| UniProt ID | PNPH_YEAST | |
|---|---|---|
| UniProt AC | Q05788 | |
| Protein Name | Purine nucleoside phosphorylase | |
| Gene Name | PNP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 311 | |
| Subcellular Localization | ||
| Protein Description | The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine (By similarity).. | |
| Protein Sequence | MSDILNVSQQREAITKAAAYISAILEPHFKNTTNFEPPRTLIICGSGLGGISTKLSRDNPPPVTVPYQDIPGFKKSTVPGHSGTLMFGSMNGSPVVLMNGRLHGYEGNTLFETTFPIRVLNHMGHVRNLIVTNAAGGINAKYQACDLMCIYDHLNIPGLAGQHPLRGPNLDEDGPRFLALSDAYDLELRKLLFKKWKELKIQRPLHEGTYTFVSGPTFETRAESKMIRMLGGDAVGMSTVPEVIVARHCGWRVLALSLITNTCVVDSPASALDESPVPLEKGKATHAEVLENGKIASNDVQNLIAAVMGEL | |
| 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 | Acetylation | ------MSDILNVSQ ------CCCCCCHHH | 33.10 | 22814378 | |
| 64 | Phosphorylation | RDNPPPVTVPYQDIP CCCCCCCCCCHHCCC | 22.87 | 27017623 | |
| 76 | Phosphorylation | DIPGFKKSTVPGHSG CCCCCCCCCCCCCCC | 34.92 | 27017623 | |
| 77 | Phosphorylation | IPGFKKSTVPGHSGT CCCCCCCCCCCCCCE | 39.33 | 27017623 | |
| 82 | Phosphorylation | KSTVPGHSGTLMFGS CCCCCCCCCEEEEEE | 39.11 | 27017623 | |
| 132 | Phosphorylation | HVRNLIVTNAAGGIN CCCEEEEECCCCCCC | 16.49 | 27017623 | |
| 267 | Phosphorylation | TNTCVVDSPASALDE HCCCCCCCCCHHCCC | 15.68 | 30377154 | |
| 275 | Phosphorylation | PASALDESPVPLEKG CCHHCCCCCCCHHCC | 30.75 | 27214570 |
| 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 PNPH_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PNPH_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 PNPH_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-275, AND MASSSPECTROMETRY. | |