UniProt ID | TRM82_YEAST | |
---|---|---|
UniProt AC | Q03774 | |
Protein Name | tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82 {ECO:0000255|HAMAP-Rule:MF_03056} | |
Gene Name | TRM82 {ECO:0000255|HAMAP-Rule:MF_03056} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 444 | |
Subcellular Localization | Nucleus . | |
Protein Description | Required for 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. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.. | |
Protein Sequence | MSVIHPLQNLLTSRDGSLVFAIIKNCILSFKYQSPNHWEFAGKWSDDFDKIQESRNTTAKEQQGQSSENENENKKLKSNKGDSIKRTAAKVPSPGLGAPPIYSYIRNLRLTSDESRLIACADSDKSLLVFDVDKTSKNVLKLRKRFCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFTQEPILGHVSMLTDVHLIKDSDGHQFIITSDRDEHIKISHYPQCFIVDKWLFGHKHFVSSICCGKDYLLLSAGGDDKIFAWDWKTGKNLSTFDYNSLIKPYLNDQHLAPPRFQNENNDIIEFAVSKIIKSKNLPFVAFFVEATKCIIILEMSEKQKGDLALKQIITFPYNVISLSAHNDEFQVTLDNKESSGVQKNFAKFIEYNLNENSFVVNNEKSNEFDSAIIQSVQGDSNLVTKKEEIYPLYNVSSLRKHGEHYS | |
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 |
---|---|---|---|---|---|
31 | Ubiquitination | KNCILSFKYQSPNHW HHHEEEEEECCCCCC | 38.72 | 23749301 | |
50 | Acetylation | KWSDDFDKIQESRNT ECCCCHHHHHHHHHC | 46.40 | 24489116 | |
66 | Phosphorylation | AKEQQGQSSENENEN HHHHHCCCCCCHHHH | 46.58 | 28889911 | |
67 | Phosphorylation | KEQQGQSSENENENK HHHHCCCCCCHHHHH | 36.23 | 17563356 | |
85 | Acetylation | SNKGDSIKRTAAKVP CCCCCHHHHHHCCCC | 47.88 | 25381059 | |
87 | Phosphorylation | KGDSIKRTAAKVPSP CCCHHHHHHCCCCCC | 26.43 | 22369663 | |
90 | Acetylation | SIKRTAAKVPSPGLG HHHHHHCCCCCCCCC | 52.82 | 24489116 | |
93 | Phosphorylation | RTAAKVPSPGLGAPP HHHCCCCCCCCCCCC | 34.29 | 22369663 | |
287 | Phosphorylation | YNSLIKPYLNDQHLA HHHCCHHHCCCCCCC | 17.09 | 22369663 | |
385 | Ubiquitination | GVQKNFAKFIEYNLN CHHHHHHHHHHEECC | 42.61 | 23749301 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of TRM82_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRM82_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 TRM82_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-93, 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-67 AND SER-93, AND MASSSPECTROMETRY. |