UniProt ID | TRMB_YEAST | |
---|---|---|
UniProt AC | Q12009 | |
Protein Name | tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055} | |
Gene Name | TRM8 {ECO:0000255|HAMAP-Rule:MF_03055} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 286 | |
Subcellular Localization | Nucleus . | |
Protein Description | Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.. | |
Protein Sequence | MKAKPLSQDPGSKRYAYRINKEENRKELKHVKINESSLVQEGQKIDLPKKRYYRQRAHSNPFSDHQLEYPVSPQDMDWSKLYPYYKNAENGQMTKKVTIADIGCGFGGLMIDLSPAFPEDLILGMEIRVQVTNYVEDRIIALRNNTASKHGFQNINVLRGNAMKFLPNFFEKGQLSKMFFCFPDPHFKQRKHKARIITNTLLSEYAYVLKEGGVVYTITDVKDLHEWMVKHLEEHPLFERLSKEWEENDECVKIMRNATEEGKKVERKKGDKFVACFTRLPTPAIL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Phosphorylation | -MKAKPLSQDPGSKR -CCCCCCCCCCCCHH | 40.85 | 19823750 | |
12 | Phosphorylation | PLSQDPGSKRYAYRI CCCCCCCCHHHEEEC | 21.24 | 19823750 | |
13 | Acetylation | LSQDPGSKRYAYRIN CCCCCCCHHHEEECC | 56.17 | 25381059 | |
21 | Acetylation | RYAYRINKEENRKEL HHEEECCCHHHHHHH | 65.12 | 25381059 | |
32 | Acetylation | RKELKHVKINESSLV HHHHCCCEECHHHHH | 39.26 | 22865919 | |
36 | Phosphorylation | KHVKINESSLVQEGQ CCCEECHHHHHCCCC | 25.20 | 22369663 | |
37 | Phosphorylation | HVKINESSLVQEGQK CCEECHHHHHCCCCC | 26.78 | 22369663 | |
59 | Phosphorylation | YYRQRAHSNPFSDHQ HHHHCCCCCCCCCCC | 45.25 | 17330950 | |
63 | Phosphorylation | RAHSNPFSDHQLEYP CCCCCCCCCCCCCCC | 35.13 | 21551504 | |
69 | Phosphorylation | FSDHQLEYPVSPQDM CCCCCCCCCCCHHHC | 19.95 | 21551504 | |
72 | Phosphorylation | HQLEYPVSPQDMDWS CCCCCCCCHHHCCHH | 16.61 | 24961812 | |
79 | Phosphorylation | SPQDMDWSKLYPYYK CHHHCCHHHHCCCCC | 14.44 | 24961812 | |
149 | Acetylation | LRNNTASKHGFQNIN EECCCHHHCCCCCCC | 45.33 | 22865919 | |
164 | Acetylation | VLRGNAMKFLPNFFE EECCCHHHHCCCHHH | 41.14 | 24489116 | |
172 | Acetylation | FLPNFFEKGQLSKMF HCCCHHHHCCCHHHE | 46.96 | 24489116 | |
230 | Acetylation | DLHEWMVKHLEEHPL HHHHHHHHHHHHCCH | 26.77 | 24489116 | |
282 | Phosphorylation | ACFTRLPTPAIL--- EEEECCCCCCCC--- | 29.91 | 21551504 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRMB_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TRMB_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-37, AND MASSSPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASSSPECTROMETRY. |