Basic Information
Name | Uncharacterized transcriptional regulatory protein TBS1 (Thiabendazole sensitive protein 1) |
Uniprot ID | P38114 |
Systematic gene name | YBR150C |
Standard gene name | TBS1 |
Gene names | TBS1 YBR150C YBR1133 |
Description from SGD | YBR150C TBS1 SGDID:S000000354, Chr II from 544493-541209, Genome Release 64-3-1, reverse complement, Verified ORF, "Protein of unknown function; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; associates with rDNA chromatin in vivo; TBS1 has a paralog, HAL9, that arose from the whole genome duplication" |
Protein length | 1094 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNMDSGITSS HGSMDKTQKQ SSEWAANQKH NQRVENTRVL MGPAVPAMPP
VPSNFPPVPT GTIMSPQLSP FPDHRLRHHP LAHMMPADKN FLAYNMESFK
SRVTKACDYC RKRKIRCTEI EPISGKCRNC IKYNKDCTFH FHEELKRRRE
EALNNKGNGK SVKKPRLDKE NKFKDENFDI AVRSRNTSST DSSPKLHTNL
SQEYIGVSAG KSASDKEDTW PDFVPIDRTV LEKIELNHTK VAGKVFVLEE
ICKNMKGTIE KLAEKSKIDV IDKEYMKRPK RKQYSKALLT KQKMFHFRQN
VLSHLTDEEF LSPINEMFTT TFKYSILQTK LVLDFSFRSA SSPSSDNILY
PLPRLAIAKR LLKNIKCPSL ASLLHIVDVD QCLQFADVHF DPAKGRLTSS
QAFLLNICLC LGATVTNFEE KQELVDEDNH ETYYFEKFEL WRLRSFTFLN
SVYYYHKLSV ARADMTALKA LLLLAKFAQQ KISASSAVKV LSVAIKVALD
LRLNLHSTYE DLELDEIIKR RRLWCYCFST DKFFSVVLSR PPFLKEENTD
VLTDESYVEL FRDKILPNLS IKYDDSKLEG VKDIVSVVNL LANHLEYVPY
IQSYFLSRLS LIESQIYYSC FSIRTTLDDT LDEIIENVLE NQKALDRMRD
DLPTILSLEN YKENMRILSL DSSKLDFEVS CCTTILLHLR WYHQKITLSL
FVISIIGDNL DQRESSRHDI AEIIRRSRLD FKRNCIEVLN ILKDFEYYPT
VQNEFLYFSL TTVFSMFLYL SEIMVNDEHA METGYIIGLL RDTHTRMLGS
EERCLSVHNL KWQTSLFFYT FFLRSTMEKF NLTSKYAKFY AFDSNYYEGV
LNRLVKHTRE SKDDMVELLK TSFINKEKMA AFGSFVTEDQ EKMEVSFNIF
NEITIQDLNF LQFSSIPKLW ENKTLEPGEE YHHSNGTNTD NNETTGADDT
DDNNNNNNNN NKNGNNSSST INNNNNNYSN SNNNDNDNNI NDDDDDDDDD
DDDDDDDDDD DDNDDDYSNN GADDDEEDDD YDRSLFPTGL ASLLDASYPE
RTANDYRDEN EQSNKLFEKI EGHLEHGVFF YDRDFFFKNV CVKM
VPSNFPPVPT GTIMSPQLSP FPDHRLRHHP LAHMMPADKN FLAYNMESFK
SRVTKACDYC RKRKIRCTEI EPISGKCRNC IKYNKDCTFH FHEELKRRRE
EALNNKGNGK SVKKPRLDKE NKFKDENFDI AVRSRNTSST DSSPKLHTNL
SQEYIGVSAG KSASDKEDTW PDFVPIDRTV LEKIELNHTK VAGKVFVLEE
ICKNMKGTIE KLAEKSKIDV IDKEYMKRPK RKQYSKALLT KQKMFHFRQN
VLSHLTDEEF LSPINEMFTT TFKYSILQTK LVLDFSFRSA SSPSSDNILY
PLPRLAIAKR LLKNIKCPSL ASLLHIVDVD QCLQFADVHF DPAKGRLTSS
QAFLLNICLC LGATVTNFEE KQELVDEDNH ETYYFEKFEL WRLRSFTFLN
SVYYYHKLSV ARADMTALKA LLLLAKFAQQ KISASSAVKV LSVAIKVALD
LRLNLHSTYE DLELDEIIKR RRLWCYCFST DKFFSVVLSR PPFLKEENTD
VLTDESYVEL FRDKILPNLS IKYDDSKLEG VKDIVSVVNL LANHLEYVPY
IQSYFLSRLS LIESQIYYSC FSIRTTLDDT LDEIIENVLE NQKALDRMRD
DLPTILSLEN YKENMRILSL DSSKLDFEVS CCTTILLHLR WYHQKITLSL
FVISIIGDNL DQRESSRHDI AEIIRRSRLD FKRNCIEVLN ILKDFEYYPT
VQNEFLYFSL TTVFSMFLYL SEIMVNDEHA METGYIIGLL RDTHTRMLGS
EERCLSVHNL KWQTSLFFYT FFLRSTMEKF NLTSKYAKFY AFDSNYYEGV
LNRLVKHTRE SKDDMVELLK TSFINKEKMA AFGSFVTEDQ EKMEVSFNIF
NEITIQDLNF LQFSSIPKLW ENKTLEPGEE YHHSNGTNTD NNETTGADDT
DDNNNNNNNN NKNGNNSSST INNNNNNYSN SNNNDNDNNI NDDDDDDDDD
DDDDDDDDDD DDNDDDYSNN GADDDEEDDD YDRSLFPTGL ASLLDASYPE
RTANDYRDEN EQSNKLFEKI EGHLEHGVFF YDRDFFFKNV CVKM
Legend
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
Use imported representation
Loading structure from server... It may take a while.
If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.
- Internet Explorer: sorry. IE doesn't support WebGL.
- Firefox (version 4 or later): try force enable WebGL.
- Chrome: try force enable WebGL.
- Safari: enable WebGL.
References
[192, 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) |
[193, 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) |
[193, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[198, 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) |
[198, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[201, 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) |
[201, 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) |
[201, 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) |
[201, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[204, 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) |
[204, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[208, 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) |
[208, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[212, 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) |
[212, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[212, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[214, 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) |
[214, 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) |
[214, 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) |
[214, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[219, 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) |
[219, 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) |
[219, 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) |
[219, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[219, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[570, 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) |
[924, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |