| UniProt ID | PPS1_YEAST | |
|---|---|---|
| UniProt AC | P38148 | |
| Protein Name | Dual specificity protein phosphatase PPS1 | |
| Gene Name | PPS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 807 | |
| Subcellular Localization | ||
| Protein Description | Protein phosphatase with specificity for serine, threonine, and tyrosine residues; has a role in the DNA synthesis phase of the cell cycle.. | |
| Protein Sequence | MVLEVPSITPGELHDLMRLHQDAEWPECKKMFPWAHDISFGQPPDFPHSLAIVKSQSDANNSALLRNSLEVNDIFQSWKVRTSFHREGDTCETGNDSNGFQYPNNTKELLNLLKFQIRQLELQVDDVALENAATYCHNHSILPFLKVDPRGLSLELKRYSRNKVGSNTTLKRSGQDVWGRRGLFRRFDLQCAKMIEMVDNIVIYCSRTGGSTDMQTESAPACSHEGNCPNCTTLALLLQICLMFVQKGYVGSGGSLYKTNLFICTYQNFNTDIPQTLIGTPLLDNEFFKNNTPLNLCSSPSEIVCFNNVDKNMVLCEKLELNKLTSATRLEETGLICGNTTDWHNYQIIKKNNISLTHRFEENTSIVNLKSLNYDTDNPTTSISQLYNIPNTKEVWKLIIKCTSNSQMPSLTKIRTYLDLLLDDDASKSQEHLHLTFPASGSIGLGNLNIQSVEILLNVCYLIFQVSQVQELLTFMYCEDGYTETSLLLTAYIIFHFNIPLQDALLRIHPRPFFLFPSDLQILGHLQPVLREFSPQNGSNLKLYANALKFRDKSFQLHISSELFSSIFFMKIPLESNFVNLKGPLPSRILRHLYLGSLDHAQNPALLKSLGITHIVSVGEVVSWTLNKDKIAHPVRPHRAITMTNTNEVAGNTTCNKSRNRADTVVSDKQENGSNVVISENSGFQICQIENLDDNGKDPLFHQIDKVLDFISNSEATGGKVLVHCMVGVSRSATVCIAECMRYLQCDLASAYLFVRVRRLNVIIQPNLFFVYELFKWWKKHYNREKDKTMDWHIICRGIAEVNMKYT | |
| 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 |
|---|---|---|---|---|---|
| 364 | Phosphorylation | THRFEENTSIVNLKS EEECCCCCEEEEEEC | 24.10 | 21126336 | |
| 365 | Phosphorylation | HRFEENTSIVNLKSL EECCCCCEEEEEECC | 35.80 | 30377154 | |
| 576 | Phosphorylation | FMKIPLESNFVNLKG EEECCCCCCCCCCCC | 43.16 | 27017623 | |
| 642 | Phosphorylation | VRPHRAITMTNTNEV CCCCCEEEECCCCCC | 19.56 | 23749301 | |
| 646 | Phosphorylation | RAITMTNTNEVAGNT CEEEECCCCCCCCCC | 24.48 | 28889911 | |
| 664 | Phosphorylation | KSRNRADTVVSDKQE CCCCCCCEEEEECCH | 23.09 | 17287358 |
| 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 PPS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PPS1_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 PPS1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PUR8_YEAST | ADE13 | physical | 11805837 | |
| RAS2_YEAST | RAS2 | genetic | 9083070 | |
| SERA_YEAST | SER3 | physical | 18719252 | |
| PP2C1_YEAST | PTC1 | genetic | 19269370 | |
| PKH3_YEAST | PKH3 | genetic | 19269370 | |
| CTK2_YEAST | CTK2 | genetic | 19269370 | |
| MNN11_YEAST | MNN11 | genetic | 19269370 | |
| ADK_YEAST | ADO1 | genetic | 19269370 | |
| CTK1_YEAST | CTK1 | genetic | 19269370 | |
| ETR1_YEAST | ETR1 | genetic | 20093466 | |
| RSC2_YEAST | RSC2 | genetic | 20093466 | |
| ETR1_YEAST | ETR1 | genetic | 27708008 | |
| IMG2_YEAST | IMG2 | genetic | 27708008 | |
| HOOK2_HUMAN | HOOK2 | physical | 27107014 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-664, AND MASSSPECTROMETRY. | |