ID A0A2K6L9Z6_RHIBE Unreviewed; 3026 AA.
AC A0A2K6L9Z6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:ENSRBIP00000020338.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000020338.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000020338.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000020338.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 61621.ENSRBIP00000020338; -.
DR Ensembl; ENSRBIT00000044216.1; ENSRBIP00000020338.1; ENSRBIG00000034107.1.
DR GeneTree; ENSGT00670000098061; -.
DR OMA; VVTKGCC; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:1990391; C:DNA repair complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004677; F:DNA-dependent protein kinase activity; IEA:Ensembl.
DR GO; GO:0035979; F:histone H2AXS139 kinase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0071481; P:cellular response to X-ray; IEA:Ensembl.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IEA:Ensembl.
DR GO; GO:0097694; P:establishment of RNA localization to telomere; IEA:Ensembl.
DR GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0071044; P:histone mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:1904354; P:negative regulation of telomere capping; IEA:Ensembl.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0048599; P:oocyte development; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0000425; P:pexophagy; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1904884; P:positive regulation of telomerase catalytic core complex assembly; IEA:Ensembl.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0002331; P:pre-B cell allelic exclusion; IEA:Ensembl.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0090399; P:replicative senescence; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
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:UP000233180};
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; 347144 MW; CF2C071ADB59C08E CRC64;
MSLALNDLLI CCRQLEHDRA TERKKEVEKF KRLIRDPETI IHLDRHSDSK QGKYLNWDAV
FRFLQRYIQK ETECLRIAKP NVSASTQASR QKKMQEISSL VKYFIKCANR RAPRLKCQEL
LNYIMDTVKD SSSGAVYGAD YSNILLKDIL SVRKYWCEIS QQQWLELFSV YFRLYLKPSQ
DVHRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQCA RQEKSSPGLN HILAALTIFL
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK
GAYESTKWKS ILYNLYDLLV NEISHIGSRG KYSSGFRNIA VKENLIELMA DICFNEDTRS
LEISQSYTTT QRESSDYSVP CKRKKIELGW EVIKDHLQKS QNDFDLVPWL QIATQLISKY
PASLPNCELS PLLMILSQLL PQQRHGERTP YVLRCLTEVA LCQDKRSNLE SSQKSDLLKL
WNKIWCITFR GISSEQIQAE NFGLLGAIIQ SSLVEVDREF WKLFTGSACR PSCPAVCCLT
LALTTSIVPG TVKMGIEQNM CEVNRSFSLK ESIMKWLLFY QLEGDLENST EVPPILHSNF
PHLVLEKILV TAMNFFQSVP ECDHHRKDKE ELSFSEVEEL FLQTTFDKMD FLTIVRECGI
EKHQSSIGFS VHQNLKESLD HYLLGLSEQL LNNYSSEITN SETLVRCSSL LVGVLGCYCY
MGVIAEEEAY KSELFQKAKS LMQCAGESIT LFKNKTNEEF RIGSLRNMMH LCTRCLSNCT
KKSPNKIASG FFLRLLTSKL MNDIADICKS FASLIKKPFD RGEVESMEQD TNGNLMEVEE
QSSMNLFNDY PDSSVSDANE PGESQSTIGA INPLAEEYLS KQDLLFLDML KFLCLCVTTA
QTNTVSFRAA DIRRKLLMLI DSSTLDPTKS LHLHMYLMLL KELPGEEYPL PMEDVVELLK
PLSNVCSLYR RDQDVCKTIL NHVLHIVKNL GQSSMDSENT RDAQGQFLTV IGSTLWSYFS
FADPYSQWAI LNVMGKDFPV NEVFTQFLAD NHHRVRMLAA ESINRLFQDT KRDSSRLPKA
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 VCQTAVTYCK DALENHLHVI VGTLIPLVDE
QVEIQKQVLD LLKYLVIDNK DNENLYLTIK LLDPFPDHVV FKDLRITQQK IKYSRGPFSL
LEEINHFLSV SVYDALPLTR LEGLKDLRRQ LELHKDQMMD IMRASQDNPQ DGIMVKLVVN
LLQLSKMAIN HTGEKEVLEA VGSCLGEVGP IDFSTIAIQH SKDASYTKAL KLFEGKELQW
TFIMLTYLNN TLVEDCVTVR SAAVTCLKNI LATKTGHSFW EIYKMTTDPM LAYLQPFRTS
RKKFLEVPRF DKENPFEGLD DINLWMPLSE NHDIWIKTLT CAFLDSGGTK CEILQLLKPM
CEVKTDFCQI 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 HCTNVSKEIE GTSYHESLYS
ALQSLRDREF SAFYESLKYA RVKEVEELCK RSLESVYSLY PTLSRLQAIG ELESIGELFS
KSVTHRQLSE VYIKWQKHSQ LLKDSDFSFQ EPIMALRTVI LEILMEKEIE NSQRECIKEI
LTKHLVELSI LSRTFKNTQL PERAIFQIKQ YNPVSCGVSE WQLEEAQVFW AKKEQSLALS
ILKQMIKKLD ASCAANNPSL KLIYTECLRV CGNWLAETCL ENPAVIMQTY LEKAVEVAGN
YDGESNDELR NGKMKAFLSL ARFSDTQYQR IENYMKSSEF ENKQALLKRA KEEVGLLREH
KIQTNRYTVK VQRELELDEL ALRALKEDRK 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 CEKTMEVMRN SQETLLTIVE VLLYDPLFDW TMNPLKALYL
QQRPEDETEL HPTLNADDQE CKRNLSDIDQ SFNKVAERVL MRLQEKLKGV EEGTVLSVGG
QVNLLIQQAM DPKNLSRLFP GWKAWV
//