UniProtKB - P38110 (ATM_YEAST)
Serine/threonine-protein kinase TEL1
TEL1
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 PublicationsCatalytic activityi
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- protein kinase activity Source: SGD
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: SGD
- protein serine kinase activity Source: RHEA
- telomeric DNA binding Source: SGD
GO - Biological processi
- cellular response to DNA damage stimulus Source: SGD
- chromatin organization Source: UniProtKB-KW
- DNA damage checkpoint signaling Source: GO_Central
- DNA damage induced protein phosphorylation Source: SGD
- DNA repair Source: SGD
- double-strand break repair Source: SGD
- histone phosphorylation Source: SGD
- negative regulation of TORC1 signaling Source: GO_Central
- phosphorylation Source: SGD
- protein phosphorylation Source: GO_Central
- telomere maintenance Source: SGD
Keywordsi
Molecular function | Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | DNA damage |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-SCE-2559586, DNA Damage/Telomere Stress Induced Senescence 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-6803207, TP53 Regulates Transcription of Caspase Activators and Caspases R-SCE-6804757, Regulation of TP53 Degradation R-SCE-69541, Stabilization of p53 R-SCE-9664873, Pexophagy |
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 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000000184, TEL1 |
VEuPathDBi | FungiDB:YBL088C |
Subcellular locationi
Mitochondrion
- mitochondrion Source: SGD
Nucleus
- nucleus Source: GO_Central
Other locations
- chromosome, telomeric region Source: UniProtKB-SubCell
Keywords - Cellular componenti
Chromosome, Nucleus, TelomerePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1319 | E → K in TEL1-11; short telomere phenotype and impairs DNA-damage checkpoint function at 37 degrees Celsius. 1 Publication | 1 | |
Mutagenesisi | 2611 – 2612 | GD → DA: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with K-2616 and E-2631. 2 Publications | 2 | |
Mutagenesisi | 2616 | N → K: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with D-2611-2612-A and E-2631. 2 Publications | 1 | |
Mutagenesisi | 2631 | D → E: Short telomere phenotype in vivo and impairs kinase activity in vitro; when associated with D-2611-2612-A and K-2616. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000088839 | 1 – 2787 | Serine/threonine-protein kinase TEL1Add BLAST | 2787 |
Proteomic databases
MaxQBi | P38110 |
PaxDbi | P38110 |
PRIDEi | P38110 |
PTM databases
iPTMneti | P38110 |
Interactioni
Subunit structurei
Interacts with XRS2 and associates with DNA double-strand breaks.
1 PublicationProtein-protein interaction databases
BioGRIDi | 32616, 189 interactors |
DIPi | DIP-6524N |
IntActi | P38110, 6 interactors |
MINTi | P38110 |
STRINGi | 4932.YBL088C |
Miscellaneous databases
RNActi | P38110, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1734 – 2326 | FATPROSITE-ProRule annotationAdd BLAST | 593 | |
Domaini | 2434 – 2746 | PI3K/PI4K catalyticPROSITE-ProRule annotationAdd BLAST | 313 | |
Domaini | 2755 – 2787 | FATCPROSITE-ProRule annotationAdd BLAST | 33 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2440 – 2446 | G-loopPROSITE-ProRule annotation | 7 | |
Regioni | 2609 – 2617 | Catalytic loopPROSITE-ProRule annotation | 9 | |
Regioni | 2629 – 2653 | Activation loopPROSITE-ProRule annotationAdd BLAST | 25 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0892, Eukaryota |
GeneTreei | ENSGT00940000174195 |
HOGENOMi | CLU_000178_8_1_1 |
InParanoidi | P38110 |
OMAi | LDKFCGL |
Family and domain databases
CDDi | cd05171, PIKKc_ATM, 1 hit |
Gene3Di | 1.10.1070.11, 1 hit |
InterProi | View protein in InterPro IPR015519, ATM/Tel1 IPR003152, FATC_dom IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR014009, PIK_FAT IPR044107, PIKKc_ATM IPR021668, TAN |
PANTHERi | PTHR11139:SF72, PTHR11139:SF72, 1 hit |
Pfami | View protein in Pfam PF02260, FATC, 1 hit PF00454, PI3_PI4_kinase, 1 hit PF11640, TAN, 1 hit |
SMARTi | View protein in SMART SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit SM01342, TAN, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in 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 |
i Sequence
Sequence statusi: Complete.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 64 | D → E in AAA69802 (PubMed:7671310).Curated | 1 | |
Sequence conflicti | 164 | C → W in CAA56016 (PubMed:7502586).Curated | 1 | |
Sequence conflicti | 1190 | F → Y in CAA56016 (PubMed:7502586).Curated | 1 | |
Sequence conflicti | 1412 | C → F in CAA56016 (PubMed:7502586).Curated | 1 | |
Sequence conflicti | 1412 | C → F in CAA84909 (PubMed:7813418).Curated | 1 |
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 |
PIRi | S45416 |
RefSeqi | NP_009465.2, NM_001178328.2 |
Genome annotation databases
EnsemblFungii | YBL088C_mRNA; YBL088C; YBL088C |
GeneIDi | 852190 |
KEGGi | sce:YBL088C |
Similar proteinsi
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 |
PIRi | S45416 |
RefSeqi | NP_009465.2, NM_001178328.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3H7B | X-ray | 1.88 | C/F | 549-557 | [»] | |
3H9H | X-ray | 2.00 | C/F | 549-557 | [»] | |
3H9S | X-ray | 2.70 | C | 549-557 | [»] | |
6JXA | electron microscopy | 4.30 | A | 1-2787 | [»] | |
6JXC | electron microscopy | 4.10 | A | 1-2787 | [»] | |
6S8F | electron microscopy | 4.00 | F/H | 968-2787 | [»] | |
SMRi | P38110 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 32616, 189 interactors |
DIPi | DIP-6524N |
IntActi | P38110, 6 interactors |
MINTi | P38110 |
STRINGi | 4932.YBL088C |
PTM databases
iPTMneti | P38110 |
Proteomic databases
MaxQBi | P38110 |
PaxDbi | P38110 |
PRIDEi | P38110 |
Genome annotation databases
EnsemblFungii | YBL088C_mRNA; YBL088C; YBL088C |
GeneIDi | 852190 |
KEGGi | sce:YBL088C |
Organism-specific databases
SGDi | S000000184, TEL1 |
VEuPathDBi | FungiDB:YBL088C |
Phylogenomic databases
eggNOGi | KOG0892, Eukaryota |
GeneTreei | ENSGT00940000174195 |
HOGENOMi | CLU_000178_8_1_1 |
InParanoidi | P38110 |
OMAi | LDKFCGL |
Enzyme and pathway databases
Reactomei | R-SCE-2559586, DNA Damage/Telomere Stress Induced Senescence 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-6803207, TP53 Regulates Transcription of Caspase Activators and Caspases R-SCE-6804757, Regulation of TP53 Degradation R-SCE-69541, Stabilization of p53 R-SCE-9664873, Pexophagy |
Miscellaneous databases
PROi | PR:P38110 |
RNActi | P38110, protein |
Family and domain databases
CDDi | cd05171, PIKKc_ATM, 1 hit |
Gene3Di | 1.10.1070.11, 1 hit |
InterProi | View protein in InterPro IPR015519, ATM/Tel1 IPR003152, FATC_dom IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR014009, PIK_FAT IPR044107, PIKKc_ATM IPR021668, TAN |
PANTHERi | PTHR11139:SF72, PTHR11139:SF72, 1 hit |
Pfami | View protein in Pfam PF02260, FATC, 1 hit PF00454, PI3_PI4_kinase, 1 hit PF11640, TAN, 1 hit |
SMARTi | View protein in SMART SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit SM01342, TAN, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | ATM_YEAST | |
Accessioni | P38110Primary (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: | May 25, 2022 | |
This is version 181 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families