| UniProt ID | SYEC_YEAST | |
|---|---|---|
| UniProt AC | P46655 | |
| Protein Name | Glutamate--tRNA ligase, cytoplasmic | |
| Gene Name | GUS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 708 | |
| Subcellular Localization | Cytoplasm. Mitochondrion. Largely excluded from the nucleus. | |
| Protein Description | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the tRNA-dependent amidotransferase (AdT), which generates mitochondrial glutaminyl-tRNA(Gln) by transamidation of glutamyl-tRNA(Gln).. | |
| Protein Sequence | MPSTLTINGKAPIVAYAELIAARIVNALAPNSIAIKLVDDKKAPAAKLDDATEDVFNKITSKFAAIFDNGDKEQVAKWVNLAQKELVIKNFAKLSQSLETLDSQLNLRTFILGGLKYSAADVACWGALRSNGMCGSIIKNKVDVNVSRWYTLLEMDPIFGEAHDFLSKSLLELKKSANVGKKKETHKANFEIDLPDAKMGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKEEFQDSILEDLDLLGIKGDRITYSSDYFQEMYDYCVQMIKDGKAYCDDTPTEKMREERMDGVASARRDRSVEENLRIFTEEMKNGTEEGLKNCVRAKIDYKALNKTLRDPVIYRCNLTPHHRTGSTWKIYPTYDFCVPIVDAIEGVTHALRTIEYRDRNAQYDWMLQALRLRKVHIWDFARINFVRTLLSKRKLQWMVDKDLVGNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPIAPRHTAIVNPVKIHLEGSEAPQEPKIEMKPKHKKNPAVGEKKVIYYKDIVVDKDDADVINVDEEVTLMDWGNVIITKKNDDGSMVAKLNLEGDFKKTKHKLTWLADTKDVVPVDLVDFDHLITKDRLEEDESFEDFLTPQTEFHTDAIADLNVKDMKIGDIIQFERKGYYRLDALPKDGKPYVFFTIPDGKSVNKYGAKK | |
| 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 |
|---|---|---|---|---|---|
| 10 | Ubiquitination | STLTINGKAPIVAYA CCEEECCCCCCHHHH | 46.64 | 17644757 | |
| 36 | Ubiquitination | APNSIAIKLVDDKKA CCCCEEEEECCCCCC | 33.17 | 17644757 | |
| 36 | Acetylation | APNSIAIKLVDDKKA CCCCEEEEECCCCCC | 33.17 | 24489116 | |
| 41 | Acetylation | AIKLVDDKKAPAAKL EEEECCCCCCCHHHC | 46.50 | 24489116 | |
| 42 | Acetylation | IKLVDDKKAPAAKLD EEECCCCCCCHHHCC | 67.60 | 24489116 | |
| 47 | Ubiquitination | DKKAPAAKLDDATED CCCCCHHHCCHHHHH | 55.33 | 23749301 | |
| 47 | Acetylation | DKKAPAAKLDDATED CCCCCHHHCCHHHHH | 55.33 | 24489116 | |
| 58 | Ubiquitination | ATEDVFNKITSKFAA HHHHHHHHHHHHHHH | 35.58 | 17644757 | |
| 58 | Acetylation | ATEDVFNKITSKFAA HHHHHHHHHHHHHHH | 35.58 | 24489116 | |
| 62 | Acetylation | VFNKITSKFAAIFDN HHHHHHHHHHHHCCC | 30.30 | 24489116 | |
| 72 | 2-Hydroxyisobutyrylation | AIFDNGDKEQVAKWV HHCCCCCHHHHHHHH | 51.98 | - | |
| 72 | Acetylation | AIFDNGDKEQVAKWV HHCCCCCHHHHHHHH | 51.98 | 24489116 | |
| 77 | Acetylation | GDKEQVAKWVNLAQK CCHHHHHHHHHHHHH | 53.47 | 24489116 | |
| 84 | Acetylation | KWVNLAQKELVIKNF HHHHHHHHHHHHHHH | 47.62 | 24489116 | |
| 89 | Acetylation | AQKELVIKNFAKLSQ HHHHHHHHHHHHHHH | 38.23 | 24489116 | |
| 89 | 2-Hydroxyisobutyrylation | AQKELVIKNFAKLSQ HHHHHHHHHHHHHHH | 38.23 | - | |
| 93 | Acetylation | LVIKNFAKLSQSLET HHHHHHHHHHHHHHH | 44.53 | 24489116 | |
| 93 | Ubiquitination | LVIKNFAKLSQSLET HHHHHHHHHHHHHHH | 44.53 | 15699485 | |
| 97 | Phosphorylation | NFAKLSQSLETLDSQ HHHHHHHHHHHHHHH | 25.46 | 30377154 | |
| 103 | Phosphorylation | QSLETLDSQLNLRTF HHHHHHHHHHCHHHH | 39.41 | 29734811 | |
| 116 | Ubiquitination | TFILGGLKYSAADVA HHHHCCCCCCHHHHH | 40.20 | 17644757 | |
| 139 | Acetylation | GMCGSIIKNKVDVNV CCCCHHHCCCCCCCH | 49.39 | 25381059 | |
| 168 | Ubiquitination | EAHDFLSKSLLELKK HHHHHHHHHHHHHHH | 47.47 | 15699485 | |
| 174 | Succinylation | SKSLLELKKSANVGK HHHHHHHHHHCCCCC | 34.99 | 23954790 | |
| 174 | Acetylation | SKSLLELKKSANVGK HHHHHHHHHHCCCCC | 34.99 | 25381059 | |
| 187 | Ubiquitination | GKKKETHKANFEIDL CCCHHHHCCCEEEEC | 53.06 | 15699485 | |
| 198 | Acetylation | EIDLPDAKMGEVVTR EEECCCCCCCCEEEC | 55.61 | 24489116 | |
| 198 | Ubiquitination | EIDLPDAKMGEVVTR EEECCCCCCCCEEEC | 55.61 | 15699485 | |
| 220 | Ubiquitination | YLHIGHAKAALLNQY CCEECHHHHHHHHHH | 28.63 | 17644757 | |
| 233 | Ubiquitination | QYFAQAYKGKLIIRF HHHHHHHCCCEEEEE | 53.22 | 17644757 | |
| 233 | Acetylation | QYFAQAYKGKLIIRF HHHHHHHCCCEEEEE | 53.22 | 24489116 | |
| 292 | Ubiquitination | VQMIKDGKAYCDDTP HHHHHCCCCCCCCCC | 46.44 | 23749301 | |
| 292 | Acetylation | VQMIKDGKAYCDDTP HHHHHCCCCCCCCCC | 46.44 | 25381059 | |
| 298 | Phosphorylation | GKAYCDDTPTEKMRE CCCCCCCCCCHHHHH | 20.89 | 27214570 | |
| 300 | Phosphorylation | AYCDDTPTEKMREER CCCCCCCCHHHHHHH | 50.78 | 23749301 | |
| 319 | Phosphorylation | ASARRDRSVEENLRI HHHHHCCCHHHHHHH | 37.86 | 27214570 | |
| 332 | Acetylation | RIFTEEMKNGTEEGL HHHHHHHHCCCHHHH | 56.35 | 24489116 | |
| 340 | Acetylation | NGTEEGLKNCVRAKI CCCHHHHHHHHHHHC | 60.19 | 25381059 | |
| 346 | 2-Hydroxyisobutyrylation | LKNCVRAKIDYKALN HHHHHHHHCCHHHHC | 26.08 | - | |
| 350 | Acetylation | VRAKIDYKALNKTLR HHHHCCHHHHCHHHC | 42.52 | 24489116 | |
| 350 | Succinylation | VRAKIDYKALNKTLR HHHHCCHHHHCHHHC | 42.52 | 23954790 | |
| 354 | Ubiquitination | IDYKALNKTLRDPVI CCHHHHCHHHCCCEE | 50.19 | 17644757 | |
| 354 | Acetylation | IDYKALNKTLRDPVI CCHHHHCHHHCCCEE | 50.19 | 24489116 | |
| 440 | 2-Hydroxyisobutyrylation | FVRTLLSKRKLQWMV HHHHHHHHCCHHHHC | 54.22 | - | |
| 472 | Phosphorylation | GVRRRGMTVEGLRNF CHHHCCCCHHHHHHH | 20.45 | 28889911 | |
| 482 | Phosphorylation | GLRNFVLSQGPSRNV HHHHHHHCCCCCCCE | 27.99 | 28889911 | |
| 486 | Phosphorylation | FVLSQGPSRNVINLE HHHCCCCCCCEEEEE | 43.22 | 30377154 | |
| 502 | Ubiquitination | NLIWAFNKKVIDPIA EEHHHCCCCCCCCCC | 41.80 | 17644757 | |
| 503 | Acetylation | LIWAFNKKVIDPIAP EHHHCCCCCCCCCCC | 45.59 | 24489116 | |
| 503 | Ubiquitination | LIWAFNKKVIDPIAP EHHHCCCCCCCCCCC | 45.59 | 17644757 | |
| 520 | Ubiquitination | TAIVNPVKIHLEGSE EEEECCEEEEECCCC | 26.18 | 17644757 | |
| 533 | Acetylation | SEAPQEPKIEMKPKH CCCCCCCCCCCCCCC | 51.01 | 24489116 | |
| 537 | Acetylation | QEPKIEMKPKHKKNP CCCCCCCCCCCCCCC | 37.82 | 24489116 | |
| 603 | Succinylation | LNLEGDFKKTKHKLT EECCCCHHCCCCEEE | 65.36 | 23954790 | |
| 603 | Acetylation | LNLEGDFKKTKHKLT EECCCCHHCCCCEEE | 65.36 | 24489116 | |
| 608 | Acetylation | DFKKTKHKLTWLADT CHHCCCCEEEEECCC | 49.52 | 24489116 | |
| 616 | Acetylation | LTWLADTKDVVPVDL EEEECCCCCEECCCE | 49.42 | 24489116 | |
| 665 | Acetylation | DLNVKDMKIGDIIQF CCCCCCCCCCCEEEE | 54.38 | 24489116 | |
| 665 | Ubiquitination | DLNVKDMKIGDIIQF CCCCCCCCCCCEEEE | 54.38 | 15699485 | |
| 675 | Ubiquitination | DIIQFERKGYYRLDA CEEEEECCCEEEEEC | 44.03 | 15699485 | |
| 685 | Acetylation | YRLDALPKDGKPYVF EEEECCCCCCCCEEE | 78.82 | 24489116 | |
| 685 | Ubiquitination | YRLDALPKDGKPYVF EEEECCCCCCCCEEE | 78.82 | 17644757 | |
| 688 | Acetylation | DALPKDGKPYVFFTI ECCCCCCCCEEEEEC | 43.22 | 24489116 | |
| 688 | Ubiquitination | DALPKDGKPYVFFTI ECCCCCCCCEEEEEC | 43.22 | 17644757 | |
| 699 | Ubiquitination | FFTIPDGKSVNKYGA EEECCCCCCCCCCCC | 59.62 | 17644757 | |
| 699 | Acetylation | FFTIPDGKSVNKYGA EEECCCCCCCCCCCC | 59.62 | 24489116 | |
| 703 | Acetylation | PDGKSVNKYGAKK-- CCCCCCCCCCCCC-- | 42.79 | 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 SYEC_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYEC_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 SYEC_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 THR-300 AND THR-472, ANDMASS SPECTROMETRY. | |
