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Database: UniProt
Entry: O74630
LinkDB: O74630
Original site: O74630 
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   26-NOV-2014, entry version 98.
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. {ECO:0000269|PubMed:10430579,
CC       ECO:0000269|PubMed:12196391, ECO:0000269|PubMed:15226425,
CC       ECO:0000269|PubMed:9771717}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
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
CC       other DNA repair proteins in response to DNA double strand breaks.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 FAT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00534}.
CC   -!- SIMILARITY: Contains 1 FATC domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00535}.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00269}.
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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   BioGrid; 275779; 28.
DR   IntAct; O74630; 1.
DR   MINT; MINT-4680183; -.
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   InParanoid; O74630; -.
DR   KO; K04728; -.
DR   OrthoDB; EOG7ZWD92; -.
DR   Reactome; REACT_214737; ATM mediated response to DNA double-strand break.
DR   Reactome; REACT_218991; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   NextBio; 20800379; -.
DR   PRO; PR:O74630; -.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0016572; P:histone phosphorylation; IGI:PomBase.
DR   GO; GO:0044773; P:mitotic DNA damage checkpoint; NAS:PomBase.
DR   GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR   Gene3D; 1.10.1070.11; -; 3.
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   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; SSF56112; 2.
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; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Telomere; Transferase.
FT   CHAIN         1   2812       Serine/threonine-protein kinase tel1.
FT                                /FTId=PRO_0000227706.
FT   DOMAIN     1773   2347       FAT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00534}.
FT   DOMAIN     2475   2812       PI3K/PI4K. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00269}.
FT   DOMAIN     2780   2812       FATC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00534, ECO:0000255|PROSITE-
FT                                ProRule:PRU00535}.
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
//
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