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Q62388

- ATM_MOUSE

UniProt

Q62388 - ATM_MOUSE

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Protein

Serine-protein kinase ATM

Gene

Atm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by wortmannin.By similarity

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-kinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. DNA binding Source: UniProtKB-KW
  4. DNA-dependent protein kinase activity Source: Ensembl
  5. histone serine kinase activity Source: Ensembl
  6. protein kinase activity Source: MGI
  7. protein N-terminus binding Source: UniProtKB
  8. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. brain development Source: MGI
  2. cell cycle arrest Source: Ensembl
  3. cellular response to DNA damage stimulus Source: MGI
  4. cellular response to gamma radiation Source: Ensembl
  5. DNA damage checkpoint Source: MGI
  6. DNA damage induced protein phosphorylation Source: Ensembl
  7. DNA repair Source: MGI
  8. female gamete generation Source: MGI
  9. heart development Source: MGI
  10. histone mRNA catabolic process Source: UniProtKB
  11. intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  12. lipoprotein catabolic process Source: MGI
  13. mitotic spindle assembly checkpoint Source: UniProtKB
  14. negative regulation of B cell proliferation Source: Ensembl
  15. neuron apoptotic process Source: MGI
  16. oocyte development Source: MGI
  17. positive regulation of DNA damage response, signal transduction by p53 class mediator Source: Ensembl
  18. positive regulation of neuron apoptotic process Source: MGI
  19. pre-B cell allelic exclusion Source: UniProtKB
  20. protein autophosphorylation Source: Ensembl
  21. protein phosphorylation Source: MGI
  22. replicative senescence Source: InterPro
  23. response to hypoxia Source: Ensembl
  24. response to ionizing radiation Source: UniProtKB
  25. signal transduction involved in mitotic G2 DNA damage checkpoint Source: Ensembl
  26. somitogenesis Source: MGI
  27. telomere maintenance Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_198629. Meiotic recombination.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_222185. Regulation of HSF1-mediated heat shock response.
REACT_27235. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Atm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:107202. Atm.

Subcellular locationi

Nucleus By similarity. Cytoplasmic vesicle By similarity
Note: Primarily nuclear. Found also in endocytic vesicles in association with beta-adaptin By similarity.By similarity

GO - Cellular componenti

  1. chromosome, telomeric region Source: Ensembl
  2. cytoplasmic vesicle Source: UniProtKB-KW
  3. nucleoplasm Source: Reactome
  4. nucleus Source: MGI
  5. spindle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Involvement in diseasei

Atm-deficient mice show a phenotype similar to human ataxia telangiectasia (AT) and consistently develop immature T-cells malignancies.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi367 – 3671S → 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. 1 Publication
Mutagenesisi1899 – 18991S → A: Retains genomic stability, cell cycle checkpoint correction and kinase activity on downstream targets; when associated with A-367 and A-1987. 1 Publication
Mutagenesisi1987 – 19871S → 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. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 30663065Serine-protein kinase ATMPRO_0000088841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei367 – 3671Phosphoserine; by autocatalysis1 Publication
Modified residuei1899 – 18991Phosphoserine; by autocatalysis1 Publication
Modified residuei1987 – 19871Phosphoserine; by autocatalysis1 Publication
Modified residuei3006 – 30061PhosphoserineBy similarity
Modified residuei3026 – 30261N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by NUAK1/ARK5 By similarity. Autophosphorylation on Ser-367, Ser-1899, Ser-1987 correlates with DNA damage-mediated activation of the kinase.By similarity1 Publication
Acetylated by KAT5 upon DNA damage; which is required for autophosphorylation and subsequent activation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ62388.
PaxDbiQ62388.
PRIDEiQ62388.

PTM databases

PhosphoSiteiQ62388.

Expressioni

Tissue specificityi

Expressed in brain, skeletal muscle, testis, followed by spleen, lung, kidney, heart, liver and thymus. Ubiquitously expressed in embryonal tissues.

Developmental stagei

Highest expression in embryonic central nervous system, from E13.5 day and during the whole cerebellar development. Decreased expression when maturation occurs.1 Publication

Gene expression databases

BgeeiQ62388.
CleanExiMM_ATM.
ExpressionAtlasiQ62388. baseline and differential.
GenevestigatoriQ62388.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

BioGridi198236. 15 interactions.
IntActiQ62388. 9 interactions.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1966 – 2576611FATPROSITE-ProRule annotationAdd
BLAST
Domaini2722 – 2972251PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini3034 – 306633FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1380 – 138910Interaction with ABL1By similarity

Domaini

The FATC domain is required for interaction with KAT5.By similarity

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 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5032.
GeneTreeiENSGT00670000098061.
HOGENOMiHOG000168373.
HOVERGENiHBG004304.
InParanoidiQ62388.
KOiK04728.
OMAiGVLGCYC.
OrthoDBiEOG789C9F.
TreeFamiTF101182.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR016024. 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]
PANTHERiPTHR11139:SF66. PTHR11139:SF66. 1 hit.
PfamiPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 10 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62388-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLALNDLLI CCRQLEHDRA TERRKEVDKF KRLIQDPETV QHLDRHSDSK
60 70 80 90 100
QGKYLNWDAV FRFLQKYIQK EMESLRTAKS NVSATTQSSR QKKMQEISSL
110 120 130 140 150
VRYFIKCANK RAPRLKCQDL LNYVMDTVKD SSNGLTYGAD CSNILLKDIL
160 170 180 190 200
SVRKYWCEVS QQQWLELFSL YFRLYLKPSQ DINRVLVARI IHAVTRGCCS
210 220 230 240 250
QTDGLPSKFL DLFSKAIQYA RQEKSSPGLS HILAALNIFL KSLAVNFRKR
260 270 280 290 300
VCEAGDEILP TLLYIWTQHR LNDSLKEVII ELIQLQIYIH HPQGARAPEE
310 320 330 340 350
GAYESMKWKS ILYNLYDLLV NEISHIGSRG KYSSGSRNIA VKENLIDLMA
360 370 380 390 400
DICYQLFDAD TRSVEISQSY VTQRESTDYS VPCKRRKIDV GWEVIKDYLQ
410 420 430 440 450
KSQSDFDLVP WLQITTRLIS KYPSSLPNCE LSPLILILYQ LLPQQRRGER
460 470 480 490 500
IPYVLRCLKE VALCQGKKSN LESSQKSDLL KLWIKIWSIT FRGISSGQTQ
510 520 530 540 550
TENFGLLEAI IQGSLVELDR EFWKLFTGSA CKPSSPSVCC LTLALSICVV
560 570 580 590 600
PDAIKMGTEQ SVCEANRSFS VKESIMRWLL FYQLEDDLED STELPPILQS
610 620 630 640 650
NFPHLVVEKI LVSLTMKNSK AAMKFFQSVP ECEQHCEDKE EPSFSEVEEL
660 670 680 690 700
FLQTTFDKMD FLTTVKEYAV EKFQSSVGFS VQQNLKESLD HYLLGLSEQL
710 720 730 740 750
LSNYSSEITS SETLVRCSSL LVGVLGCYCY MGIITEDEAH KSELFQKAKS
760 770 780 790 800
LMQCAGESIS LFKNKTNEES RIGSLRNVMH LCTSCLCIHT KHTPNKIASG
810 820 830 840 850
FFLRLLTSKL MNDIADICKS LASCTKKPLD HGVHPGEDDE DGGGCDSLME
860 870 880 890 900
AEGPSSTGLS TAYPASSVSD ANDYGENQNA VGAMSPLAAD YLSKQDHLLL
910 920 930 940 950
DMLRFLGRSV TASQSHTVSF RGADIRRKLL LLLDSSILDL MKPLHLHMYL
960 970 980 990 1000
VLLKDLPGNE HSLPMEDVVE LLQPLSLVCS LHRRDQDVCK TILSNVLHIV
1010 1020 1030 1040 1050
TNLGQGSVDM ESTRIAQGHF LTVMGAFWHL TKEKKCVFSV RMALVKCLQT
1060 1070 1080 1090 1100
LLEADPYSEW AILNVKGQDF PVNEAFSQFL ADDHHQVRML AAGSVNRLFQ
1110 1120 1130 1140 1150
DMRQGDFSRS LKALPLKFQQ TSFNNAYTTA EAGIRGLLCD SQNPDLLDEI
1160 1170 1180 1190 1200
YNRKSVLLMM IAVVLHCSPV CEKQALFALC KSVKENRLEP HLVKKVLEKV
1210 1220 1230 1240 1250
SESFGCRSLE DFMISHLDYL VLEWLNLQDT EYSLSSFPFM LLNYTSIEDF
1260 1270 1280 1290 1300
YRSCYKILIP HLVIRSHFDE VKSIANQIQK CWKSLLVDCF PKILVHILPY
1310 1320 1330 1340 1350
FAYEGTRDSY VSQKRETATK VYDTLKGEDF LGKQIDQVFI SNLPEIVVEL
1360 1370 1380 1390 1400
LMTLHETADS ADSDASQSAT ALCDFSGDLD PAPNPPYFPS HVIQATFAYI
1410 1420 1430 1440 1450
SNCHKTKFKS ILEILSKIPD SYQKILLAIC EQAAETNNVF KKHRILKIYH
1460 1470 1480 1490 1500
LFVSLLLKDI QSGLGGAWAF VLRDVIYTLI HYINKRSSHF TDVSLRSFSL
1510 1520 1530 1540 1550
CCDLLSRVCH TAVTQCKDAL ESHLHVIVGT LIPLVDYQEV QEQVLDLLKY
1560 1570 1580 1590 1600
LVIDNKDNKN LSVTIKLLDP FPDHVIFKDL RLTQQKIKYS GGPFSLLEEI
1610 1620 1630 1640 1650
NHFLSVSAYN PLPLTRLEGL KDLRRQLEQH KDQMLDLLRA SQDNPQDGIV
1660 1670 1680 1690 1700
VKLVVSLLQL SKMAVNQTGE REVLEAVGRC LGEIGPLDFS TIAVQHNKDV
1710 1720 1730 1740 1750
SYTKAYGLPE DRELQWTLIM LTALNNTLVE DSVKIRSAAA TCLKNILATK
1760 1770 1780 1790 1800
IGHIFWENYK TSADPMLTYL QPFRTSRKKF LEVPRSVKED VLEGLDAVNL
1810 1820 1830 1840 1850
WVPQSESHDI WIKTLTCAFL DSGGINSEIL QLLKPMCEVK TDFCQMLLPY
1860 1870 1880 1890 1900
LIHDVLLQDT HESWRTLLSA HVRGFFTSCF KHSSQASRSA TPANSDSESE
1910 1920 1930 1940 1950
NFLRCCLDKK SQRTMLAVVD YLRRQKRPSS GTAFDDAFWL DLNYLEVAKV
1960 1970 1980 1990 2000
AQSCSAHFTA LLYAEIYSDK KSTDEQEKRS PTFEEGSQGT TISSLSEKSK
2010 2020 2030 2040 2050
EETGISLQDL LLEIYRSIGE PDSLYGCGGG KMLQPLTRIR TYEHEATWEK
2060 2070 2080 2090 2100
ALVTYDLETS ISSSTRQSGI IQALQNLGLS HILSVYLKGL DYERREWCAE
2110 2120 2130 2140 2150
LQELRYQAAW RNMQWGLCAS AGQEVEGTSY HESLYNALQC LRNREFSTFY
2160 2170 2180 2190 2200
ESLRYASLFR VKEVEELSKG SLESVYSLYP TLSRLQAIGE LENSGELFSR
2210 2220 2230 2240 2250
SVTDRERSEA YWKWQKHSQL LKDSDFSFQE PLMALRTVIL ETLVQKEMER
2260 2270 2280 2290 2300
SQGACSKDIL TKHLVEFSVL ARTFKNTQLP ERAIFKIKQY NSAICGISEW
2310 2320 2330 2340 2350
HLEEAQVFWA KKEQSLALSI LKQMIKKLDS SFKDKENDAG LKVIYAECLR
2360 2370 2380 2390 2400
VCGSWLAETC LENPAVIMQT YLEKAVKVAG SYDGNSRELR NGQMKAFLSL
2410 2420 2430 2440 2450
ARFSDTQYQR IENYMKSSEF ENKQTLLKRA KEEVGLLREH KIQTNRYTVK
2460 2470 2480 2490 2500
VQRELELDEC ALRALREDRK RFLCKAVENY INCLLSGEEH DLWVFRLCSL
2510 2520 2530 2540 2550
WLENSGVSEV NGMMKKDGMK ISSYKFLPLM YQLAARMGTK MTGGLGFHEV
2560 2570 2580 2590 2600
LNNLISRISL DHPHHTLFII LALANANKDE FLSKPETTRR SRITKSTSKE
2610 2620 2630 2640 2650
NSHLDEDRTE AATRIIHSIR SKRCKMVKDM EALCDAYIIL ANMDASQWRA
2660 2670 2680 2690 2700
QRKGINIPAN QPITKLKNLE DVVVPTMEIK VDPTGEYENL VTIKSFKTEF
2710 2720 2730 2740 2750
RLAGGLNLPK IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ
2760 2770 2780 2790 2800
RNTETRKRKL TICTYKVVPL SQRSGVLEWC TGTVPIGEYL VNSEDGAHRR
2810 2820 2830 2840 2850
YRPNDFSANQ CQKKMMEVQK KSFEEKYDTF MTICQNFEPV FRYFCMEKFL
2860 2870 2880 2890 2900
DPAVWFEKRL AYTRSVATSS IVGYILGLGD RHVQNILINE QSAELVHIDL
2910 2920 2930 2940 2950
GVAFEQGKIL PTPETVPFRL SRDIVDGMGI TGVEGVFRRC CEKTMEVMRS
2960 2970 2980 2990 3000
SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDESDL HSTPNADDQE
3010 3020 3030 3040 3050
CKQSLSDTDQ SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAM
3060
DPKNLSRLFP GWKAWV
Length:3,066
Mass (Da):349,418
Last modified:July 27, 2011 - v2
Checksum:i7AE54BF9801C6336
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti600 – 6001S → R in AAC52673. (PubMed:8661102)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43678 mRNA. Translation: AAC52673.1.
AC079869 Genomic DNA. No translation available.
AC156640 Genomic DNA. No translation available.
CCDSiCCDS40636.1.
RefSeqiNP_031525.2. NM_007499.2.
UniGeneiMm.5088.

Genome annotation databases

EnsembliENSMUST00000118282; ENSMUSP00000113388; ENSMUSG00000034218.
GeneIDi11920.
KEGGimmu:11920.
UCSCiuc009pmd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U43678 mRNA. Translation: AAC52673.1 .
AC079869 Genomic DNA. No translation available.
AC156640 Genomic DNA. No translation available.
CCDSi CCDS40636.1.
RefSeqi NP_031525.2. NM_007499.2.
UniGenei Mm.5088.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198236. 15 interactions.
IntActi Q62388. 9 interactions.

PTM databases

PhosphoSitei Q62388.

Proteomic databases

MaxQBi Q62388.
PaxDbi Q62388.
PRIDEi Q62388.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000118282 ; ENSMUSP00000113388 ; ENSMUSG00000034218 .
GeneIDi 11920.
KEGGi mmu:11920.
UCSCi uc009pmd.2. mouse.

Organism-specific databases

CTDi 472.
MGIi MGI:107202. Atm.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00670000098061.
HOGENOMi HOG000168373.
HOVERGENi HBG004304.
InParanoidi Q62388.
KOi K04728.
OMAi GVLGCYC.
OrthoDBi EOG789C9F.
TreeFami TF101182.

Enzyme and pathway databases

Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_198629. Meiotic recombination.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_222185. Regulation of HSF1-mediated heat shock response.
REACT_27235. Meiotic Recombination.

Miscellaneous databases

ChiTaRSi ATM. mouse.
NextBioi 279985.
PROi Q62388.
SOURCEi Search...

Gene expression databases

Bgeei Q62388.
CleanExi MM_ATM.
ExpressionAtlasi Q62388. baseline and differential.
Genevestigatori Q62388.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
InterProi IPR016024. 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 ]
PANTHERi PTHR11139:SF66. PTHR11139:SF66. 1 hit.
Pfami PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 10 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. 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. 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. Cited for: FUNCTION.

Entry informationi

Entry nameiATM_MOUSE
AccessioniPrimary (citable) accession number: Q62388
Secondary accession number(s): E9QNY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3