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 01-MAY-2013, entry version 87.
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;
OC Schizosaccharomycetaceae; 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
RT two 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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=10430579;
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
RT of the downstream protein kinases chk1(+) and cds1(+).";
RL Genetics 152:1501-1512(1999).
RN [4]
RP FUNCTION.
RX PubMed=12196391;
RA Nakamura T.M., Moser B.A., Russell P.;
RT "Telomere binding of checkpoint sensor and DNA repair proteins
RT contributes 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
RT 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
RT the C-terminus of Nbs1.";
RL Mol. Cell. Biol. 25:5363-5379(2005).
CC -!- FUNCTION: Serine/threonine protein kinase which activates
CC checkpoint signaling upon genotoxic stresses such as ionizing
CC radiation (IR), ultraviolet light (UV), or DNA replication
CC stalling, thereby acting as a DNA damage sensor. Recognizes the
CC substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to
CC form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the
CC regulation of DNA damage response mechanism. Undirectly involved
CC in the phosphorylation of rad32 which is necessary for its
CC telomere function. Required for the control of telomere length and
CC genome stability.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Interacts with nbs1. This interaction is required for
CC phosphorylation of histone H2A.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome,
CC telomere (By similarity). Note=Localizes to nuclear DNA repair
CC foci with other DNA repair proteins in response to DNA double
CC strand breaks (By similarity).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC -!- SIMILARITY: Contains 1 FAT domain.
CC -!- SIMILARITY: Contains 1 FATC domain.
CC -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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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 ProteinModelPortal; O74630; -.
DR IntAct; O74630; 1.
DR STRING; 4896.SPCC23B6.03c-1; -.
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; -.
DR eggNOG; COG5032; -.
DR KO; K04728; -.
DR OrthoDB; EOG41G6C5; -.
DR NextBio; 20800379; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0000077; P:DNA damage checkpoint; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016572; P:histone phosphorylation; IGI:PomBase.
DR GO; GO:0090399; P:replicative senescence; IEA:InterPro.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR Gene3D; 1.10.1070.11; -; 3.
DR InterPro; IPR015519; ATM/Tel1.
DR InterPro; IPR003152; FATC.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR11139:SF3; PTHR11139:SF3; 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; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Kinase_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 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; Complete proteome;
KW DNA damage; DNA repair; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Telomere;
KW Transferase.
FT CHAIN 1 2812 Serine/threonine-protein kinase tel1.
FT /FTId=PRO_0000227706.
FT DOMAIN 1773 2347 FAT.
FT DOMAIN 2475 2812 PI3K/PI4K.
FT DOMAIN 2780 2812 FATC.
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
//
