Basic Information
Name | tRNA (guanine(37)-N1)-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5) |
Uniprot ID | P38793 |
Systematic gene name | YHR070W |
Standard gene name | TRM5 |
Gene names | TRM5 YHR070W |
Description from SGD | YHR070W TRM5 SGDID:S000001112, Chr VIII from 234881-236380, Genome Release 64-3-1, Verified ORF, "tRNA(m(1)G37)methyltransferase; methylates a tRNA base adjacent to the anticodon that has a role in prevention of frameshifting; localized to both cytoplasm and mitochondria, and modifies both cytoplasmic and mitochondrial tRNAs; mutations in human ortholog TRMT5 are associated with skeletal muscle respiratory chain deficiencies, and trm5 mutations analogous to disease mutations decrease respiration" |
Protein length | 499 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MKIALPVFQK FNRLISSCKM SGVFPYNPPV NRQMRELDRS FFITKIPMCA
VKFPEPKNIS VFSKNFKNCI LRVPRIPHVV KLNSSKPKDE LTSVQNKKLK
TADGNNTPVT KGVLLHESIH SVEDAYGKLP EDALAFLKEN SAEIVPHEYV
LDYDFWKAEE ILRAVLPEQF LEEVPTGFTI TGHIAHLNLR TEFKPFDSLI
GQVILDKNNK IECVVDKVSS IATQFRTFPM KVIAGKSDSL VVEQKESNCT
FKFDFSKVYW NSRLHTEHER LVKQYFQPGQ VVCDVFAGVG PFAVPAGKKD
VIVLANDLNP ESYKYLKENI ALNKVAKTVK SFNMDGADFI RQSPQLLQQW
IQDEEGGKIT IPLPLKKRHR SQQHNDQQPP QPRTKELIIP SHISHYVMNL
PDSAISFLGN FRGIFAAHTK GATDTIQMPW VHVHCFEKYP PGDQVTEDEL
HARVHARIIA ALKVTADDLP LNAVSLHLVR KVAPTKPMYC ASFQLPANV
VKFPEPKNIS VFSKNFKNCI LRVPRIPHVV KLNSSKPKDE LTSVQNKKLK
TADGNNTPVT KGVLLHESIH SVEDAYGKLP EDALAFLKEN SAEIVPHEYV
LDYDFWKAEE ILRAVLPEQF LEEVPTGFTI TGHIAHLNLR TEFKPFDSLI
GQVILDKNNK IECVVDKVSS IATQFRTFPM KVIAGKSDSL VVEQKESNCT
FKFDFSKVYW NSRLHTEHER LVKQYFQPGQ VVCDVFAGVG PFAVPAGKKD
VIVLANDLNP ESYKYLKENI ALNKVAKTVK SFNMDGADFI RQSPQLLQQW
IQDEEGGKIT IPLPLKKRHR SQQHNDQQPP QPRTKELIIP SHISHYVMNL
PDSAISFLGN FRGIFAAHTK GATDTIQMPW VHVHCFEKYP PGDQVTEDEL
HARVHARIIA ALKVTADDLP LNAVSLHLVR KVAPTKPMYC ASFQLPANV
Legend
- X K-acetylation
- X Phoshorylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[64, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[107, 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) |
[107, 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) |
[107, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[236, Ubi] | 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) |
[239, 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) |
[371, 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) |
[371, 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) |
[371, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |