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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 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
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.1 Publication

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
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.1 Publication

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 – 11Removed By similarity
Chaini2 – 30663065Serine-protein kinase ATMPRO_0000088841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei367 – 3671Phosphoserine; by autocatalysis1 Publication
Modified residuei1899 – 18991Phosphoserine; by autocatalysis1 Publication
Modified residuei1987 – 19871Phosphoserine; by autocatalysis1 Publication
Modified residuei3006 – 30061Phosphoserine By similarity
Modified residuei3026 – 30261N6-acetyllysine By 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.1 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.1 Publication

Protein-protein interaction databases

BioGridi198236. 15 interactions.
IntActiQ62388. 9 interactions.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1966 – 2576611FATAdd
BLAST
Domaini2722 – 2972251PI3K/PI4KAdd
BLAST
Domaini3034 – 306633FATCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1380 – 138910Interaction with ABL1 By similarity

Domaini

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

Sequence similaritiesi

Contains 1 FAT domain.
Contains 1 FATC domain.
Contains 1 PI3K/PI4K domain.

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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti600 – 6001S → R in AAC52673. 1 Publication

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

« 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: September 3, 2014
This is version 143 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

Similar proteinsi