UniProt ID | SYMC_YEAST | |
---|---|---|
UniProt AC | P00958 | |
Protein Name | Methionine--tRNA ligase, cytoplasmic | |
Gene Name | MES1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 751 | |
Subcellular Localization | Cytoplasm . Largely excluded from the nucleus. | |
Protein Description | Catalyzes the attachment of methionine to tRNA(Met) in a two-step reaction: methionine is first activated by ATP to form Met-AMP and then transferred to the acceptor end of tRNA(Met).. | |
Protein Sequence | MSFLISFDKSKKHPAHLQLANNLKIALALEYASKNLKPEVDNDNAAMELRNTKEPFLLFDANAILRYVMDDFEGQTSDKYQFALASLQNLLYHKELPQQHVEVLTNKAIENYLVELKEPLTTTDLILFANVYALNSSLVHSKFPELPSKVHNAVALAKKHVPRDSSSFKNIGAVKIQADLTVKPKDSEILPKPNERNILITSALPYVNNVPHLGNIIGSVLSADIFARYCKGRNYNALFICGTDEYGTATETKALEEGVTPRQLCDKYHKIHSDVYKWFQIGFDYFGRTTTDKQTEIAQHIFTKLNSNGYLEEQSMKQLYCPVHNSYLADRYVEGECPKCHYDDARGDQCDKCGALLDPFELINPRCKLDDASPEPKYSDHIFLSLDKLESQISEWVEKASEEGNWSKNSKTITQSWLKDGLKPRCITRDLVWGTPVPLEKYKDKVLYVWFDATIGYVSITSNYTKEWKQWWNNPEHVSLYQFMGKDNVPFHTVVFPGSQLGTEENWTMLHHLNTTEYLQYENGKFSKSRGVGVFGNNAQDSGISPSVWRYYLASVRPESSDSHFSWDDFVARNNSELLANLGNFVNRLIKFVNAKYNGVVPKFDPKKVSNYDGLVKDINEILSNYVKEMELGHERRGLEIAMSLSARGNQFLQENKLDNTLFSQSPEKSDAVVAVGLNIIYAVSSIITPYMPEIGEKINKMLNAPALKIDDRFHLAILEGHNINKAEYLFQRIDEKKIDEWRAKYGGQQV | |
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 | ------MSFLISFDK ------CCEEEECCC | 28.85 | 6371805 | |
6 | Phosphorylation | --MSFLISFDKSKKH --CCEEEECCCCCCC | 29.55 | 30377154 | |
9 | Acetylation | SFLISFDKSKKHPAH CEEEECCCCCCCHHH | 63.26 | 24489116 | |
31 | Phosphorylation | KIALALEYASKNLKP HHHHHHHHHHHCCCC | 19.61 | 19823750 | |
33 | Phosphorylation | ALALEYASKNLKPEV HHHHHHHHHCCCCCC | 22.60 | 19795423 | |
37 | Succinylation | EYASKNLKPEVDNDN HHHHHCCCCCCCCCC | 48.83 | 23954790 | |
37 | Acetylation | EYASKNLKPEVDNDN HHHHHCCCCCCCCCC | 48.83 | 24489116 | |
53 | Ubiquitination | AMELRNTKEPFLLFD HHHHHHCCCCEEEEC | 67.92 | 17644757 | |
53 | Acetylation | AMELRNTKEPFLLFD HHHHHHCCCCEEEEC | 67.92 | 24489116 | |
67 | Phosphorylation | DANAILRYVMDDFEG CHHHHHHHHHHCCCC | 9.18 | 28889911 | |
76 | Phosphorylation | MDDFEGQTSDKYQFA HHCCCCCCCCHHHHH | 50.15 | 28889911 | |
80 | Phosphorylation | EGQTSDKYQFALASL CCCCCCHHHHHHHHH | 17.54 | 28889911 | |
107 | Ubiquitination | HVEVLTNKAIENYLV HHHHHHHHHHHHHHH | 45.57 | 24961812 | |
165 | Phosphorylation | KKHVPRDSSSFKNIG HHCCCCCCCCCCCCC | 29.21 | 19823750 | |
166 | Phosphorylation | KHVPRDSSSFKNIGA HCCCCCCCCCCCCCE | 44.05 | 19823750 | |
167 | Phosphorylation | HVPRDSSSFKNIGAV CCCCCCCCCCCCCEE | 44.16 | 19823750 | |
169 | Acetylation | PRDSSSFKNIGAVKI CCCCCCCCCCCEEEE | 49.99 | 24489116 | |
253 | Ubiquitination | YGTATETKALEEGVT CCCCHHHHHHHCCCC | 44.75 | 23749301 | |
260 | Phosphorylation | KALEEGVTPRQLCDK HHHHCCCCHHHHHHH | 24.50 | 22369663 | |
270 | Acetylation | QLCDKYHKIHSDVYK HHHHHHHHHCHHHHH | 38.74 | 22865919 | |
293 | Acetylation | FGRTTTDKQTEIAQH CCCCCCCCHHHHHHH | 57.96 | 24489116 | |
293 | Ubiquitination | FGRTTTDKQTEIAQH CCCCCCCCHHHHHHH | 57.96 | 23749301 | |
304 | Acetylation | IAQHIFTKLNSNGYL HHHHHHHHHHCCCCC | 34.62 | 24489116 | |
310 | Phosphorylation | TKLNSNGYLEEQSMK HHHHCCCCCCCHHHC | 18.39 | 29734811 | |
326 | Phosphorylation | LYCPVHNSYLADRYV CCCCCCCHHHHHHHC | 13.47 | 30377154 | |
368 | Ubiquitination | ELINPRCKLDDASPE HHCCCCCCCCCCCCC | 57.12 | 23749301 | |
373 | Phosphorylation | RCKLDDASPEPKYSD CCCCCCCCCCCCCCC | 36.47 | 22369663 | |
377 | Ubiquitination | DDASPEPKYSDHIFL CCCCCCCCCCCCEEE | 56.58 | 17644757 | |
378 | Phosphorylation | DASPEPKYSDHIFLS CCCCCCCCCCCEEEC | 30.00 | 25005228 | |
388 | Ubiquitination | HIFLSLDKLESQISE CEEECHHHHHHHHHH | 60.49 | 17644757 | |
394 | Phosphorylation | DKLESQISEWVEKAS HHHHHHHHHHHHHHH | 20.12 | 19779198 | |
399 | Ubiquitination | QISEWVEKASEEGNW HHHHHHHHHHHHCCC | 47.82 | 17644757 | |
407 | Phosphorylation | ASEEGNWSKNSKTIT HHHHCCCCCCCCCCC | 26.42 | 19779198 | |
411 | Ubiquitination | GNWSKNSKTITQSWL CCCCCCCCCCCHHHH | 54.03 | 23749301 | |
419 | Acetylation | TITQSWLKDGLKPRC CCCHHHHHCCCCCCE | 43.42 | 24489116 | |
441 | Acetylation | GTPVPLEKYKDKVLY CCCCCHHHHCCCEEE | 66.34 | 24489116 | |
443 | Acetylation | PVPLEKYKDKVLYVW CCCHHHHCCCEEEEE | 63.24 | 24489116 | |
529 | Phosphorylation | ENGKFSKSRGVGVFG ECCCCCCCCCEEEEC | 32.82 | 22369663 | |
576 | Phosphorylation | DFVARNNSELLANLG HHHHHCCHHHHHHHH | 32.92 | 24909858 | |
591 | Acetylation | NFVNRLIKFVNAKYN HHHHHHHHHHHHHCC | 48.10 | 24489116 | |
596 | Acetylation | LIKFVNAKYNGVVPK HHHHHHHHCCCCCCC | 33.76 | 24489116 | |
596 | Succinylation | LIKFVNAKYNGVVPK HHHHHHHHCCCCCCC | 33.76 | 23954790 | |
603 | Acetylation | KYNGVVPKFDPKKVS HCCCCCCCCCHHHCC | 51.28 | 24489116 | |
628 | Acetylation | EILSNYVKEMELGHE HHHHHHHHHHHCCCC | 40.77 | 24489116 | |
657 | Acetylation | NQFLQENKLDNTLFS HHHHHHCCCCCCCCC | 57.37 | 24489116 | |
701 | Acetylation | EIGEKINKMLNAPAL HHHHHHHHHHCCCCC | 48.51 | 24489116 | |
737 | Acetylation | LFQRIDEKKIDEWRA HHHHHCHHHHHHHHH | 51.81 | 24489116 |
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 SYMC_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYMC_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 SYMC_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Cytoplasmic methionyl-tRNA synthetase from Bakers' yeast. A monomerwith a post-translationally modified N-terminus."; Fasiolo F., Gibson B.W., Walter P., Chatton B., Biemann K.,Boulanger Y.; J. Biol. Chem. 260:15571-15576(1985). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGEOF INITIATOR METHIONINE, AND ACETYLATION AT SER-2. | |
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-373, AND MASSSPECTROMETRY. |