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Protein

Serine/threonine-protein kinase TEL1

Gene

TEL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.13 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD
  • telomeric DNA binding Source: SGD

GO - Biological processi

  • cellular response to DNA damage stimulus Source: SGD
  • DNA damage checkpoint Source: InterPro
  • DNA damage induced protein phosphorylation Source: SGD
  • DNA repair Source: SGD
  • double-strand break repair Source: SGD
  • histone phosphorylation Source: SGD
  • phosphorylation Source: SGD
  • replicative senescence Source: InterPro
  • response to ionizing radiation Source: InterPro
  • telomere maintenance Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28977-MONOMER.
ReactomeiR-SCE-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-5693548. Sensing of DNA Double Strand Breaks.
R-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-SCE-6804756. Regulation of TP53 Activity through Phosphorylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase TEL1 (EC:2.7.11.1)
Alternative name(s):
ATM homolog
DNA-damage checkpoint kinase TEL1
Telomere length regulation protein 1
Gene namesi
Name:TEL1
Ordered Locus Names:YBL088C
ORF Names:YBL0706
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL088C.
SGDiS000000184. TEL1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosometelomere 1 Publication

  • Note: Localizes to nuclear DNA repair foci in response to DNA double strand breaks.

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1319 – 13191E → K in TEL1-11; short telomere phenotype and impairs DNA-damage checkpoint function at 37 degrees Celsius. 1 Publication
Mutagenesisi2611 – 26122GD → DA: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with K-2616 and E-2631. 2 Publications
Mutagenesisi2616 – 26161N → K: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with D-2611-2612-A and E-2631. 2 Publications
Mutagenesisi2631 – 26311D → E: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with D-2611-2612-A and K-2616. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27872787Serine/threonine-protein kinase TEL1PRO_0000088839Add
BLAST

Proteomic databases

MaxQBiP38110.

PTM databases

iPTMnetiP38110.

Interactioni

Subunit structurei

Interacts with XRS2 and associates with DNA double-strand breaks.1 Publication

Protein-protein interaction databases

BioGridi32616. 142 interactions.
DIPiDIP-6524N.
IntActiP38110. 5 interactions.
MINTiMINT-631245.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H7BX-ray1.88C/F549-557[»]
3H9HX-ray2.00C/F549-557[»]
3H9SX-ray2.70C549-557[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1734 – 2326593FATPROSITE-ProRule annotationAdd
BLAST
Domaini2461 – 2787327PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2755 – 278733FATCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family. ATM subfamily.Curated
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00670000098061.
HOGENOMiHOG000034179.
InParanoidiP38110.
KOiK04728.
OMAiQDSIMEQ.
OrthoDBiEOG7ZWD92.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR015519. ATM/Tel1.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR014009. PIK_FAT.
IPR021668. TAN.
[Graphical view]
PANTHERiPTHR11139:SF72. PTHR11139:SF72. 6 hits.
PfamiPF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM01342. TAN. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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]

Sequencei

Sequence statusi: Complete.

P38110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDHGIVETL NFLSSTKIKE RNNALDELTT ILKEDPERIP TKALSTTAEA
60 70 80 90 100
LVELLASEHT KYCDLLRNLT VSTTNKLSLS ENRLSTISYV LRLFVEKSCE
110 120 130 140 150
RFKVKTLKLL LAVVPELMVK DGSKSLLDAV SVHLSFALDA LIKSDPFKLK
160 170 180 190 200
FMIHQWISLV DKICEYFQSQ MKLSMVDKTL TNFISILLNL LALDTVGIFQ
210 220 230 240 250
VTRTITWTVI DFLRLSKKEN GNTRLIMSLI NQLILKCHCF SVIDTLMLIK
260 270 280 290 300
EAWSYNLTIG CTSNELVQDQ LSLFDVMSSE LMNHKLPYMI GQENYVEELR
310 320 330 340 350
SESLVSLYRE YILLRLSNYK PQLFTVNHVE FSYIRGSRDK NSWFALPDFR
360 370 380 390 400
LRDRGGRSVW LKILGITKSL LTYFALNRKN ENYSLLFKRR KCDSDIPSIL
410 420 430 440 450
RISDDMDTFL IHLLEENSSH EFEVLGLQLC SFYGTLQDFT KSFAEQLKEL
460 470 480 490 500
LFSKFEKIQC FNWVCFSFIP LLSQKECELS NGDMARLFKV CLPLVKSNES
510 520 530 540 550
CQLSCLLLAN SIKFSKQLLS DEKTINQIYD LYELSDILGP ILVTNESFML
560 570 580 590 600
WGYLQYVGKD FQSMNGISSA DRIFEWLKSK WNQLRGTDAK QDQFCNFISW
610 620 630 640 650
LGNKYDPENP FNDKKGEGAN PVSLCWDESH KIWQHFQEQR EFLLGVKPEE
660 670 680 690 700
KSECFNTPFF NLPKVSLDLT RYNEILYRLL ENIESDAFSS PLQKFTWVAK
710 720 730 740 750
LIQIVDNLCG DSTFSEFIAA YKRTTLITIP QLSFDSQNSY QSFFEEVLSI
760 770 780 790 800
RTINVDHLVL DKINMKEIVN DFIRMQKNKS QTGTSAINYF EASSEDTTQN
810 820 830 840 850
NSPYTIGGRF QKPLHSTIDK AVRAYLWSSR NKSISERLVA ILEFSDCVST
860 870 880 890 900
DVFISYLGTV CQWLKQAIGE KSSYNKILEE FTEVLGEKLL CNHYSSSNQA
910 920 930 940 950
MLLLTSYIEA IRPQWLSYPE QPLNSDCNDI LDWIISRFED NSFTGVAPTV
960 970 980 990 1000
NLSMLLLSLL QNHDLSHGSI RGGKQRVFAT FIKCLQKLDS SNIINIMNSI
1010 1020 1030 1040 1050
SSYMAQVSYK NQSIIFYEIK SLFGPPQQSI EKSAFYSLAM SMLSLVSYPS
1060 1070 1080 1090 1100
LVFSLEDMMT YSGFNHTRAF IQQALNKITV AFRYQNLTEL FEYCKFDLIM
1110 1120 1130 1140 1150
YWFNRTKVPT SKLEKEWDIS LFGFADIHEF LGRYFVEISA IYFSQGFNQK
1160 1170 1180 1190 1200
WILDMLHAIT GNGDAYLVDN SYYLCIPLAF ISGGVNELIF DILPQISGKT
1210 1220 1230 1240 1250
TVKYHKKYRL LMLKWIIRFT DLGSLTELRS TVEKLFPTSY LSPYLFENSS
1260 1270 1280 1290 1300
VSMRYQYPLH IPLALGATLV QTQFAHEKNN THEFKLLFLS VITDLEKTST
1310 1320 1330 1340 1350
YIGKLRCARE LKYLFVLYEN VLVKSSTLNF IIIRLSKFLI DTQIHDEVIT
1360 1370 1380 1390 1400
IFSSLLNLAD KNTFEIEPSL PNLFCKIFIY LRENKQLSPS FQQAIKLLEH
1410 1420 1430 1440 1450
RDLIKIKTWK YCLDAIFGNI VQDDIYENTE LLDASDCGVD DVVLVSLLFS
1460 1470 1480 1490 1500
YARRPVASKI GCSLSKAAAI NILKHHVPKE YLSKNFKLWF AALSRRILQQ
1510 1520 1530 1540 1550
EVQRERSTNF NNEVHLKNFE MVFRHPEQPH MIYQRISTFN KEAELYDSTE
1560 1570 1580 1590 1600
VFFISECILT YLVGYSIGNS ESEFCFRDNI MNENKDKVAP LDKDVLNAIY
1610 1620 1630 1640 1650
PLANNFGMES FICDTYLSVN EPYNCWLSKF ARSLIHQISF NIPPIVCLYP
1660 1670 1680 1690 1700
LCKGSTAFCE LVLTDLFFLS TTYDPKSCLN WSNRIFTQIA MLLHVKDSEI
1710 1720 1730 1740 1750
KLKMLFNVIK MIRMGSRCKE RNCLRIYSSL DLQEICQISL KIKEFKFGYL
1760 1770 1780 1790 1800
LFEEMNMPNI REMNINTLQK IYECINDGDF LAGLPVPHSI EGVLNSINRI
1810 1820 1830 1840 1850
DSDTWKRFLF NNADFDANYT TSLEEEKESL IKATEDSGFY GLTSLLESRL
1860 1870 1880 1890 1900
SGSSDVYKWN LELGDWKLLT PKVVDSKAKG LYYAIKNLPQ DVGFAEKSLE
1910 1920 1930 1940 1950
KSLLTIFDSR QHFISQTEWM DTLNAIIEFI KIAAIPQDVT SFPQTLMSIM
1960 1970 1980 1990 2000
KADKERLNTI DFYDHKTTLK SRHTLMNVLS RNSLDENVKC SKYLRLGSII
2010 2020 2030 2040 2050
QLANYVQLAI ANGAPQDALR NATLMSKTVK NIAKLYDDPS VVSQIEKLAS
2060 2070 2080 2090 2100
FTSANALWES REYKAPVMIM RDLLAQNEKN ISESILYDDF KLLINVPMDQ
2110 2120 2130 2140 2150
IKARLVKWSS ESRLEPAAAI YEKIIVNWDI NVEDHESCSD VFYTLGSFLD
2160 2170 2180 2190 2200
EQAQKLRSNG EIEDREHRSY TGKSTLKALE LIYKNTKLPE NERKDAKRHY
2210 2220 2230 2240 2250
NRVLLQYNRD SEVLKALLLQ KEKFLWHALH FYLNTLVFSN RYDNDIIDKF
2260 2270 2280 2290 2300
CGLWFENDDN SKINQLLYKE IGTIPSWKFL PWVNQIASKI SMEENEFQKP
2310 2320 2330 2340 2350
LQLTMKRLLY KLPYDSLYSV MSILLYEKQS NKDTNISQKI QAVKKILLEL
2360 2370 2380 2390 2400
QGYDRGAFAK KYLLPVQEFC EMSVELANLK FVQNTKTLRL ANLKIGQYWL
2410 2420 2430 2440 2450
KQLNMEKLPL PTSNFTVKSS ADGRKARPYI VSVNETVGIT TTGLSLPKIV
2460 2470 2480 2490 2500
TFNISDGTTQ KALMKGSNDD LRQDAIMEQV FQQVNKVLQN DKVLRNLDLG
2510 2520 2530 2540 2550
IRTYKVVPLG PKAGIIEFVA NSTSLHQILS KLHTNDKITF DQARKGMKAV
2560 2570 2580 2590 2600
QTKSNEERLK AYLKITNEIK PQLRNFFFDS FPDPLDWFEA KKTYTKGVAA
2610 2620 2630 2640 2650
SSIVGYILGL GDRHLNNILL DCSTGEPIHI DLGIAFDQGK LLPIPELVPF
2660 2670 2680 2690 2700
RLTRDIVDGF GVTGVDGLFR RSCERVYAVL RKDYVKVMCV LNILKWDPLY
2710 2720 2730 2740 2750
SWVMSPVKKY EHLFEEEHEI TNFDNVSKFI SNNDRNENQE SYRALKGVEE
2760 2770 2780
KLMGNGLSVE SSVQDLIQQA TDPSNLSVIY MGWSPFY
Length:2,787
Mass (Da):321,524
Last modified:July 27, 2011 - v3
Checksum:iC7FA8C6AFD6B04D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641D → E in AAA69802 (PubMed:7671310).Curated
Sequence conflicti164 – 1641C → W in CAA56016 (PubMed:7502586).Curated
Sequence conflicti1190 – 11901F → Y in CAA56016 (PubMed:7502586).Curated
Sequence conflicti1412 – 14121C → F in CAA56016 (PubMed:7502586).Curated
Sequence conflicti1412 – 14121C → F in CAA84909 (PubMed:7813418).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79489 Genomic DNA. Translation: CAA56016.1.
Z35849 Genomic DNA. Translation: CAA84909.1.
U31331 Genomic DNA. Translation: AAA69802.1.
BK006936 Genomic DNA. Translation: DAA07036.2.
PIRiS45416.
RefSeqiNP_009465.2. NM_001178328.2.

Genome annotation databases

EnsemblFungiiYBL088C; YBL088C; YBL088C.
GeneIDi852190.
KEGGisce:YBL088C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79489 Genomic DNA. Translation: CAA56016.1.
Z35849 Genomic DNA. Translation: CAA84909.1.
U31331 Genomic DNA. Translation: AAA69802.1.
BK006936 Genomic DNA. Translation: DAA07036.2.
PIRiS45416.
RefSeqiNP_009465.2. NM_001178328.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H7BX-ray1.88C/F549-557[»]
3H9HX-ray2.00C/F549-557[»]
3H9SX-ray2.70C549-557[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32616. 142 interactions.
DIPiDIP-6524N.
IntActiP38110. 5 interactions.
MINTiMINT-631245.

PTM databases

iPTMnetiP38110.

Proteomic databases

MaxQBiP38110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL088C; YBL088C; YBL088C.
GeneIDi852190.
KEGGisce:YBL088C.

Organism-specific databases

EuPathDBiFungiDB:YBL088C.
SGDiS000000184. TEL1.

Phylogenomic databases

GeneTreeiENSGT00670000098061.
HOGENOMiHOG000034179.
InParanoidiP38110.
KOiK04728.
OMAiQDSIMEQ.
OrthoDBiEOG7ZWD92.

Enzyme and pathway databases

BioCyciYEAST:G3O-28977-MONOMER.
ReactomeiR-SCE-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SCE-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-SCE-5693548. Sensing of DNA Double Strand Breaks.
R-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-SCE-6804756. Regulation of TP53 Activity through Phosphorylation.

Miscellaneous databases

PROiP38110.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
InterProiIPR015519. ATM/Tel1.
IPR003152. FATC_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR014009. PIK_FAT.
IPR021668. TAN.
[Graphical view]
PANTHERiPTHR11139:SF72. PTHR11139:SF72. 6 hits.
PfamiPF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF11640. TAN. 1 hit.
[Graphical view]
SMARTiSM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
SM01342. TAN. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 1412.
    Strain: ATCC 204508 / S288c.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1284, FUNCTION, MUTAGENESIS OF 2611-GLY-ASP-2612; ASN-2616 AND ASP-2631.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A KINASE, FUNCTION, MUTAGENESIS OF 2611-GLY-ASP-2612; ASN-2616 AND ASP-2631.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The yeast Xrs2 complex functions in S phase checkpoint regulation."
    D'Amours D., Jackson S.P.
    Genes Dev. 15:2238-2249(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Lcd1p recruits Mec1p to DNA lesions in vitro and in vivo."
    Rouse J., Jackson S.P.
    Mol. Cell 9:857-869(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECRUITMENT TO DNA LESIONS.
  12. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH XRS2, ASSOCIATION WITH DNA DOUBLE-STRAND BREAKS.
  14. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF SLX4.
  17. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-1319.

Entry informationi

Entry nameiATM_YEAST
AccessioniPrimary (citable) accession number: P38110
Secondary accession number(s): D6VPR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.