UniProt ID | TRM10_YEAST | |
---|---|---|
UniProt AC | Q12400 | |
Protein Name | tRNA (guanine(9)-N1)-methyltransferase {ECO:0000305|PubMed:12702816} | |
Gene Name | TRM10 {ECO:0000303|PubMed:12702816} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 293 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs.. | |
Protein Sequence | MSNDEINQNEEKVKRTPPLPPVPEGMSKKQWKKMCKRQRWEENKAKYNAERRVKKKRLRHERSAKIQEYIDRGEEVPQELIREPRINVNQTDSGIEIILDCSFDELMNDKEIVSLSNQVTRAYSANRRANHFAEIKVAPFDKRLKQRFETTLKNTNYENWNHFKFLPDDKIMFGDEHISKDKIVYLTADTEEKLEKLEPGMRYIVGGIVDKNRYKELCLKKAQKMGIPTRRLPIDEYINLEGRRVLTTTHVVQLMLKYFDDHNWKNAFESVLPPRKLDAEAKSASSSPAPKDT | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSNDEINQN ------CCHHHHHHC | 53.65 | 22369663 | |
16 | Phosphorylation | NEEKVKRTPPLPPVP CHHHHCCCCCCCCCC | 24.44 | 22369663 | |
179 | Phosphorylation | MFGDEHISKDKIVYL ECCCCCCCCCEEEEE | 36.39 | 28889911 | |
187 | Phosphorylation | KDKIVYLTADTEEKL CCEEEEEECCCHHHH | 12.56 | 28889911 | |
190 | Phosphorylation | IVYLTADTEEKLEKL EEEEECCCHHHHHHC | 43.51 | 28889911 | |
283 | Phosphorylation | KLDAEAKSASSSPAP HCCHHHHHHCCCCCC | 40.19 | 25005228 | |
285 | Phosphorylation | DAEAKSASSSPAPKD CHHHHHHCCCCCCCC | 38.14 | 25005228 | |
286 | Phosphorylation | AEAKSASSSPAPKDT HHHHHHCCCCCCCCC | 39.80 | 25005228 | |
287 | Phosphorylation | EAKSASSSPAPKDT- HHHHHCCCCCCCCC- | 23.68 | 25005228 |
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 TRM10_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRM10_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 TRM10_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PUS1_YEAST | PUS1 | genetic | 18314501 | |
XPOT_YEAST | LOS1 | genetic | 18314501 | |
TAD2_YEAST | TAD2 | genetic | 19061648 | |
LTV1_YEAST | LTV1 | genetic | 19061648 | |
MRT4_YEAST | MRT4 | genetic | 19061648 | |
NOP15_YEAST | NOP15 | genetic | 19061648 | |
H1_YEAST | HHO1 | genetic | 19061648 | |
IF2G_YEAST | GCD11 | genetic | 19061648 | |
PUS3_YEAST | DEG1 | genetic | 19547744 | |
SRS2_YEAST | SRS2 | genetic | 21459050 | |
NTM1_YEAST | TAE1 | genetic | 27708008 | |
RV161_YEAST | RVS161 | genetic | 27708008 | |
PEX19_YEAST | PEX19 | genetic | 27708008 | |
BRE1_YEAST | BRE1 | genetic | 27708008 | |
MAF1_YEAST | MAF1 | genetic | 27708008 | |
TRM1_YEAST | TRM1 | genetic | 27708008 | |
RSSA2_YEAST | RPS0B | genetic | 27708008 | |
PFKA2_YEAST | PFK2 | genetic | 27708008 | |
AF9_YEAST | YAF9 | genetic | 27708008 | |
VPS27_YEAST | VPS27 | genetic | 27708008 | |
RS10A_YEAST | RPS10A | genetic | 27708008 | |
ELP4_YEAST | ELP4 | genetic | 27708008 | |
HSP7F_YEAST | SSE1 | genetic | 27708008 | |
PUS1_YEAST | PUS1 | genetic | 27708008 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
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-2 AND THR-16, AND MASSSPECTROMETRY. |