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 | ||
* 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 | ||||||
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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-275, AND MASSSPECTROMETRY. |