UniProt ID | TMT1_YEAST | |
---|---|---|
UniProt AC | P32643 | |
Protein Name | Trans-aconitate 3-methyltransferase | |
Gene Name | TMT1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 299 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation.. | |
Protein Sequence | MSTFSASDFNSERYSSSRPSYPSDFYKMIDEYHDGERKLLVDVGCGPGTATLQMAQELKPFEQIIGSDLSATMIKTAEVIKEGSPDTYKNVSFKISSSDDFKFLGADSVDKQKIDMITAVECAHWFDFEKFQRSAYANLRKDGTIAIWGYADPIFPDYPEFDDLMIEVPYGKQGLGPYWEQPGRSRLRNMLKDSHLDPELFHDIQVSYFCAEDVRDKVKLHQHTKKPLLIRKQVTLVEFADYVRTWSAYHQWKQDPKNKDKEDVADWFIKESLRRRPELSTNTKIEVVWNTFYKLGKRV | |
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 | Acetylation | ------MSTFSASDF ------CCCCCHHHC | 37.85 | 22814378 | |
14 | Phosphorylation | SDFNSERYSSSRPSY HHCCCCCCCCCCCCC | 14.62 | 28889911 | |
16 | Phosphorylation | FNSERYSSSRPSYPS CCCCCCCCCCCCCCH | 22.79 | 22369663 | |
17 | Phosphorylation | NSERYSSSRPSYPSD CCCCCCCCCCCCCHH | 42.12 | 22369663 | |
20 | Phosphorylation | RYSSSRPSYPSDFYK CCCCCCCCCCHHHHH | 48.87 | 22369663 | |
21 | Phosphorylation | YSSSRPSYPSDFYKM CCCCCCCCCHHHHHH | 14.94 | 22369663 | |
23 | Phosphorylation | SSRPSYPSDFYKMID CCCCCCCHHHHHHHH | 31.92 | 22369663 | |
26 | Phosphorylation | PSYPSDFYKMIDEYH CCCCHHHHHHHHHHC | 12.49 | 22369663 | |
70 | Phosphorylation | QIIGSDLSATMIKTA HHHCCCCCHHHHHHH | 27.04 | 27017623 | |
84 | Phosphorylation | AEVIKEGSPDTYKNV HHHHCCCCCCCCCCE | 22.24 | 22369663 | |
87 | Phosphorylation | IKEGSPDTYKNVSFK HCCCCCCCCCCEEEE | 39.52 | 22369663 | |
88 | Phosphorylation | KEGSPDTYKNVSFKI CCCCCCCCCCEEEEE | 14.14 | 21440633 |
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 TMT1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMT1_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 TMT1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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 TYR-14; SER-17; SER-20;SER-84 AND THR-87, AND MASS SPECTROMETRY. |