ATM_SCHPO
ID ATM_SCHPO Reviewed; 2812 AA.
AC O74630;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Serine/threonine-protein kinase tel1;
DE EC=2.7.11.1;
DE AltName: Full=ATM homolog;
DE AltName: Full=DNA-damage checkpoint kinase tel1;
DE AltName: Full=Telomere length regulation protein 1;
GN Name=tel1; ORFNames=SPCC23B6.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9771717; DOI=10.1038/2517;
RA Naitoh T., Matsuura A., Ishikawa F.;
RT "Circular chromosome formation in a fission yeast mutant defective in two
RT ATM homologues.";
RL Nat. Genet. 20:203-206(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=10430579; DOI=10.1093/genetics/152.4.1501;
RA Matsuura A., Naito T., Ishikawa F.;
RT "Genetic control of telomere integrity in Schizosaccharomyces pombe:
RT rad3(+) and tel1(+) are parts of two regulatory networks independent of the
RT downstream protein kinases chk1(+) and cds1(+).";
RL Genetics 152:1501-1512(1999).
RN [4]
RP FUNCTION.
RX PubMed=12196391; DOI=10.1093/genetics/161.4.1437;
RA Nakamura T.M., Moser B.A., Russell P.;
RT "Telomere binding of checkpoint sensor and DNA repair proteins contributes
RT to maintenance of functional fission yeast telomeres.";
RL Genetics 161:1437-1452(2002).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION OF HISTONE H2A.
RX PubMed=15226425; DOI=10.1128/mcb.24.14.6215-6230.2004;
RA Nakamura T.M., Du L.-L., Redon C., Russell P.;
RT "Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks,
RT maintains checkpoint arrest, and influences DNA repair in fission yeast.";
RL Mol. Cell. Biol. 24:6215-6230(2004).
RN [6]
RP INTERACTION WITH NBS1, AND PHOSPHORYLATION OF HISTONE H2A.
RX PubMed=15964794; DOI=10.1128/mcb.25.13.5363-5379.2005;
RA You Z., Chahwan C., Bailis J., Hunter T., Russell P.;
RT "ATM activation and its recruitment to damaged DNA require binding to the
RT C-terminus of Nbs1.";
RL Mol. Cell. Biol. 25:5363-5379(2005).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of
CC DNA damage, involved in the regulation of DNA damage response
CC mechanism. Undirectly involved in the phosphorylation of rad32 which is
CC necessary for its telomere function. Required for the control of
CC telomere length and genome stability. {ECO:0000269|PubMed:10430579,
CC ECO:0000269|PubMed:12196391, ECO:0000269|PubMed:15226425,
CC ECO:0000269|PubMed:9771717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
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;
CC -!- SUBUNIT: Interacts with nbs1. This interaction is required for
CC phosphorylation of histone H2A. {ECO:0000269|PubMed:15964794}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}. Note=Localizes to nuclear DNA repair foci with other DNA
CC repair proteins in response to DNA double strand breaks. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
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DR EMBL; AB001995; BAA33817.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB51562.1; -; Genomic_DNA.
DR PIR; T43271; T43271.
DR RefSeq; NP_588126.1; NM_001023116.2.
DR SMR; O74630; -.
DR BioGRID; 275779; 31.
DR IntAct; O74630; 1.
DR STRING; 4896.SPCC23B6.03c.1; -.
DR iPTMnet; O74630; -.
DR PaxDb; O74630; -.
DR PRIDE; O74630; -.
DR EnsemblFungi; SPCC23B6.03c.1; SPCC23B6.03c.1:pep; SPCC23B6.03c.
DR GeneID; 2539209; -.
DR KEGG; spo:SPCC23B6.03c; -.
DR PomBase; SPCC23B6.03c; tel1.
DR VEuPathDB; FungiDB:SPCC23B6.03c; -.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_226973_0_0_1; -.
DR InParanoid; O74630; -.
DR OMA; CGWSAFQ; -.
DR Reactome; R-SPO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SPO-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-SPO-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-69541; Stabilization of p53.
DR Reactome; R-SPO-9664873; Pexophagy.
DR PRO; PR:O74630; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072371; F:histone kinase activity (H2A-S121 specific); EXP:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IMP:CACAO.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:1904514; P:positive regulation of initiation of premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0062209; P:spatial regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR015519; ATM/Tel1.
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; PTHR11139:SF72; PTHR11139:SF72; 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; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; DNA damage; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transferase.
FT CHAIN 1..2812
FT /note="Serine/threonine-protein kinase tel1"
FT /id="PRO_0000227706"
FT DOMAIN 1773..2347
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2449..2758
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2780..2812
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2455..2461
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2627..2635
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2647..2671
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2739..2763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2812 AA; 327145 MW; E3EE5B30C140BBB1 CRC64;
MTSLNDIVNK LSSSKIKTRS DALQNLRSYI IYSRNGNSLN QEDALIIEKA IKRAFELEWQ
ISANHGKRQI SKASQEQKLQ DISYLLRTCV ESYILLFREP HILALLDIIL RHTFTANGSI
CEVVCLNFSK ALRLLLSHSP HLHHLRFSDW QSLVSYCCQA IEKLSIAEET YVSDSEEEPI
SQKNYQEISI WKSHDVIRVK QEVVELIYVM RSLVQWYAAP INFVSEQLLK FFEFFFYAYT
EETDAHLPAL QCLFQLCAYA IPNCNDYSAS VVLLVFKILI NSDKWKRLDL RLQLIQCLAI
SYPLWSNSET WDPHRSIRSF NLDLLNSSFF SLKNFLNFFG KRSSLSLANF RFHTVEPKNN
IAKLYDPRLH LFFSLRHNSF FESYFIYFFL AKLILLKKTV LSLASTEQAN KKQKTCSQIE
ELLLQAELAN ISASSFSLQL MVIITAISDN LTNDDLLSIQ KMSLNFTEKK NELQSWSFFI
LFNICYNKAY SSMLTTSCKK EILAAASRGL LNSVTSPVCY QILTYFNMYR PLCFASIFPF
IKQQFILFND YSPMLSYEAI DYWKSLYILL NENLFVGQSS FKSVFLKWLK WHLYHLFSKE
GELPFFSFTD SSIIIFDLLM MIFYRPLSLS YITTEIRSPF ERNLFHLKEA WSPVTLRFPY
TTDEICKQST EGCYPFNSNH TIDCDSLQNV IKMLESSIDE ISSASYDKDE LDKETPSFEA
VMIFSQISFL CGFLNCFIQK KGIHNVTPNN LVIFKNLFPE VLSFVKSNHS YDPIINCIST
NLQFTISDEP KHLRYEIGSD LIRSTHFRDS NPLKTLVLYI MDMASKNVFI KPQEFDHDEY
FSQEEEDIYR PENLIRNHQI LGLMEGSLEQ IRNTDLFILQ KYIDYFSSHP HDSLINILHL
YPIETFCFGM SAIGAYFLDV ARTSEPIFYK CLEILAQKIL MNYDYERDEV YLMIFIKIFQ
KCVHSKLQFT DATLKLIVKI TKFIEKVFIE TKFSSLSGRQ TFLKFIFQLS PTSHVYSKFD
YQKLISLTLK DSDVCVIYNF VDDLVIFLKK CDKTLIEGFV LPILSIKIEK SLYKGFCYLY
LTLKVFLSIS SNRSALLYQL LKLANSYETS TIFEPLLRKL HIQSANIKQL FRIYRLEIFW
SFVSKDLSNT TNDFLEFPYK PIYFSLSDFL KENSDEIILV LILTKNITLA KLITSRMSVD
FSEKYTQLIP VITTYTHLSE VENKKYSLRF NSIDEALDVE LLNRSKAFLF CLEMLKEVKE
LGSTFKSISS TSFKVYSQLT IFANRVSFNN STAIPFFSTK SVLWYCNRLF QELEGFSSIP
SVIDLVLRRL AIQLHFATDE ELQVTISFRL CAFLCFSDPF ITSNYLVMIV LRIARQLLSI
PCTQSLGLGI ARFHLKKFKP TDFDYFFQLA EFCMDFLGFC YNTIGTKMEA IQDFYTWFDG
YVTALLNFEY EGYGFLRCQI NFVRSVMTTK NEWIEVSNKL FERGHFLKRI AMNNYLCLYF
WQVLDACPRN VLHSLSLEIW KCYKAYDITE FPDSLKLFFS DIMGWNFFKS PEIADLNHYI
PKTDPRLCDT KTYEESKLII WKLICQKACS LLFKYDILLD SFIEDCIRMF FENGNHQELR
KFLNFPKDSI IYDSDFKTLV SEEGSFQWVK LQPTNFDSLS NWTKEETLKL LNMMGKSSTT
HSLKLLSTYM VGFSTSIIQY IIHLILLEFD FNGNNKKQKE YVTQLILSGL LNKNTNSIRK
TCMNILLYLR RQLGHHALNP FEANYWVPIN YSVAASTAYD CHLYEQSLLF LTIHNTKTDE
LDITLLSDIL SQLPCPDAYY GIKRETSFKN ILLKAVHEKR SPLAISYLDA ANMYRSNEDE
GTKMMFSNTL NNAGFFSLNE FYIDSLKAND AIDECSNEVY ASAWRMQKWD IPPLSLDNKT
TKDCLVFEVL HAVHNYAIYG NYLHLEEYIN KKLLLINPNE EPDSLLFYAL AYDLKFLIRC
NQSQFNCDIL QLLKENKQMS SQLHECFQLL LEIRNVLLSL LQSHKQLDLS DDLASFRKYY
ILELLKISES FLIVDNLQNA FSVAMLSDAL YRKFDLADEN LKHDIDFLSS KILWQRDEKI
DAIGMLSESL SKTNSSIFPS ISYAYLGNWL YTTKSEKTEL VSKNYFEKSL SHMSHLNAKE
KAKIYCMFAQ FCDNNYSSPD LTEDFKRMEK LYFEKKNDIQ QLERSIVNAS NMKEEKMLKN
HHSREMSSFI IDEREYLRMS TFRSKMLTQS ITHYLKCLSE SDENDVLISR CCTMWLSNSH
LDELNNSLQH YLQNLPCKKF IPVFYQLAAR LMNENSKFQQ SLTSICYNVG RNHPYHSLHV
LFSLVSNVPE IENLDAGSRY RAVKKILDLL KVNQGLSNLV TKLLCSFENY VSLAEWNPRS
KVDSTSFSRF PGYKWFLKDA ANYGLPPITM NVKVNDTGDY SNIPTVSSFD DTIHFASGIN
APKVITCLGS NGHTYKQLVK GGNDDLRQDA VMEQVFEQVN GFLRSYRKTS QRNLSMRTYK
VIPLALKTGV IEWVQDTIPL GEYLDSAHKV YHPKEWSLST CRKLIAEKQM EDLETRLKVY
DLVCRHYRPV FRHFFLESYA DPVQWFTTQT NYARSTAVAS VLGHVLGLGD RHGQNILIDK
TSGEVIHIDL GIAFEQGKKL PVPECVPFRL TRDVVDGMGI TGVEGVFRRC MEFTLETLRR
EEDSLLSVLE VLRYDPLFSW LISPLRRMKK QKMQLENFNQ PESGNITTDA SRDPKIQRNN
VSGESEAERA ILKVRQKLSS TLSVEASVGE LIRIAQDPSY LALMFCGWSA FQ
