ID F6ZIB3_MACMU Unreviewed; 3026 AA.
AC F6ZIB3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Serine-protein kinase ATM {ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU365027};
GN Name=ATM {ECO:0000313|Ensembl:ENSMMUP00000036720.3,
GN ECO:0000313|VGNC:VGNC:70173};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000036720.3, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000036720.3}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000036720.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon double strand breaks (DSBs), apoptosis and genotoxic
CC stresses such as ionizing ultraviolet A light (UVA), thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates 'Ser-139' of histone variant H2AX at double strand
CC breaks (DSBs), thereby regulating DNA damage response mechanism. Also
CC plays a role in pre-B cell allelic exclusion, a process leading to
CC expression of a single immunoglobulin heavy chain allele to enforce
CC clonality and monospecific recognition by the B-cell antigen receptor
CC (BCR) expressed on individual B-lymphocytes. After the introduction of
CC DNA breaks by the RAG complex on one immunoglobulin allele, acts by
CC mediating a repositioning of the second allele to pericentromeric
CC heterochromatin, preventing accessibility to the RAG complex and
CC recombination of the second allele. Also involved in signal
CC transduction and cell cycle control. May function as a tumor
CC suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates
CC DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN),
CC TERF1, RAD9, UBQLN4 and DCLRE1C. May play a role in vesicle and/or
CC protein transport. Could play a role in T-cell development, gonad and
CC neurological function. Binds DNA ends. Plays a role in replication-
CC dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus
CC in response to genotoxic stress prevents its MDM2-mediated
CC ubiquitination and subsequent proteasome degradation. Phosphorylates
CC ATF2 which stimulates its function in DNA damage response.
CC Phosphorylates ERCC6 which is essential for its chromatin remodeling
CC activity at DNA double-strand breaks. {ECO:0000256|RuleBase:RU365027}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|RuleBase:RU365027};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|RuleBase:RU365027}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769, ECO:0000256|RuleBase:RU365027}.
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DR Ensembl; ENSMMUT00000043730.3; ENSMMUP00000036720.3; ENSMMUG00000004153.4.
DR VEuPathDB; HostDB:ENSMMUG00000004153; -.
DR VGNC; VGNC:70173; ATM.
DR eggNOG; KOG0892; Eukaryota.
DR GeneTree; ENSGT00670000098061; -.
DR HOGENOM; CLU_000178_3_2_1; -.
DR Proteomes; UP000006718; Chromosome 14.
DR Bgee; ENSMMUG00000004153; Expressed in spleen and 23 other cell types or tissues.
DR ExpressionAtlas; F6ZIB3; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048584; P:positive regulation of response to stimulus; IEA:UniProt.
DR GO; GO:0080135; P:regulation of cellular response to stress; IEA:UniProt.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038980; ATM_plant.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11640; TAN; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365027};
KW Cytoplasmic vesicle {ECO:0000256|RuleBase:RU365027};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1910..2536
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2656..2968
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2994..3026
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 3026 AA; 347067 MW; D2A211978150A725 CRC64;
MSLALNDLLI CCRQLEHERA TERKKEVEKF KRLIRDPETI IHLDRHSDSK QGKYLNWDAV
FRFLQKYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL VKYFIKCANR RAPRLKCQEL
LNYIMDTVKD SSSGAVYGAD YSNILLKDIL SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ
DVHRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQCA RQEKSSPGLN HILAALTIFL
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTREK
GAYESTKWKS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA DICHQVFNED
TRSLEISQSY TTTQRESGDY SVPCKRKKIE LGWEVIKDHL QKSQNDFDLV PWLQIATQLI
SKYPASLPNC ELSPLLMILS QLLPQQRHGE RTPYVLRCLT EVALCQDKRS NLESSQKSDL
LKLWNKIWCI TFRGISSEQI QAENFGLLGA IIQSSLVEVD REFWKLFTGS ACRPSCPAVC
CLTLALTTSV VPGTVKMGIE QNMCEVNRSF SLKESIMKWL LFYQLEGDLE NSTEVPPILH
SNFPHLVLEK ILVSLTMKNC KAAMNFFQSV PECEHHRKDK EELSFSEVEE LFLQTTFDKM
DFLTIVRECG IEKHQSSIGF SVHQNLKESL DCYLLGLSEQ LLNNYSSEIT NSETLVRCSS
LLVGVLGCYC YMGVIAEEEA CKSELFQKAK SLMQCAGESI TLFKNKTNEE FRIGSLRNMM
HLFTRCLSNC TKASLIKKPF DRGEVESREE DTNGNLMEVE DQSSMNLFND YPDSSVSDAN
EPGESQSTIG AINPLAEEYL SKQDLLFLDM LKFLCLCVTT AQTNTVSFRA ADIRRKLLML
IDSSTLDPTK SLHLHMYLML LKELPGEEYP LPMEDVVELL KPLSNVCSLY RRDQDVCKTI
LNHVLHIVKN LGQSNMDSEN TRDAQGQFLT VIGAFWHLTK ERKCTFSVRM ALVNCLKTLL
EADPYSKWAI LNVMGKDFPV NEVFTQFLAD NHHRVRMLAA ESINRLFQDT KGDSSTLLKA
LPLRLQQTAF ENAYLKAQEG MREMSHSAEN PEPLDEIYNR KSVLLMLIAV VLSCSPICEK
QALFALCKSV KENGLEPHLV KKVLEKVSET FGYRCLEDFM ASHLDYLVLE WLNLQDTEYN
LSSFPFILLN YTNIEDFYRS CYKVLVPHLV IRSHFDEVKS IANQIQEDWK SLLTDCFPKI
LVNILPYFAY EGTGDSGMAQ QRETATKVYD MLKSENLLGK QIDHLFISNL PEIVVELLMT
LHEPANSSAS QSTDLCDFSG DLDPAPNPPH FPSHVIKATF AYISNCHKTK LKSILEILSK
SPDSYQKILL AICEQAAETN NVYKKHRILK IYHLFVSLLL KDIKSGLGGA WAFVLRDVIY
TLIHYINQRP SRIMDVSLRS FSLCCDLLSQ VCQTVVTYCK DALENHLHVI VGTLIPLVDE
QVEVQKQVLD LLKYLVIDNK DNENLYLTIK LLDPFPDHVV FKDLRIAQQK IKYSRGPFSL
LEEINHFLSV SVYDALPLTR LEGLKDLRRQ LELHKDQMMD IMRASQDNPQ DGIMVKLVVN
LLQLSKMAIN HTGEKEVLEA VGTCLGEVGP IDFSTIAIQH SKDASYTKAL KLFEGKELQW
TFIMLTYLNN TLVEDCVKVR SAAVTCLKNI LATKTGHSFW EIYKMTTDPM LAYLQPFRTS
RKKFLEVPRF DKENPFEGLD DINLWIPLSE NHDIWIKTLT CAFLDSGGTK CEILQLLKPM
CEVKTDFCQT VLPYLIHDIL LQDTNESWRN LLSTHVQGFF TSCLRHFSQT SRSTTPANLD
SESEHFFRCC LDKKSQRTML AVVDYMRRQK RPSSGTIFDD AFWLDLNYLE VAKVAQSCAA
HFTALLYAEI YADKKSMDDQ EKRSLAFEEG SQSTTISSLS EKSKEETGIS LQDLLLEIYR
SIGEPDSLYG CGGGKMLQPI TRLRTYEHEA MWGKALVTYD LETAISSSTR QAGIIQALQN
LGLCHILSVY LKGLDYENKD WCPELQELHY QAAWRNMQWD YCTNVSKEIE GTSYHESLYN
ALQSLRDREF STFYESLKYA RVKEVEELCK RSLESVYSLY PTLSRLQAIG ELESIGELFS
KSVTHRQLSE VYIKWQKHSQ LLKDSDFSFQ EPIMALRTVI LEILMEKEID NSQRECIKEI
LTKHLVELSI LARTFKNTQL PERAIFQIKQ YNSVSCGVSE WQLEEAQVFW AKKEQSLALS
ILKQMIKKLD ASCAANNPSL KLIYTECLRV CGNWLAETCL ENPAVIMQTY LEKAVEVAGN
YDGESNDELR NGKMKAFLSL ARFSDTQYQR IENYMKSSEF ENKQALLKRA KEEVGLLREH
KIQTNRYTVK VQRELELDEL ALHALKEDRK RFLCKAVENY INCLLSGEEH DMWVFRLCSL
WLENSGVSEV NGMMKRDGMK IPSYKFLPLM YQLAARMGTK MMGGLGFHEV LNNLISRISM
DHPHHTLFII LALANANRDE FLTKPEVARR SRITKNAPKQ SSQLDEDRTE AANRIICTIR
SRRPQMVRSV EALCDAYIIL ANLDATQWKT QRKGINIPAD QPITKLKNLE DVVVPTMEIK
VDHTGEYGNL VTIQSFKAEF RLAGGVNLPK IIDCVGSDGK ERRQLVKGRD DLRQDAVMQQ
VFQMCNTLLQ RNTETRKRKL TICTYKVVPL SQRSGVLEWC TGTIPIGEFL VNNEDGAHKR
YRPNDFSAFQ CQKKMMEVQK KSFEDKYEVF MDVCQNFQPV FRYFCMEKFL DPAIWFEKRL
AYTRSVATSS IVGYILGLGD RHVQNILINE QSAELVHIDL GVAFEQGKIL PTPETVPFRL
TRDIVDGMGI TGVEGVFRRC CEKTIEVMRN SQETLLTIVE VLLYDPLFDW TMNPLKALYL
QQRPEDETEL HPTVNADDQE CKRNLSDIDQ SFNKVAERVL MRLQEKLKGV EEGTVLSVGG
QVNLLIQQAM DPKNLSRLFP GWKAWV
//
