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Q62388 (ATM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3066 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Phosphorylates ATF2 which stimulates its function in DNA damage response. 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 processCell cycle
DNA damage
   Cellular componentCytoplasmic vesicle
Nucleus
   DiseaseTumor suppressor
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from mutant phenotype PubMed 12937170. Source: MGI

DNA damage induced protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

DNA repair

Inferred from direct assay PubMed 15364958. Source: MGI

brain development

Inferred from genetic interaction PubMed 16687486. Source: MGI

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Traceable author statement PubMed 11040211. Source: MGI

cellular response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

neuron apoptotic process

Inferred from genetic interaction PubMed 11248063. Source: MGI

oocyte development

Inferred from mutant phenotype PubMed 11536012. Source: MGI

positive regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 15364958. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction involved in mitotic G2 DNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

somitogenesis

Inferred from genetic interaction PubMed 16687486. Source: MGI

   Cellular_componentchromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 15604234. Source: MGI

spindle

Inferred from direct assay PubMed 15509711. Source: MGI

   Molecular_function1-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: Ensembl

histone serine kinase activity

Inferred from electronic annotation. Source: Ensembl

protein N-terminus binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15680327. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 15364958. Source: MGI

protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 30663065Serine-protein kinase ATM
PRO_0000088841

Regions

Domain1966 – 2576611FAT
Domain2722 – 2972251PI3K/PI4K
Domain3034 – 306633FATC
Region1380 – 138910Interaction with ABL1 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue3671Phosphoserine; by autocatalysis Ref.7
Modified residue18991Phosphoserine; by autocatalysis Ref.7
Modified residue19871Phosphoserine; by autocatalysis Ref.7
Modified residue30061Phosphoserine By similarity
Modified residue30261N6-acetyllysine By similarity

Experimental info

Mutagenesis3671S → 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
Mutagenesis18991S → A: Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987. Ref.7
Mutagenesis19871S → 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 conflict6001S → R in AAC52673. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62388 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7AE54BF9801C6336

FASTA3,066349,418
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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: PHOSPHORYLATION 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.
CCDSCCDS40636.1.
RefSeqNP_031525.2. NM_007499.2.
UniGeneMm.5088.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198236. 15 interactions.
IntActQ62388. 9 interactions.

PTM databases

PhosphoSiteQ62388.

Proteomic databases

MaxQBQ62388.
PaxDbQ62388.
PRIDEQ62388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000118282; ENSMUSP00000113388; ENSMUSG00000034218.
GeneID11920.
KEGGmmu:11920.
UCSCuc009pmd.2. mouse.

Organism-specific databases

CTD472.
MGIMGI:107202. Atm.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00670000098061.
HOGENOMHOG000168373.
HOVERGENHBG004304.
InParanoidQ62388.
KOK04728.
OMAGVLGCYC.
OrthoDBEOG789C9F.
TreeFamTF101182.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

BgeeQ62388.
CleanExMM_ATM.
GenevestigatorQ62388.

Family and domain databases

Gene3D1.10.1070.11. 3 hits.
InterProIPR016024. ARM-type_fold.
IPR015519. ATM.
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]
PANTHERPTHR11139:SF66. PTHR11139:SF66. 1 hit.
PfamPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 10 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. 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]
ProtoNetSearch...

Other

ChiTaRSATM. mouse.
NextBio279985.
PROQ62388.
SOURCESearch...

Entry information

Entry nameATM_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot