| UniProt ID | ASPG1_YEAST | |
|---|---|---|
| UniProt AC | P38986 | |
| Protein Name | L-asparaginase 1 | |
| Gene Name | ASP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 381 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | ||
| Protein Sequence | MKSDSVEITTICPDVENSQFVVQSNCPETIPEILKSQNAAVNGSGIACQQRSLPRIKILGTGGTIASKAIDSSQTAGYHVDLTIQDLLDAIPDISKVCDIEYEQLCNVDSKDINEDILYKIYKGVSESLQAFDGIVITHGTDTLSETAFFIESTIDAGDVPIVFVGSMRPSTSVSADGPMNLYQAICIASNPKSRGRGVLVSLNDQISSGYYITKTNANSLDSFNVRQGYLGNFVNNEIHYYYPPVKPQGCHKFKLRVDGKHFKLPEVCILYAHQAFPPAIVNLVADKYDGIVLATMGAGSLPEEVNETCMKLSLPIVYSKRSMDGMVPIANVPKKGSKEDNLIASGYLSPEKSRILLQLCLAGNYTLEEIKHVFTGVYGG | |
| 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 |
|---|---|---|---|---|---|
| 2 | Ubiquitination | ------MKSDSVEIT ------CCCCCEEEE | 64.07 | 23749301 | |
| 5 | Phosphorylation | ---MKSDSVEITTIC ---CCCCCEEEEEEC | 28.83 | 21440633 | |
| 36 | Phosphorylation | TIPEILKSQNAAVNG CHHHHHHHCCCCCCC | 25.81 | 21440633 | |
| 61 | Phosphorylation | PRIKILGTGGTIASK CCEEEEECCCCHHHH | 29.06 | 21126336 | |
| 111 | Ubiquitination | QLCNVDSKDINEDIL HHCCCCCCCCCHHHH | 59.15 | 23749301 | |
| 120 | Acetylation | INEDILYKIYKGVSE CCHHHHHHHHHCHHH | 35.79 | 24489116 | |
| 220 | Phosphorylation | ITKTNANSLDSFNVR EEECCCCCCCCCCCC | 31.01 | 22369663 | |
| 223 | Phosphorylation | TNANSLDSFNVRQGY CCCCCCCCCCCCCCE | 24.82 | 22369663 | |
| 230 | Phosphorylation | SFNVRQGYLGNFVNN CCCCCCCEEHHHHCC | 11.78 | 21551504 | |
| 241 | Phosphorylation | FVNNEIHYYYPPVKP HHCCEEEEECCCCCC | 15.45 | 21551504 | |
| 243 | Phosphorylation | NNEIHYYYPPVKPQG CCEEEEECCCCCCCC | 8.22 | 21551504 | |
| 320 | Phosphorylation | LSLPIVYSKRSMDGM HCCCEEEECCCCCCC | 15.65 | 21440633 | |
| 321 | Ubiquitination | SLPIVYSKRSMDGMV CCCEEEECCCCCCCE | 30.70 | 23749301 | |
| 336 | Acetylation | PIANVPKKGSKEDNL EEECCCCCCCCCCCE | 63.45 | 24489116 | |
| 346 | Phosphorylation | KEDNLIASGYLSPEK CCCCEEECCCCCHHH | 22.45 | 19823750 | |
| 348 | Phosphorylation | DNLIASGYLSPEKSR CCEEECCCCCHHHHH | 11.08 | 19823750 | |
| 350 | Phosphorylation | LIASGYLSPEKSRIL EEECCCCCHHHHHHH | 23.64 | 19795423 | |
| 353 | Ubiquitination | SGYLSPEKSRILLQL CCCCCHHHHHHHHHH | 48.71 | 23749301 | |
| 354 | Phosphorylation | GYLSPEKSRILLQLC CCCCHHHHHHHHHHH | 23.92 | 27017623 |
| 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 ASPG1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASPG1_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 ASPG1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ASPG1_YEAST | ASP1 | physical | 11283351 | |
| ASPG1_YEAST | ASP1 | physical | 18467557 | |
| ASPG1_YEAST | ASP1 | physical | 22615397 | |
| UBC9_HUMAN | UBE2I | physical | 27107014 | |
| GMCL1_HUMAN | GMCL1 | physical | 27107014 |
| 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-223 AND SER-350, ANDMASS SPECTROMETRY. | |