Reviewed, UniProtKB/Swiss-Prot P38110 (ATM_YEAST)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase TEL1
    EC=2.7.11.1
Alternative name(s):
    DNA-damage checkpoint kinase TEL1
    Telomere length regulation protein 1
    ATM homolog

Gene names

Name:	TEL1
Ordered Locus Names:	YBL088C
ORF Names:	YBL0706

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2787 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited by the MRX-complex to sites of DNA lesions immediately after damage to initiate non-homologous end-joining (NHEJ). Subsequently displaced by the RPA complex in a reaction probably involving the SAE2 protein. Phosphorylates MRE11 and XRS2, 2 subunits of the MRX-complex. The phosphorylation of MRE11 is a feedback response from the checkpoint signaling pathway. Phosphorylates RAD9, CHK1 and RAD53, leading to the activation of the CHK1 and RAD23 kinases involved in the DNA damage response cascade. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Phosphorylates also SLX4 and RTT107 which are involved in genome stability. Required for the control of telomere length and genome stability. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with XRS2 and associates with DNA double-strand breaks. Ref.12
Subcellular location	Nucleus. Telomere. Note: Localizes to nuclear DNA repair foci in response to DNA double strand breaks. Ref.13
Sequence similarities	Belongs to the PI3/PI4-kinase family. ATM subfamily. Contains 1 FAT domain. Contains 1 FATC domain. Contains 1 PI3K/PI4K domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosomal protein Nucleus Telomere
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA damage induced protein phosphorylation Inferred from mutant phenotype. Source: SGD double-strand break repair Inferred from genetic interaction. Source: SGD histone phosphorylation Inferred from genetic interaction. Source: SGD telomere maintenance via telomerase Inferred from mutant phenotype. Source: SGD
Cellular component	chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: SGD nucleus Traceable author statement. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW telomeric DNA binding Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GDE1	Q02979	1	EBI-19099,EBI-31287

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2787	2787	Serine/threonine-protein kinase TEL1		PRO_0000088839
Regions
	Domain	1734 – 2326	593	FAT
	Domain	2461 – 2787	327	PI3K/PI4K
	Domain	2755 – 2787	33	FATC
Experimental info
	Mutagenesis	1319	1	E → K in TEL1-11; short telomere phenotype and impairs DNA-damage checkpoint function at 37 degrees Celsius. Ref.16
	Mutagenesis	2611 – 2612	2	GD → DA: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with K-2616 and E-2631.
	Mutagenesis	2616	1	N → K: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with D-2611-2612-A and E-2631. Ref.3 Ref.5
	Mutagenesis	2631	1	D → E: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with D-2611-2612-A and K-2616. Ref.3 Ref.5
	Sequence conflict	64	1	D → E in AAA69802. Ref.3
	Sequence conflict	164	1	C → W in CAA56016. Ref.1
	Sequence conflict	1190	1	F → Y in CAA56016. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38110-1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: CF158AD96B363932	FASTA	2,787	321,569
	10 20 30 40 50 60 MEDHGIVETL NFLSSTKIKE RNNALDELTT ILKEDPERIP TKALSTTAEA LVELLASEHT 70 80 90 100 110 120 KYCDLLRNLT VSTTNKLSLS ENRLSTISYV LRLFVEKSCE RFKVKTLKLL LAVVPELMVK 130 140 150 160 170 180 DGSKSLLDAV SVHLSFALDA LIKSDPFKLK FMIHQWISLV DKICEYFQSQ MKLSMVDKTL 190 200 210 220 230 240 TNFISILLNL LALDTVGIFQ VTRTITWTVI DFLRLSKKEN GNTRLIMSLI NQLILKCHCF 250 260 270 280 290 300 SVIDTLMLIK EAWSYNLTIG CTSNELVQDQ LSLFDVMSSE LMNHKLPYMI GQENYVEELR 310 320 330 340 350 360 SESLVSLYRE YILLRLSNYK PQLFTVNHVE FSYIRGSRDK NSWFALPDFR LRDRGGRSVW 370 380 390 400 410 420 LKILGITKSL LTYFALNRKN ENYSLLFKRR KCDSDIPSIL RISDDMDTFL IHLLEENSSH 430 440 450 460 470 480 EFEVLGLQLC SFYGTLQDFT KSFAEQLKEL LFSKFEKIQC FNWVCFSFIP LLSQKECELS 490 500 510 520 530 540 NGDMARLFKV CLPLVKSNES CQLSCLLLAN SIKFSKQLLS DEKTINQIYD LYELSDILGP 550 560 570 580 590 600 ILVTNESFML WGYLQYVGKD FQSMNGISSA DRIFEWLKSK WNQLRGTDAK QDQFCNFISW 610 620 630 640 650 660 LGNKYDPENP FNDKKGEGAN PVSLCWDESH KIWQHFQEQR EFLLGVKPEE KSECFNTPFF 670 680 690 700 710 720 NLPKVSLDLT RYNEILYRLL ENIESDAFSS PLQKFTWVAK LIQIVDNLCG DSTFSEFIAA 730 740 750 760 770 780 YKRTTLITIP QLSFDSQNSY QSFFEEVLSI RTINVDHLVL DKINMKEIVN DFIRMQKNKS 790 800 810 820 830 840 QTGTSAINYF EASSEDTTQN NSPYTIGGRF QKPLHSTIDK AVRAYLWSSR NKSISERLVA 850 860 870 880 890 900 ILEFSDCVST DVFISYLGTV CQWLKQAIGE KSSYNKILEE FTEVLGEKLL CNHYSSSNQA 910 920 930 940 950 960 MLLLTSYIEA IRPQWLSYPE QPLNSDCNDI LDWIISRFED NSFTGVAPTV NLSMLLLSLL 970 980 990 1000 1010 1020 QNHDLSHGSI RGGKQRVFAT FIKCLQKLDS SNIINIMNSI SSYMAQVSYK NQSIIFYEIK 1030 1040 1050 1060 1070 1080 SLFGPPQQSI EKSAFYSLAM SMLSLVSYPS LVFSLEDMMT YSGFNHTRAF IQQALNKITV 1090 1100 1110 1120 1130 1140 AFRYQNLTEL FEYCKFDLIM YWFNRTKVPT SKLEKEWDIS LFGFADIHEF LGRYFVEISA 1150 1160 1170 1180 1190 1200 IYFSQGFNQK WILDMLHAIT GNGDAYLVDN SYYLCIPLAF ISGGVNELIF DILPQISGKT 1210 1220 1230 1240 1250 1260 TVKYHKKYRL LMLKWIIRFT DLGSLTELRS TVEKLFPTSY LSPYLFENSS VSMRYQYPLH 1270 1280 1290 1300 1310 1320 IPLALGATLV QTQFAHEKNN THEFKLLFLS VITDLEKTST YIGKLRCARE LKYLFVLYEN 1330 1340 1350 1360 1370 1380 VLVKSSTLNF IIIRLSKFLI DTQIHDEVIT IFSSLLNLAD KNTFEIEPSL PNLFCKIFIY 1390 1400 1410 1420 1430 1440 LRENKQLSPS FQQAIKLLEH RDLIKIKTWK YFLDAIFGNI VQDDIYENTE LLDASDCGVD 1450 1460 1470 1480 1490 1500 DVVLVSLLFS YARRPVASKI GCSLSKAAAI NILKHHVPKE YLSKNFKLWF AALSRRILQQ 1510 1520 1530 1540 1550 1560 EVQRERSTNF NNEVHLKNFE MVFRHPEQPH MIYQRISTFN KEAELYDSTE VFFISECILT 1570 1580 1590 1600 1610 1620 YLVGYSIGNS ESEFCFRDNI MNENKDKVAP LDKDVLNAIY PLANNFGMES FICDTYLSVN 1630 1640 1650 1660 1670 1680 EPYNCWLSKF ARSLIHQISF NIPPIVCLYP LCKGSTAFCE LVLTDLFFLS TTYDPKSCLN 1690 1700 1710 1720 1730 1740 WSNRIFTQIA MLLHVKDSEI KLKMLFNVIK MIRMGSRCKE RNCLRIYSSL DLQEICQISL 1750 1760 1770 1780 1790 1800 KIKEFKFGYL LFEEMNMPNI REMNINTLQK IYECINDGDF LAGLPVPHSI EGVLNSINRI 1810 1820 1830 1840 1850 1860 DSDTWKRFLF NNADFDANYT TSLEEEKESL IKATEDSGFY GLTSLLESRL SGSSDVYKWN 1870 1880 1890 1900 1910 1920 LELGDWKLLT PKVVDSKAKG LYYAIKNLPQ DVGFAEKSLE KSLLTIFDSR QHFISQTEWM 1930 1940 1950 1960 1970 1980 DTLNAIIEFI KIAAIPQDVT SFPQTLMSIM KADKERLNTI DFYDHKTTLK SRHTLMNVLS 1990 2000 2010 2020 2030 2040 RNSLDENVKC SKYLRLGSII QLANYVQLAI ANGAPQDALR NATLMSKTVK NIAKLYDDPS 2050 2060 2070 2080 2090 2100 VVSQIEKLAS FTSANALWES REYKAPVMIM RDLLAQNEKN ISESILYDDF KLLINVPMDQ 2110 2120 2130 2140 2150 2160 IKARLVKWSS ESRLEPAAAI YEKIIVNWDI NVEDHESCSD VFYTLGSFLD EQAQKLRSNG 2170 2180 2190 2200 2210 2220 EIEDREHRSY TGKSTLKALE LIYKNTKLPE NERKDAKRHY NRVLLQYNRD SEVLKALLLQ 2230 2240 2250 2260 2270 2280 KEKFLWHALH FYLNTLVFSN RYDNDIIDKF CGLWFENDDN SKINQLLYKE IGTIPSWKFL 2290 2300 2310 2320 2330 2340 PWVNQIASKI SMEENEFQKP LQLTMKRLLY KLPYDSLYSV MSILLYEKQS NKDTNISQKI 2350 2360 2370 2380 2390 2400 QAVKKILLEL QGYDRGAFAK KYLLPVQEFC EMSVELANLK FVQNTKTLRL ANLKIGQYWL 2410 2420 2430 2440 2450 2460 KQLNMEKLPL PTSNFTVKSS ADGRKARPYI VSVNETVGIT TTGLSLPKIV TFNISDGTTQ 2470 2480 2490 2500 2510 2520 KALMKGSNDD LRQDAIMEQV FQQVNKVLQN DKVLRNLDLG IRTYKVVPLG PKAGIIEFVA 2530 2540 2550 2560 2570 2580 NSTSLHQILS KLHTNDKITF DQARKGMKAV QTKSNEERLK AYLKITNEIK PQLRNFFFDS 2590 2600 2610 2620 2630 2640 FPDPLDWFEA KKTYTKGVAA SSIVGYILGL GDRHLNNILL DCSTGEPIHI DLGIAFDQGK 2650 2660 2670 2680 2690 2700 LLPIPELVPF RLTRDIVDGF GVTGVDGLFR RSCERVYAVL RKDYVKVMCV LNILKWDPLY 2710 2720 2730 2740 2750 2760 SWVMSPVKKY EHLFEEEHEI TNFDNVSKFI SNNDRNENQE SYRALKGVEE KLMGNGLSVE 2770 2780 SSVQDLIQQA TDPSNLSVIY MGWSPFY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"TEL1, a gene involved in controlling telomere length in S. cerevisiae, is homologous to the human ataxia telangiectasia gene." Greenwell P.W., Kronmal S.L., Porter S.E., Gassenhuber J., Obermaier B., Petes T.D. Cell 82:823-829(1995) [PubMed: 7671310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1284, FUNCTION, MUTAGENESIS OF 2611-GLY-ASP-2612; ASN-2616 AND ASP-2631.
[4]	"Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast cell cycle checkpoint pathways." Sanchez Y., Desany B.A., Jones W.J., Liu Q., Wang B., Elledge S.J. Science 271:357-360(1996) [PubMed: 8553072] [Abstract] Cited for: FUNCTION.
[5]	"Protein kinase activity of Tel1p and Mec1p, two Saccharomyces cerevisiae proteins related to the human ATM protein kinase." Mallory J.C., Petes T.D. Proc. Natl. Acad. Sci. U.S.A. 97:13749-13754(2000) [PubMed: 11095737] [Abstract] Cited for: IDENTIFICATION AS A KINASE, FUNCTION, MUTAGENESIS OF 2611-GLY-ASP-2612; ASN-2616 AND ASP-2631.
[6]	"Hyperactivation of the yeast DNA damage checkpoint by TEL1 and DDC2 overexpression." Clerici M., Paciotti V., Baldo V., Romano M., Lucchini G., Longhese M.P. EMBO J. 20:6485-6498(2001) [PubMed: 11707419] [Abstract] Cited for: FUNCTION.
[7]	"Suppression of spontaneous chromosomal rearrangements by S phase checkpoint functions in Saccharomyces cerevisiae." Myung K., Datta A., Kolodner R.D. Cell 104:397-408(2001) [PubMed: 11239397] [Abstract] Cited for: FUNCTION.
[8]	"The yeast Xrs2 complex functions in S phase checkpoint regulation." D'Amours D., Jackson S.P. Genes Dev. 15:2238-2249(2001) [PubMed: 11544181] [Abstract] Cited for: FUNCTION.
[9]	"A DNA damage response pathway controlled by Tel1 and the Mre11 complex." Usui T., Ogawa H., Petrini J.H.J. Mol. Cell 7:1255-1266(2001) [PubMed: 11430828] [Abstract] Cited for: FUNCTION.
[10]	"Lcd1p recruits Mec1p to DNA lesions in vitro and in vivo." Rouse J., Jackson S.P. Mol. Cell 9:857-869(2002) [PubMed: 11983176] [Abstract] Cited for: RECRUITMENT TO DNA LESIONS.
[11]	"Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage." Redon C., Pilch D.R., Rogakou E.P., Orr A.H., Lowndes N.F., Bonner W.M. EMBO Rep. 4:678-684(2003) [PubMed: 12792653] [Abstract] Cited for: FUNCTION.
[12]	"ATM-related Tel1 associates with double-strand breaks through an Xrs2-dependent mechanism." Nakada D., Matsumoto K., Sugimoto K. Genes Dev. 17:1957-1962(2003) [PubMed: 12923051] [Abstract] Cited for: FUNCTION, INTERACTION WITH XRS2, ASSOCIATION WITH DNA DOUBLE-STRAND BREAKS.
[13]	"Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins." Lisby M., Barlow J.H., Burgess R.C., Rothstein R. Cell 118:699-713(2004) [PubMed: 15369670] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break." Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M., Petrini J.H.J., Haber J.E., Lichten M. Curr. Biol. 14:1703-1711(2004) [PubMed: 15458641] [Abstract] Cited for: FUNCTION.
[15]	"Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent manner and is required for repair of DNA alkylation damage." Flott S., Rouse J. Biochem. J. 391:325-333(2005) [PubMed: 15975089] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION OF SLX4.
[16]	"A mutation in yeast Tel1p that causes differential effects on the DNA damage checkpoint and telomere maintenance." Chakhparonian M., Faucher D., Wellinger R.J. Curr. Genet. 48:310-322(2005) [PubMed: 16228207] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-1319.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X79489 Genomic DNA. Translation: CAA56016.1. Z35849 Genomic DNA. Translation: CAA84909.1. U31331 Genomic DNA. Translation: AAA69802.1.
PIR	S45416.
RefSeq	NP_009465.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6524N.
IntAct	P38110. 11 interactions.
STRING	P38110.
Proteomic databases
PeptideAtlas	P38110.
Genome annotation databases
Ensembl	YBL088C; YBL088C; YBL088C; Saccharomyces cerevisiae. [Genome view]
GeneID	852190.
KEGG	sce:YBL088C.
NMPDR	fig|4932.3.peg.151.
Organism-specific databases
CYGD	YBL088c.
SGD	S000000184. TEL1.
Phylogenomic databases
HOGENOM	P38110.
OMA	QDSIMEQ
OrthoDB	EOG9S4QZV
Enzyme and pathway databases
BRENDA	2.7.11.1. 250.
Gene expression databases
ArrayExpress	P38110.
Genevestigator	P38110.
GermOnline	YBL088C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR015519. Ataxia_Telang_Mut. IPR003152. FATC. IPR011009. Kinase-like_dom. IPR000403. PI3/4_kinase_cat. IPR018936. PI3/4_kinase_CS. IPR014009. PIK_FAT. [Graphical view]
Gene3D	G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
PANTHER	PTHR11139:SF3. Ataxia_Telang_Mut. 1 hit.
Pfam	PF02260. FATC. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	970667.

Entry information

Entry name

ATM_YEAST

Accession

Primary (citable) accession number: P38110

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	September 5, 2006
Last modified:	November 24, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)