Basic Information
Name | tRNA pseudouridine(32) synthase, mitochondrial (EC 5.4.99.28) (tRNA pseudouridine synthase 9) (tRNA pseudouridylate synthase 9) (tRNA-uridine isomerase 9) |
Uniprot ID | Q12069 |
Systematic gene name | YDL036C |
Standard gene name | PUS9 |
Gene names | PUS9 YDL036C D2743 |
Description from SGD | YDL036C PUS9 SGDID:S000002194, Chr IV from 388901-387513, Genome Release 64-3-1, reverse complement, Verified ORF, "Mitochondrial tRNA:pseudouridine synthase; catalyzes the formation of pseudouridine at position 32 in mitochondrial tRNAs; contains an N-terminal mitochondrial targeting sequence; PUS9 has a paralog, RIB2, that arose from the whole genome duplication" |
Protein length | 462 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MQRNNRLRNL FTVPVIMARQ LKRNALSAGL AFAGNATSNE FDEHLQNEVE
REREIQKKKK IKRTQSKKSP DLINKSTFQS RTIGSKKEKH RQLDPEYEIV
IDGPLRKIKP YHFTYRTFCK ERWRDKKLVD VFISEFRDRE SEYYKRTIEN
GDVHINDETA DLSTVIRNGD LITHQVHRHE PPVTSRPIKV IFEDDNIMVI
DKPSGIPVHP TGRYRFNTIT KMLQNNLGFV VNPCNRLDRL TSGLMFLAKT
PKGADNIGDQ LKAREVTKEY VAKVVGEFPE TEVIVEKPLK LIEPRLALNA
VCQMDEKGAK HAKTVFNRIS YDGKTSIVKC KPLTGRSHQI RVHLQYLGHP
IANDPIYSND EVWGNNLGKG GQADFDIVIT KLDEIGKRKP AKSWFHSNGG
YGEVLRQEKC SICESDLYTD PGPNDLDLWL HAYLYESTET EEGTEKKKWC
YKTEYPEWAL RR
REREIQKKKK IKRTQSKKSP DLINKSTFQS RTIGSKKEKH RQLDPEYEIV
IDGPLRKIKP YHFTYRTFCK ERWRDKKLVD VFISEFRDRE SEYYKRTIEN
GDVHINDETA DLSTVIRNGD LITHQVHRHE PPVTSRPIKV IFEDDNIMVI
DKPSGIPVHP TGRYRFNTIT KMLQNNLGFV VNPCNRLDRL TSGLMFLAKT
PKGADNIGDQ LKAREVTKEY VAKVVGEFPE TEVIVEKPLK LIEPRLALNA
VCQMDEKGAK HAKTVFNRIS YDGKTSIVKC KPLTGRSHQI RVHLQYLGHP
IANDPIYSND EVWGNNLGKG GQADFDIVIT KLDEIGKRKP AKSWFHSNGG
YGEVLRQEKC SICESDLYTD PGPNDLDLWL HAYLYESTET EEGTEKKKWC
YKTEYPEWAL RR
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
[69, 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) |
[69, 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) |
[69, 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) |
[69, 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) |
[69, 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) |
[69, 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) |
[69, 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) |
[69, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |