UniProt ID | SYYC_YEAST | |
---|---|---|
UniProt AC | P36421 | |
Protein Name | Tyrosine--tRNA ligase, cytoplasmic | |
Gene Name | TYS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 394 | |
Subcellular Localization | Cytoplasm. Nucleus. Predominantly cytoplasmic, only a small fraction (about 1.5%) found in the nucleus. | |
Protein Description | Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: L-tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36. Also involved in nuclear tRNA export. Also attaches D-Tyr to tRNA(Tyr), this reaction is about 150-fold less efficient than attachment of L-Tyr. [PubMed: 10766779] | |
Protein Sequence | MSSAATVDPNEAFGLITKNLQEVLNPQIIKDVLEVQKRHLKLYWGTAPTGRPHCGYFVPMTKLADFLKAGCEVTVLLADLHAFLDNMKAPLEVVNYRAKYYELTIKAILRSINVPIEKLKFVVGSSYQLTPDYTMDIFRLSNIVSQNDAKRAGADVVKQVANPLLSGLIYPLMQALDEQFLDVDCQFGGVDQRKIFVLAEENLPSLGYKKRAHLMNPMVPGLAQGGKMSASDPNSKIDLLEEPKQVKKKINSAFCSPGNVEENGLLSFVQYVIAPIQELKFGTNHFEFFIDRPEKFGGPITYKSFEEMKLAFKEEKLSPPDLKIGVADAINELLEPIRQEFANNKEFQEASEKGYPVATPQKSKKAKKPKNKGTKYPGATKTNEIATKLEETKL | |
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 | ------MSSAATVDP ------CCCCCCCCH | 28.78 | 28152593 | |
2 | Acetylation | ------MSSAATVDP ------CCCCCCCCH | 28.78 | - | |
3 | Phosphorylation | -----MSSAATVDPN -----CCCCCCCCHH | 22.18 | 19823750 | |
6 | Phosphorylation | --MSSAATVDPNEAF --CCCCCCCCHHHHH | 25.76 | 19823750 | |
30 | Acetylation | VLNPQIIKDVLEVQK HHCHHHHHHHHHHHH | 43.33 | 24489116 | |
37 | Acetylation | KDVLEVQKRHLKLYW HHHHHHHHHHHEEEE | 47.14 | 24489116 | |
99 | Acetylation | EVVNYRAKYYELTIK HHHHHHHHHHHHHHH | 39.09 | 24489116 | |
118 | 2-Hydroxyisobutyrylation | SINVPIEKLKFVVGS HCCCCHHHCEEEECC | 58.66 | - | |
118 | Acetylation | SINVPIEKLKFVVGS HCCCCHHHCEEEECC | 58.66 | 24489116 | |
150 | Acetylation | IVSQNDAKRAGADVV CCCHHHHHHHCHHHH | 45.72 | 25381059 | |
150 | Ubiquitination | IVSQNDAKRAGADVV CCCHHHHHHHCHHHH | 45.72 | 23749301 | |
150 | Succinylation | IVSQNDAKRAGADVV CCCHHHHHHHCHHHH | 45.72 | 23954790 | |
194 | Ubiquitination | FGGVDQRKIFVLAEE CCCCCHHHEEEEEEC | 34.56 | 23749301 | |
209 | Succinylation | NLPSLGYKKRAHLMN CCCCCCCCCCHHHCC | 33.70 | 23954790 | |
209 | Acetylation | NLPSLGYKKRAHLMN CCCCCCCCCCHHHCC | 33.70 | 24489116 | |
229 | Phosphorylation | LAQGGKMSASDPNSK HHHCCCCCCCCCCCC | 28.27 | 21440633 | |
231 | Phosphorylation | QGGKMSASDPNSKID HCCCCCCCCCCCCCC | 46.42 | 22369663 | |
235 | Phosphorylation | MSASDPNSKIDLLEE CCCCCCCCCCCCCCC | 36.05 | 22369663 | |
236 | Succinylation | SASDPNSKIDLLEEP CCCCCCCCCCCCCCH | 47.05 | 23954790 | |
236 | Acetylation | SASDPNSKIDLLEEP CCCCCCCCCCCCCCH | 47.05 | 24489116 | |
244 | Acetylation | IDLLEEPKQVKKKIN CCCCCCHHHHHHHHH | 71.63 | 24489116 | |
247 | Acetylation | LEEPKQVKKKINSAF CCCHHHHHHHHHHCC | 45.94 | 24489116 | |
295 | Acetylation | FFIDRPEKFGGPITY EECCCHHHHCCCCEE | 52.58 | 24489116 | |
295 | Ubiquitination | FFIDRPEKFGGPITY EECCCHHHHCCCCEE | 52.58 | 23749301 | |
303 | Acetylation | FGGPITYKSFEEMKL HCCCCEECCHHHHHH | 39.76 | 24489116 | |
303 | Succinylation | FGGPITYKSFEEMKL HCCCCEECCHHHHHH | 39.76 | 23954790 | |
309 | Acetylation | YKSFEEMKLAFKEEK ECCHHHHHHHHHHHH | 39.69 | 24489116 | |
313 | Ubiquitination | EEMKLAFKEEKLSPP HHHHHHHHHHHCCCC | 60.40 | 23749301 | |
313 | Acetylation | EEMKLAFKEEKLSPP HHHHHHHHHHHCCCC | 60.40 | 25381059 | |
316 | Acetylation | KLAFKEEKLSPPDLK HHHHHHHHCCCCCHH | 56.19 | 24489116 | |
318 | Phosphorylation | AFKEEKLSPPDLKIG HHHHHHCCCCCHHHH | 45.51 | 21440633 | |
353 | Acetylation | EFQEASEKGYPVATP HHHHHHHCCCCCCCC | 62.34 | 24489116 | |
353 | Ubiquitination | EFQEASEKGYPVATP HHHHHHHCCCCCCCC | 62.34 | 23749301 | |
353 | Succinylation | EFQEASEKGYPVATP HHHHHHHCCCCCCCC | 62.34 | 23954790 | |
359 | Phosphorylation | EKGYPVATPQKSKKA HCCCCCCCCCCCCCC | 26.87 | 22369663 | |
363 | Phosphorylation | PVATPQKSKKAKKPK CCCCCCCCCCCCCCC | 33.85 | 21440633 | |
372 | Acetylation | KAKKPKNKGTKYPGA CCCCCCCCCCCCCCC | 74.26 | 25381059 | |
375 | Acetylation | KPKNKGTKYPGATKT CCCCCCCCCCCCCHH | 59.10 | 24489116 | |
381 | Acetylation | TKYPGATKTNEIATK CCCCCCCHHHHHHHH | 49.14 | 25381059 | |
388 | Acetylation | KTNEIATKLEETKL- HHHHHHHHHHHHCC- | 44.90 | 24489116 | |
392 | Phosphorylation | IATKLEETKL----- HHHHHHHHCC----- | 28.42 | 24909858 | |
393 | Acetylation | ATKLEETKL------ HHHHHHHCC------ | 56.32 | 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 SYYC_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYYC_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 SYYC_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-235 AND THR-359, ANDMASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, AND MASSSPECTROMETRY. |