| UniProt ID | SYNC_YEAST | |
|---|---|---|
| UniProt AC | P38707 | |
| Protein Name | Asparagine--tRNA ligase, cytoplasmic | |
| Gene Name | DED81 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 554 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | ||
| Protein Sequence | MSSLYIKEATGVDELTTAGSQDHPFKTPAYALFASQQKSDATEPKLFVFKTEDNEYQEISASALKKARKGCDGLKKKAVKQKEQELKKQQKEAENAAKQLSALNITIKEDESLPAAIKTRIYDSYSKVGQRVKVSGWIHRLRSNKKVIFVVLRDGSGFIQCVLSGDLALAQQTLDLTLESTVTLYGTIVKLPEGKTAPGGVELNVDYYEVVGLAPGGEDSFTNKIAEGSDPSLLLDQRHLALRGDALSAVMKVRAALLKSVRRVYDEEHLTEVTPPCMVQTQVEGGSTLFKMNYYGEEAYLTQSSQLYLETCLASLGDVYTIQESFRAEKSHTRRHLSEYTHIEAELAFLTFDDLLQHIETLIVKSVQYVLEDPIAGPLVKQLNPNFKAPKAPFMRLQYKDAITWLNEHDIKNEEGEDFKFGDDIAEAAERKMTDTIGVPIFLTRFPVEIKSFYMKRCSDDPRVTESVDVLMPNVGEITGGSMRIDDMDELMAGFKREGIDTDAYYWFIDQRKYGTCPHGGYGIGTERILAWLCDRFTVRDCSLYPRFSGRCKP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 7 | Ubiquitination | -MSSLYIKEATGVDE -CCCEEEEECCCCCC | 27.95 | 24961812 | |
| 7 | Acetylation | -MSSLYIKEATGVDE -CCCEEEEECCCCCC | 27.95 | 24489116 | |
| 10 | Phosphorylation | SLYIKEATGVDELTT CEEEEECCCCCCCCC | 38.54 | 22369663 | |
| 16 | Phosphorylation | ATGVDELTTAGSQDH CCCCCCCCCCCCCCC | 16.74 | 22369663 | |
| 17 | Phosphorylation | TGVDELTTAGSQDHP CCCCCCCCCCCCCCC | 41.46 | 22369663 | |
| 20 | Phosphorylation | DELTTAGSQDHPFKT CCCCCCCCCCCCCCC | 29.94 | 22369663 | |
| 26 | Ubiquitination | GSQDHPFKTPAYALF CCCCCCCCCHHHHHH | 59.03 | 17644757 | |
| 27 | Phosphorylation | SQDHPFKTPAYALFA CCCCCCCCHHHHHHH | 17.33 | 28889911 | |
| 35 | Phosphorylation | PAYALFASQQKSDAT HHHHHHHHCCCCCCC | 26.30 | 24930733 | |
| 38 | Acetylation | ALFASQQKSDATEPK HHHHHCCCCCCCCCE | 42.54 | 24489116 | |
| 38 | Ubiquitination | ALFASQQKSDATEPK HHHHHCCCCCCCCCE | 42.54 | 23749301 | |
| 45 | Succinylation | KSDATEPKLFVFKTE CCCCCCCEEEEEECC | 48.61 | 23954790 | |
| 45 | Acetylation | KSDATEPKLFVFKTE CCCCCCCEEEEEECC | 48.61 | 24489116 | |
| 50 | Acetylation | EPKLFVFKTEDNEYQ CCEEEEEECCCCCHH | 45.78 | 24489116 | |
| 51 | Phosphorylation | PKLFVFKTEDNEYQE CEEEEEECCCCCHHC | 36.79 | 22369663 | |
| 62 | Phosphorylation | EYQEISASALKKARK CHHCCCHHHHHHHHC | 27.61 | 23749301 | |
| 65 | Acetylation | EISASALKKARKGCD CCCHHHHHHHHCCCC | 44.07 | 24489116 | |
| 65 | Succinylation | EISASALKKARKGCD CCCHHHHHHHHCCCC | 44.07 | 23954790 | |
| 75 | Acetylation | RKGCDGLKKKAVKQK HCCCCHHHHHHHHHH | 58.73 | 25381059 | |
| 82 | 2-Hydroxyisobutyrylation | KKKAVKQKEQELKKQ HHHHHHHHHHHHHHH | 56.50 | - | |
| 101 | Phosphorylation | ENAAKQLSALNITIK HHHHHHHHHCCCEEC | 28.37 | 22369663 | |
| 106 | Phosphorylation | QLSALNITIKEDESL HHHHCCCEECCCCCC | 25.56 | 22369663 | |
| 112 | Phosphorylation | ITIKEDESLPAAIKT CEECCCCCCCHHHHH | 52.56 | 22369663 | |
| 127 | Ubiquitination | RIYDSYSKVGQRVKV HHCCCCCCCCCEEEE | 42.00 | 23749301 | |
| 224 | Ubiquitination | GEDSFTNKIAEGSDP CCCCCCCHHCCCCCH | 39.99 | 17644757 | |
| 229 | Phosphorylation | TNKIAEGSDPSLLLD CCHHCCCCCHHHHHC | 37.54 | 22369663 | |
| 232 | Phosphorylation | IAEGSDPSLLLDQRH HCCCCCHHHHHCHHH | 36.32 | 22369663 | |
| 252 | 2-Hydroxyisobutyrylation | DALSAVMKVRAALLK HHHHHHHHHHHHHHH | 23.21 | - | |
| 252 | Acetylation | DALSAVMKVRAALLK HHHHHHHHHHHHHHH | 23.21 | 24489116 | |
| 366 | Phosphorylation | IETLIVKSVQYVLED HHHHHHHCHHHHHHC | 11.98 | 19779198 | |
| 369 | Phosphorylation | LIVKSVQYVLEDPIA HHHHCHHHHHHCCCC | 12.59 | 19779198 | |
| 381 | Acetylation | PIAGPLVKQLNPNFK CCCCHHHHHCCCCCC | 57.67 | 24489116 | |
| 388 | Ubiquitination | KQLNPNFKAPKAPFM HHCCCCCCCCCCCCC | 71.11 | 23749301 | |
| 388 | Acetylation | KQLNPNFKAPKAPFM HHCCCCCCCCCCCCC | 71.11 | 22865919 | |
| 400 | Acetylation | PFMRLQYKDAITWLN CCCCHHHHHHHHHHH | 27.94 | 24489116 | |
| 420 | Acetylation | NEEGEDFKFGDDIAE CCCCCCCCCCHHHHH | 61.84 | 24489116 | |
| 432 | Ubiquitination | IAEAAERKMTDTIGV HHHHHHHHCCCCCCC | 37.34 | 24961812 | |
| 434 | Phosphorylation | EAAERKMTDTIGVPI HHHHHHCCCCCCCCE | 32.78 | 22369663 | |
| 436 | Phosphorylation | AERKMTDTIGVPIFL HHHHCCCCCCCCEEE | 15.51 | 22369663 | |
| 444 | Phosphorylation | IGVPIFLTRFPVEIK CCCCEEEECCCEEEE | 21.37 | 22369663 | |
| 451 | Succinylation | TRFPVEIKSFYMKRC ECCCEEEEEEEHHHC | 22.47 | 23954790 | |
| 451 | Acetylation | TRFPVEIKSFYMKRC ECCCEEEEEEEHHHC | 22.47 | 24489116 | |
| 465 | Phosphorylation | CSDDPRVTESVDVLM CCCCCCCCCEEEEEC | 24.67 | 26447709 | |
| 467 | Phosphorylation | DDPRVTESVDVLMPN CCCCCCCEEEEECCC | 17.79 | 26447709 | |
| 496 | Acetylation | DELMAGFKREGIDTD HHHHHCHHHCCCCCC | 48.93 | 24489116 | |
| 496 | Ubiquitination | DELMAGFKREGIDTD HHHHHCHHHCCCCCC | 48.93 | 23749301 | |
| 513 | Acetylation | YWFIDQRKYGTCPHG EEEEECCCCCCCCCC | 42.26 | 22865919 | |
| 513 | Ubiquitination | YWFIDQRKYGTCPHG EEEEECCCCCCCCCC | 42.26 | 23749301 |
| 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 SYNC_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYNC_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 SYNC_YEAST !! | ||||||
| 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-101; SER-112 ANDSER-229, AND MASS SPECTROMETRY. | |
