Basic Information

NameTEL2-interacting protein 1
Uniprot IDP36097
Systematic gene nameYKL033W
Standard gene nameTTI1
Gene namesTTI1 FMP47 YKL033W YKL246
Description from SGDYKL033W TTI1 SGDID:S000001516, Chr XI from 375456-378572, Genome Release 64-3-1, Verified ORF, "Subunit of the ASTRA complex, involved in chromatin remodeling; telomere length regulator involved in the stability or biogenesis of PIKKs such as TORC1; similar to S. pombe Tti1p; detected in highly purified mitochondria in high-throughput studies"
Protein length1038
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MNSDTNAFKD IRISCVELSR IAFLPTESFD PNSLTLLACL KKVEEKLSAY
EDDSLSPKFA DYVFVPIASL LKQPALGESQ TEYVLLIIFH LLRTCWSSNG
KFSEQLGQQL FPLITFLVSS DKDNQKLITR SDEFKYAGCL VLHQFFKSVR
SQRYHKEFFS NSKPNLLPAL GHSVTILLKI LEQSPQNNEL QFKALASLEV
LFQDIISDGE MLSFILPGNV SVFAKILTKP GRQIHYKVCV RTLEVLAKLL
VLVYDDFSLD IKVNKLTDIR ELSDTKLKHE INQSFMFNGP IVLLRTDGKT
HRDTSWLTAT SGQINIALEA FIPKLLKRNN ESIDEALATF VSILLTRCEN
SLNNCEKVLV STLVHLERDP MSKLPSHLVK LKEVVNEDLH KLSDIIRFEN
ADRLSSLSFA ITILEKNNER DTMINEVVRC LFESLNESIE PPSLINHKER
IIEQSSQLTT TVNFENLEST NALIALPRLS EDMSLKLKKF TYHMGSLLLE
RHILNDVVTE LISEQVDSPR TQKIVALWLS TNFIKAMEKQ PKEEEVYLQF
ESDANYSSSM VEEVCLIVLE FCNELSQDIS MEIEGKGIKK SDEFAVCTVL
FSIETICAVM REEFQPELID YIYTVVDALA SPSEAIRYVS QSCALRIADT
LYHGSIPNMI LSNVDYLVES ISSRLNSGMT ERVSQILMVI CQLAGYETIE
NFKDVIETIF KLLDYYHGYS DLCLQFFQLF KIIILEMKKK YINDDEMILK
IANQHISQST FSPWGMTDFQ QVLNILDKET QVKDDITDEN DVDFLKDDNE
PSNFQEYFDS KLREPDSDDD EEEREEEVEG SSKEYTDQWT SPIPSDSYKI
LLQILGYGER LLTHPSKRLR VQILIVMRLI FPLLSTQHNL LIREVASTWD
SIIQCVLCSD YSIVQPACSC VEQMIKYSGD FVAKRFIELW QKLCQDSFIL
KELRIDPTVH NHEKKSISKH VKFPPVTENA LVSMVHMVLE GVKITEYLIS
EAVLEQIIYC CIQVVPVEKI SSMSLIVGDI VWKIRNIN

Legend

  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[254, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[258, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[273, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[496, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[787, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[787, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[817, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[817, Phos]Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications)
[817, Phos]Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications)
[817, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[817, Phos]MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications)
[817, Phos]Chen, Y.C.,  Jiang, P.H.,  Chen, H.M.,  Chen, C.H.,  Wang, Y.T.,  Chen, Y.J.,  Yu, C.J.,  Teng, S.C. (2018a). Glucose intake hampers PKA-regulated HSP90 chaperone activity. Elife 7: e39925. (Publication) (All modifications)
[817, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[817, Phos]Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications)
[817, Phos]Soulard, A.,  Cremonesi, A.,  Moes, S.,  Schütz, F.,  Jenö, P.,  Hall, M.N. (2010). The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates. Molecular Biology of the Cell 21(19): 3475-3486. (Publication) (All modifications)
[817, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[831, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[831, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)