TEL1/YBL088C Protein Information Help

Standard Name Tel1p 1
Systematic Name Ybl088cp
ORF Classification Verified
Description Protein kinase primarily involved in telomere length regulation; contributes to cell cycle checkpoint control in response to DNA damage; functionally redundant with Mec1p; regulates P-body formation induced by replication stress; homolog of human ataxia-telangiectasia mutated (ATM) gene, the gene responsible for ataxia telangiectasia (AT) (OMIM 607585) (2, 3, 4, 5, 6)
Name Description TELomere maintenance 1
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 2,787
Molecular Weight (Da) 321,524
Isoelectric Point (pI) 6.92

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Tel1p (InterPro)
Physical Interactions There are 20 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0001F7BD2C | P38110
MIPS: YBL088C
NCBI: 1870083 | 330443403 | 341940587 | 496689 | 586447 | 896461 | NP_009465.2
GenBank/EMBL/DDBJ: DAA07036.2 | U31331 | X79489 | Z35849
External Classifications EC: 2.7.11.1 [Non-specific serine/threonine protein kinase]
Amino Acid Sequence (or in FASTA format)
       1  MEDHGIVETL NFLSSTKIKE RNNALDELTT ILKEDPERIP TKALSTTAEA
      51  LVELLASEHT KYCDLLRNLT VSTTNKLSLS ENRLSTISYV LRLFVEKSCE
     101  RFKVKTLKLL LAVVPELMVK DGSKSLLDAV SVHLSFALDA LIKSDPFKLK
     151  FMIHQWISLV DKICEYFQSQ MKLSMVDKTL TNFISILLNL LALDTVGIFQ
     201  VTRTITWTVI DFLRLSKKEN GNTRLIMSLI NQLILKCHCF SVIDTLMLIK
     251  EAWSYNLTIG CTSNELVQDQ LSLFDVMSSE LMNHKLPYMI GQENYVEELR
     301  SESLVSLYRE YILLRLSNYK PQLFTVNHVE FSYIRGSRDK NSWFALPDFR
     351  LRDRGGRSVW LKILGITKSL LTYFALNRKN ENYSLLFKRR KCDSDIPSIL
     401  RISDDMDTFL IHLLEENSSH EFEVLGLQLC SFYGTLQDFT KSFAEQLKEL
     451  LFSKFEKIQC FNWVCFSFIP LLSQKECELS NGDMARLFKV CLPLVKSNES
     501  CQLSCLLLAN SIKFSKQLLS DEKTINQIYD LYELSDILGP ILVTNESFML
     551  WGYLQYVGKD FQSMNGISSA DRIFEWLKSK WNQLRGTDAK QDQFCNFISW
     601  LGNKYDPENP FNDKKGEGAN PVSLCWDESH KIWQHFQEQR EFLLGVKPEE
     651  KSECFNTPFF NLPKVSLDLT RYNEILYRLL ENIESDAFSS PLQKFTWVAK
     701  LIQIVDNLCG DSTFSEFIAA YKRTTLITIP QLSFDSQNSY QSFFEEVLSI
     751  RTINVDHLVL DKINMKEIVN DFIRMQKNKS QTGTSAINYF EASSEDTTQN
     801  NSPYTIGGRF QKPLHSTIDK AVRAYLWSSR NKSISERLVA ILEFSDCVST
     851  DVFISYLGTV CQWLKQAIGE KSSYNKILEE FTEVLGEKLL CNHYSSSNQA
     901  MLLLTSYIEA IRPQWLSYPE QPLNSDCNDI LDWIISRFED NSFTGVAPTV
     951  NLSMLLLSLL QNHDLSHGSI RGGKQRVFAT FIKCLQKLDS SNIINIMNSI
    1001  SSYMAQVSYK NQSIIFYEIK SLFGPPQQSI EKSAFYSLAM SMLSLVSYPS
    1051  LVFSLEDMMT YSGFNHTRAF IQQALNKITV AFRYQNLTEL FEYCKFDLIM
    1101  YWFNRTKVPT SKLEKEWDIS LFGFADIHEF LGRYFVEISA IYFSQGFNQK
    1151  WILDMLHAIT GNGDAYLVDN SYYLCIPLAF ISGGVNELIF DILPQISGKT
    1201  TVKYHKKYRL LMLKWIIRFT DLGSLTELRS TVEKLFPTSY LSPYLFENSS
    1251  VSMRYQYPLH IPLALGATLV QTQFAHEKNN THEFKLLFLS VITDLEKTST
    1301  YIGKLRCARE LKYLFVLYEN VLVKSSTLNF IIIRLSKFLI DTQIHDEVIT
    1351  IFSSLLNLAD KNTFEIEPSL PNLFCKIFIY LRENKQLSPS FQQAIKLLEH
    1401  RDLIKIKTWK YCLDAIFGNI VQDDIYENTE LLDASDCGVD DVVLVSLLFS
    1451  YARRPVASKI GCSLSKAAAI NILKHHVPKE YLSKNFKLWF AALSRRILQQ
    1501  EVQRERSTNF NNEVHLKNFE MVFRHPEQPH MIYQRISTFN KEAELYDSTE
    1551  VFFISECILT YLVGYSIGNS ESEFCFRDNI MNENKDKVAP LDKDVLNAIY
    1601  PLANNFGMES FICDTYLSVN EPYNCWLSKF ARSLIHQISF NIPPIVCLYP
    1651  LCKGSTAFCE LVLTDLFFLS TTYDPKSCLN WSNRIFTQIA MLLHVKDSEI
    1701  KLKMLFNVIK MIRMGSRCKE RNCLRIYSSL DLQEICQISL KIKEFKFGYL
    1751  LFEEMNMPNI REMNINTLQK IYECINDGDF LAGLPVPHSI EGVLNSINRI
    1801  DSDTWKRFLF NNADFDANYT TSLEEEKESL IKATEDSGFY GLTSLLESRL
    1851  SGSSDVYKWN LELGDWKLLT PKVVDSKAKG LYYAIKNLPQ DVGFAEKSLE
    1901  KSLLTIFDSR QHFISQTEWM DTLNAIIEFI KIAAIPQDVT SFPQTLMSIM
    1951  KADKERLNTI DFYDHKTTLK SRHTLMNVLS RNSLDENVKC SKYLRLGSII
    2001  QLANYVQLAI ANGAPQDALR NATLMSKTVK NIAKLYDDPS VVSQIEKLAS
    2051  FTSANALWES REYKAPVMIM RDLLAQNEKN ISESILYDDF KLLINVPMDQ
    2101  IKARLVKWSS ESRLEPAAAI YEKIIVNWDI NVEDHESCSD VFYTLGSFLD
    2151  EQAQKLRSNG EIEDREHRSY TGKSTLKALE LIYKNTKLPE NERKDAKRHY
    2201  NRVLLQYNRD SEVLKALLLQ KEKFLWHALH FYLNTLVFSN RYDNDIIDKF
    2251  CGLWFENDDN SKINQLLYKE IGTIPSWKFL PWVNQIASKI SMEENEFQKP
    2301  LQLTMKRLLY KLPYDSLYSV MSILLYEKQS NKDTNISQKI QAVKKILLEL
    2351  QGYDRGAFAK KYLLPVQEFC EMSVELANLK FVQNTKTLRL ANLKIGQYWL
    2401  KQLNMEKLPL PTSNFTVKSS ADGRKARPYI VSVNETVGIT TTGLSLPKIV
    2451  TFNISDGTTQ KALMKGSNDD LRQDAIMEQV FQQVNKVLQN DKVLRNLDLG
    2501  IRTYKVVPLG PKAGIIEFVA NSTSLHQILS KLHTNDKITF DQARKGMKAV
    2551  QTKSNEERLK AYLKITNEIK PQLRNFFFDS FPDPLDWFEA KKTYTKGVAA
    2601  SSIVGYILGL GDRHLNNILL DCSTGEPIHI DLGIAFDQGK LLPIPELVPF
    2651  RLTRDIVDGF GVTGVDGLFR RSCERVYAVL RKDYVKVMCV LNILKWDPLY
    2701  SWVMSPVKKY EHLFEEEHEI TNFDNVSKFI SNNDRNENQE SYRALKGVEE
    2751  KLMGNGLSVE SSVQDLIQQA TDPSNLSVIY MGWSPFY*             

external links for Tel1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Candida (CGD) BioPIXIE MIPS
Candida (CandidaDB) CYC2008 (complexes) Pfam domains
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Tel1p
1) Lustig AJ and Petes TD  (1986) Identification of yeast mutants with altered telomere structure. Proc Natl Acad Sci U S A 83(5):1398-402
2) Ritchie KB and Petes TD  (2000) The Mre11p/Rad50p/Xrs2p complex and the Tel1p function in a single pathway for telomere maintenance in yeast. Genetics 155(1):475-9
3) Craven RJ, et al.  (2002) Regulation of genome stability by TEL1 and MEC1, yeast homologs of the mammalian ATM and ATR genes. Genetics 161(2):493-507
4) Giannattasio M, et al.  (2002) A dominant-negative MEC3 mutant uncovers new functions for the Rad17 complex and Tel1. Proc Natl Acad Sci U S A 99(20):12997-3002
5) Nakada D, et al.  (2003) The ATM-related Tel1 protein of Saccharomyces cerevisiae controls a checkpoint response following phleomycin treatment. Nucleic Acids Res 31(6):1715-24
6) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76