
	Sequence conflict	600	1	S → R in AAC52673. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q62388 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 7AE54BF9801C6336	FASTA	3,066	349,418
	10 20 30 40 50 60 MSLALNDLLI CCRQLEHDRA TERRKEVDKF KRLIQDPETV QHLDRHSDSK QGKYLNWDAV 70 80 90 100 110 120 FRFLQKYIQK EMESLRTAKS NVSATTQSSR QKKMQEISSL VRYFIKCANK RAPRLKCQDL 130 140 150 160 170 180 LNYVMDTVKD SSNGLTYGAD CSNILLKDIL SVRKYWCEVS QQQWLELFSL YFRLYLKPSQ 190 200 210 220 230 240 DINRVLVARI IHAVTRGCCS QTDGLPSKFL DLFSKAIQYA RQEKSSPGLS HILAALNIFL 250 260 270 280 290 300 KSLAVNFRKR VCEAGDEILP TLLYIWTQHR LNDSLKEVII ELIQLQIYIH HPQGARAPEE 310 320 330 340 350 360 GAYESMKWKS ILYNLYDLLV NEISHIGSRG KYSSGSRNIA VKENLIDLMA DICYQLFDAD 370 380 390 400 410 420 TRSVEISQSY VTQRESTDYS VPCKRRKIDV GWEVIKDYLQ KSQSDFDLVP WLQITTRLIS 430 440 450 460 470 480 KYPSSLPNCE LSPLILILYQ LLPQQRRGER IPYVLRCLKE VALCQGKKSN LESSQKSDLL 490 500 510 520 530 540 KLWIKIWSIT FRGISSGQTQ TENFGLLEAI IQGSLVELDR EFWKLFTGSA CKPSSPSVCC 550 560 570 580 590 600 LTLALSICVV PDAIKMGTEQ SVCEANRSFS VKESIMRWLL FYQLEDDLED STELPPILQS 610 620 630 640 650 660 NFPHLVVEKI LVSLTMKNSK AAMKFFQSVP ECEQHCEDKE EPSFSEVEEL FLQTTFDKMD 670 680 690 700 710 720 FLTTVKEYAV EKFQSSVGFS VQQNLKESLD HYLLGLSEQL LSNYSSEITS SETLVRCSSL 730 740 750 760 770 780 LVGVLGCYCY MGIITEDEAH KSELFQKAKS LMQCAGESIS LFKNKTNEES RIGSLRNVMH 790 800 810 820 830 840 LCTSCLCIHT KHTPNKIASG FFLRLLTSKL MNDIADICKS LASCTKKPLD HGVHPGEDDE 850 860 870 880 890 900 DGGGCDSLME AEGPSSTGLS TAYPASSVSD ANDYGENQNA VGAMSPLAAD YLSKQDHLLL 910 920 930 940 950 960 DMLRFLGRSV TASQSHTVSF RGADIRRKLL LLLDSSILDL MKPLHLHMYL VLLKDLPGNE 970 980 990 1000 1010 1020 HSLPMEDVVE LLQPLSLVCS LHRRDQDVCK TILSNVLHIV TNLGQGSVDM ESTRIAQGHF 1030 1040 1050 1060 1070 1080 LTVMGAFWHL TKEKKCVFSV RMALVKCLQT LLEADPYSEW AILNVKGQDF PVNEAFSQFL 1090 1100 1110 1120 1130 1140 ADDHHQVRML AAGSVNRLFQ DMRQGDFSRS LKALPLKFQQ TSFNNAYTTA EAGIRGLLCD 1150 1160 1170 1180 1190 1200 SQNPDLLDEI YNRKSVLLMM IAVVLHCSPV CEKQALFALC KSVKENRLEP HLVKKVLEKV 1210 1220 1230 1240 1250 1260 SESFGCRSLE DFMISHLDYL VLEWLNLQDT EYSLSSFPFM LLNYTSIEDF YRSCYKILIP 1270 1280 1290 1300 1310 1320 HLVIRSHFDE VKSIANQIQK CWKSLLVDCF PKILVHILPY FAYEGTRDSY VSQKRETATK 1330 1340 1350 1360 1370 1380 VYDTLKGEDF LGKQIDQVFI SNLPEIVVEL LMTLHETADS ADSDASQSAT ALCDFSGDLD 1390 1400 1410 1420 1430 1440 PAPNPPYFPS HVIQATFAYI SNCHKTKFKS ILEILSKIPD SYQKILLAIC EQAAETNNVF 1450 1460 1470 1480 1490 1500 KKHRILKIYH LFVSLLLKDI QSGLGGAWAF VLRDVIYTLI HYINKRSSHF TDVSLRSFSL 1510 1520 1530 1540 1550 1560 CCDLLSRVCH TAVTQCKDAL ESHLHVIVGT LIPLVDYQEV QEQVLDLLKY LVIDNKDNKN 1570 1580 1590 1600 1610 1620 LSVTIKLLDP FPDHVIFKDL RLTQQKIKYS GGPFSLLEEI NHFLSVSAYN PLPLTRLEGL 1630 1640 1650 1660 1670 1680 KDLRRQLEQH KDQMLDLLRA SQDNPQDGIV VKLVVSLLQL SKMAVNQTGE REVLEAVGRC 1690 1700 1710 1720 1730 1740 LGEIGPLDFS TIAVQHNKDV SYTKAYGLPE DRELQWTLIM LTALNNTLVE DSVKIRSAAA 1750 1760 1770 1780 1790 1800 TCLKNILATK IGHIFWENYK TSADPMLTYL QPFRTSRKKF LEVPRSVKED VLEGLDAVNL 1810 1820 1830 1840 1850 1860 WVPQSESHDI WIKTLTCAFL DSGGINSEIL QLLKPMCEVK TDFCQMLLPY LIHDVLLQDT 1870 1880 1890 1900 1910 1920 HESWRTLLSA HVRGFFTSCF KHSSQASRSA TPANSDSESE NFLRCCLDKK SQRTMLAVVD 1930 1940 1950 1960 1970 1980 YLRRQKRPSS GTAFDDAFWL DLNYLEVAKV AQSCSAHFTA LLYAEIYSDK KSTDEQEKRS 1990 2000 2010 2020 2030 2040 PTFEEGSQGT TISSLSEKSK EETGISLQDL LLEIYRSIGE PDSLYGCGGG KMLQPLTRIR 2050 2060 2070 2080 2090 2100 TYEHEATWEK ALVTYDLETS ISSSTRQSGI IQALQNLGLS HILSVYLKGL DYERREWCAE 2110 2120 2130 2140 2150 2160 LQELRYQAAW RNMQWGLCAS AGQEVEGTSY HESLYNALQC LRNREFSTFY ESLRYASLFR 2170 2180 2190 2200 2210 2220 VKEVEELSKG SLESVYSLYP TLSRLQAIGE LENSGELFSR SVTDRERSEA YWKWQKHSQL 2230 2240 2250 2260 2270 2280 LKDSDFSFQE PLMALRTVIL ETLVQKEMER SQGACSKDIL TKHLVEFSVL ARTFKNTQLP 2290 2300 2310 2320 2330 2340 ERAIFKIKQY NSAICGISEW HLEEAQVFWA KKEQSLALSI LKQMIKKLDS SFKDKENDAG 2350 2360 2370 2380 2390 2400 LKVIYAECLR VCGSWLAETC LENPAVIMQT YLEKAVKVAG SYDGNSRELR NGQMKAFLSL 2410 2420 2430 2440 2450 2460 ARFSDTQYQR IENYMKSSEF ENKQTLLKRA KEEVGLLREH KIQTNRYTVK VQRELELDEC 2470 2480 2490 2500 2510 2520 ALRALREDRK RFLCKAVENY INCLLSGEEH DLWVFRLCSL WLENSGVSEV NGMMKKDGMK 2530 2540 2550 2560 2570 2580 ISSYKFLPLM YQLAARMGTK MTGGLGFHEV LNNLISRISL DHPHHTLFII LALANANKDE 2590 2600 2610 2620 2630 2640 FLSKPETTRR SRITKSTSKE NSHLDEDRTE AATRIIHSIR SKRCKMVKDM EALCDAYIIL 2650 2660 2670 2680 2690 2700 ANMDASQWRA QRKGINIPAN QPITKLKNLE DVVVPTMEIK VDPTGEYENL VTIKSFKTEF 2710 2720 2730 2740 2750 2760 RLAGGLNLPK IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ RNTETRKRKL 2770 2780 2790 2800 2810 2820 TICTYKVVPL SQRSGVLEWC TGTVPIGEYL VNSEDGAHRR YRPNDFSANQ CQKKMMEVQK 2830 2840 2850 2860 2870 2880 KSFEEKYDTF MTICQNFEPV FRYFCMEKFL DPAVWFEKRL AYTRSVATSS IVGYILGLGD 2890 2900 2910 2920 2930 2940 RHVQNILINE QSAELVHIDL GVAFEQGKIL PTPETVPFRL SRDIVDGMGI TGVEGVFRRC 2950 2960 2970 2980 2990 3000 CEKTMEVMRS SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDESDL HSTPNADDQE 3010 3020 3030 3040 3050 3060 CKQSLSDTDQ SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAM DPKNLSRLFP GWKAWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and chromosomal localization of Atm, the mouse homolog of the ataxia-telangiectasia gene." Pecker I., Avraham K.B., Gilbert D.J., Savitsky K., Rotman G., Harnik R., Fukao T., Schroeck E., Hirotsume S., Tagle D.A., Collins F.S., Wynshaw-Boris A., Ried T., Copeland N.G., Jenkins N.A., Shiloh Y., Ziv Y. Genomics 35:39-45(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Analysis of the ATM protein in wild-type and ataxia telangiectasia cells." Lakin N.D., Weber P., Stankovic T., Rottinghaus S.T., Taylor A.M.R., Jackson S.P. Oncogene 13:2707-2716(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"Atm expression patterns suggest a contribution from the peripheral nervous system to the phenotype of ataxia-telangiectasia." Soares H.D., Morgan J.I., McKinnon P.J. Neuroscience 86:1045-1054(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE. Strain: B6C3-F1.
[5]	"ATM binds to beta-adaptin in cytoplasmic vesicles." Lim D.-S., Kirsch D.G., Canman C.E., Ahn J.-H., Ziv Y., Newman L.S., Darnell R.B., Shiloh Y., Kastan M.B. Proc. Natl. Acad. Sci. U.S.A. 95:10146-10151(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AP2B1 AND AP3B2.
[6]	"ATM phosphorylates histone H2AX in response to DNA double-strand breaks." Burma S., Chen B.P., Murphy M., Kurimasa A., Chen D.J. J. Biol. Chem. 276:42462-42467(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF H2AFX.
[7]	"Multiple autophosphorylation sites are dispensable for murine ATM activation in vivo." Daniel J.A., Pellegrini M., Lee J.H., Paull T.T., Feigenbaum L., Nussenzweig A. J. Cell Biol. 183:777-783(2008) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION AT SER-367; SER-1899 AND SER-1987, FUNCTION, MUTAGENESIS OF SER-367; SER-1899 AND SER-1987.
[8]	"RAG-1 and ATM coordinate monoallelic recombination and nuclear positioning of immunoglobulin loci." Hewitt S.L., Yin B., Ji Y., Chaumeil J., Marszalek K., Tenthorey J., Salvagiotto G., Steinel N., Ramsey L.B., Ghysdael J., Farrar M.A., Sleckman B.P., Schatz D.G., Busslinger M., Bassing C.H., Skok J.A. Nat. Immunol. 10:655-664(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U43678 mRNA. Translation: AAC52673.1. AC079869 Genomic DNA. No translation available. AC156640 Genomic DNA. No translation available.
IPI	IPI00124810.
RefSeq	NP_031525.2. NM_007499.2.
UniGene	Mm.5088.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q62388. 8 interactions.
PTM databases
PhosphoSite	Q62388.
Proteomic databases
PaxDb	Q62388.
PRIDE	Q62388.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000118282; ENSMUSP00000113388; ENSMUSG00000034218.
GeneID	11920.
KEGG	mmu:11920.
UCSC	uc009pmd.2. mouse.
Organism-specific databases
CTD	472.
MGI	MGI:107202. Atm.
Phylogenomic databases
eggNOG	COG5032.
GeneTree	ENSGT00670000098061.
HOGENOM	HOG000168373.
HOVERGEN	HBG004304.
InParanoid	Q62388.
KO	K04728.
OMA	GVLGCYC.
OrthoDB	EOG4X97G7.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse).
Gene expression databases
ArrayExpress	Q62388.
Bgee	Q62388.
CleanEx	MM_ATM.
Genevestigator	Q62388.
GermOnline	ENSMUSG00000034218. Mus musculus.
Family and domain databases
Gene3D	1.10.1070.11. 3 hits.
InterPro	IPR016024. ARM-type_fold. IPR015519. ATM/Tel1. IPR003152. FATC. IPR011009. Kinase-like_dom. IPR000403. PI3/4_kinase_cat_dom. IPR018936. PI3/4_kinase_CS. IPR003151. PIK-rel_kinase_FAT. IPR014009. PIK_FAT. IPR021668. TAN. [Graphical view]
PANTHER	PTHR11139:SF3. PTHR11139:SF3. 1 hit.
Pfam	PF02259. FAT. 1 hit. PF02260. FATC. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. PF11640. TAN. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 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. PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATM. mouse.
NextBio	279985.
SOURCE	Search...

Entry information

Entry name

ATM_MOUSE

Accession

Primary (citable) accession number: Q62388
Secondary accession number(s): E9QNY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program