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Q62388

- ATM_MOUSE

UniProt

Q62388 - ATM_MOUSE

Protein

Serine-protein kinase ATM

Gene

Atm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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 binding Source: UniProtKB
    7. protein kinase activity Source: MGI
    8. protein N-terminus binding Source: UniProtKB
    9. 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

    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 membrane-bounded vesicle Source: UniProtKB-SubCell
    3. nucleoplasm Source: Reactome
    4. nucleus Source: MGI
    5. spindle Source: MGI

    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.
    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

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    MSLALNDLLI CCRQLEHDRA TERRKEVDKF KRLIQDPETV QHLDRHSDSK     50
    QGKYLNWDAV FRFLQKYIQK EMESLRTAKS NVSATTQSSR QKKMQEISSL 100
    VRYFIKCANK RAPRLKCQDL LNYVMDTVKD SSNGLTYGAD CSNILLKDIL 150
    SVRKYWCEVS QQQWLELFSL YFRLYLKPSQ DINRVLVARI IHAVTRGCCS 200
    QTDGLPSKFL DLFSKAIQYA RQEKSSPGLS HILAALNIFL KSLAVNFRKR 250
    VCEAGDEILP TLLYIWTQHR LNDSLKEVII ELIQLQIYIH HPQGARAPEE 300
    GAYESMKWKS ILYNLYDLLV NEISHIGSRG KYSSGSRNIA VKENLIDLMA 350
    DICYQLFDAD TRSVEISQSY VTQRESTDYS VPCKRRKIDV GWEVIKDYLQ 400
    KSQSDFDLVP WLQITTRLIS KYPSSLPNCE LSPLILILYQ LLPQQRRGER 450
    IPYVLRCLKE VALCQGKKSN LESSQKSDLL KLWIKIWSIT FRGISSGQTQ 500
    TENFGLLEAI IQGSLVELDR EFWKLFTGSA CKPSSPSVCC LTLALSICVV 550
    PDAIKMGTEQ SVCEANRSFS VKESIMRWLL FYQLEDDLED STELPPILQS 600
    NFPHLVVEKI LVSLTMKNSK AAMKFFQSVP ECEQHCEDKE EPSFSEVEEL 650
    FLQTTFDKMD FLTTVKEYAV EKFQSSVGFS VQQNLKESLD HYLLGLSEQL 700
    LSNYSSEITS SETLVRCSSL LVGVLGCYCY MGIITEDEAH KSELFQKAKS 750
    LMQCAGESIS LFKNKTNEES RIGSLRNVMH LCTSCLCIHT KHTPNKIASG 800
    FFLRLLTSKL MNDIADICKS LASCTKKPLD HGVHPGEDDE DGGGCDSLME 850
    AEGPSSTGLS TAYPASSVSD ANDYGENQNA VGAMSPLAAD YLSKQDHLLL 900
    DMLRFLGRSV TASQSHTVSF RGADIRRKLL LLLDSSILDL MKPLHLHMYL 950
    VLLKDLPGNE HSLPMEDVVE LLQPLSLVCS LHRRDQDVCK TILSNVLHIV 1000
    TNLGQGSVDM ESTRIAQGHF LTVMGAFWHL TKEKKCVFSV RMALVKCLQT 1050
    LLEADPYSEW AILNVKGQDF PVNEAFSQFL ADDHHQVRML AAGSVNRLFQ 1100
    DMRQGDFSRS LKALPLKFQQ TSFNNAYTTA EAGIRGLLCD SQNPDLLDEI 1150
    YNRKSVLLMM IAVVLHCSPV CEKQALFALC KSVKENRLEP HLVKKVLEKV 1200
    SESFGCRSLE DFMISHLDYL VLEWLNLQDT EYSLSSFPFM LLNYTSIEDF 1250
    YRSCYKILIP HLVIRSHFDE VKSIANQIQK CWKSLLVDCF PKILVHILPY 1300
    FAYEGTRDSY VSQKRETATK VYDTLKGEDF LGKQIDQVFI SNLPEIVVEL 1350
    LMTLHETADS ADSDASQSAT ALCDFSGDLD PAPNPPYFPS HVIQATFAYI 1400
    SNCHKTKFKS ILEILSKIPD SYQKILLAIC EQAAETNNVF KKHRILKIYH 1450
    LFVSLLLKDI QSGLGGAWAF VLRDVIYTLI HYINKRSSHF TDVSLRSFSL 1500
    CCDLLSRVCH TAVTQCKDAL ESHLHVIVGT LIPLVDYQEV QEQVLDLLKY 1550
    LVIDNKDNKN LSVTIKLLDP FPDHVIFKDL RLTQQKIKYS GGPFSLLEEI 1600
    NHFLSVSAYN PLPLTRLEGL KDLRRQLEQH KDQMLDLLRA SQDNPQDGIV 1650
    VKLVVSLLQL SKMAVNQTGE REVLEAVGRC LGEIGPLDFS TIAVQHNKDV 1700
    SYTKAYGLPE DRELQWTLIM LTALNNTLVE DSVKIRSAAA TCLKNILATK 1750
    IGHIFWENYK TSADPMLTYL QPFRTSRKKF LEVPRSVKED VLEGLDAVNL 1800
    WVPQSESHDI WIKTLTCAFL DSGGINSEIL QLLKPMCEVK TDFCQMLLPY 1850
    LIHDVLLQDT HESWRTLLSA HVRGFFTSCF KHSSQASRSA TPANSDSESE 1900
    NFLRCCLDKK SQRTMLAVVD YLRRQKRPSS GTAFDDAFWL DLNYLEVAKV 1950
    AQSCSAHFTA LLYAEIYSDK KSTDEQEKRS PTFEEGSQGT TISSLSEKSK 2000
    EETGISLQDL LLEIYRSIGE PDSLYGCGGG KMLQPLTRIR TYEHEATWEK 2050
    ALVTYDLETS ISSSTRQSGI IQALQNLGLS HILSVYLKGL DYERREWCAE 2100
    LQELRYQAAW RNMQWGLCAS AGQEVEGTSY HESLYNALQC LRNREFSTFY 2150
    ESLRYASLFR VKEVEELSKG SLESVYSLYP TLSRLQAIGE LENSGELFSR 2200
    SVTDRERSEA YWKWQKHSQL LKDSDFSFQE PLMALRTVIL ETLVQKEMER 2250
    SQGACSKDIL TKHLVEFSVL ARTFKNTQLP ERAIFKIKQY NSAICGISEW 2300
    HLEEAQVFWA KKEQSLALSI LKQMIKKLDS SFKDKENDAG LKVIYAECLR 2350
    VCGSWLAETC LENPAVIMQT YLEKAVKVAG SYDGNSRELR NGQMKAFLSL 2400
    ARFSDTQYQR IENYMKSSEF ENKQTLLKRA KEEVGLLREH KIQTNRYTVK 2450
    VQRELELDEC ALRALREDRK RFLCKAVENY INCLLSGEEH DLWVFRLCSL 2500
    WLENSGVSEV NGMMKKDGMK ISSYKFLPLM YQLAARMGTK MTGGLGFHEV 2550
    LNNLISRISL DHPHHTLFII LALANANKDE FLSKPETTRR SRITKSTSKE 2600
    NSHLDEDRTE AATRIIHSIR SKRCKMVKDM EALCDAYIIL ANMDASQWRA 2650
    QRKGINIPAN QPITKLKNLE DVVVPTMEIK VDPTGEYENL VTIKSFKTEF 2700
    RLAGGLNLPK IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ VFQMCNTLLQ 2750
    RNTETRKRKL TICTYKVVPL SQRSGVLEWC TGTVPIGEYL VNSEDGAHRR 2800
    YRPNDFSANQ CQKKMMEVQK KSFEEKYDTF MTICQNFEPV FRYFCMEKFL 2850
    DPAVWFEKRL AYTRSVATSS IVGYILGLGD RHVQNILINE QSAELVHIDL 2900
    GVAFEQGKIL PTPETVPFRL SRDIVDGMGI TGVEGVFRRC CEKTMEVMRS 2950
    SQETLLTIVE VLLYDPLFDW TMNPLKALYL QQRPEDESDL HSTPNADDQE 3000
    CKQSLSDTDQ SFNKVAERVL MRLQEKLKGV EEGTVLSVGG QVNLLIQQAM 3050
    DPKNLSRLFP GWKAWV 3066
    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.
    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

    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 1, 2014
    This is version 144 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