UniProt ID | YMR1_YEAST | |
---|---|---|
UniProt AC | P47147 | |
Protein Name | Phosphoinositide 3-phosphatase | |
Gene Name | YMR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 688 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P). Involved in the control of PI3P-dependent signaling and in the maintenance of endosomal system integrity.. | |
Protein Sequence | MEYIKIAKVSNVVLHRRGTATQGTLHLTTHHLIFESPQLSTEFWFPYPLIYGVHKNPGSTLLSKLTSTNQIQLEGTDSQNYKLYQGKDLWSFVNIKVIGKDYAVFSLDFGGDLHLQARKVYDSILNLTVLSNITQLYAFIYISNNLERKLPSPDSWDIYDPIKEFRRQGLDSKDETCPWRLSTVNEHYEFCPTYPSKLFVPRSTSDILLKHASKFRSQKRIPVLTYHHKATDCNILRSSQPLPGLINQRSIQDEKLVWESFNSFCNKDIRRTKHVIVDARPRTNALAQMALGGGTENMDNYNFFLADNNMGVDKSLKLPTVTRLFLGIDNIHIVSNTAAYMTEVICQGGDLNLPLEQNLIRSQKFSNWLKLNTLILKSVDMLLKSIIFNHSNVLVHCSDGWDRTSQVVSLLEICLDPFYRTFEGFMILVEKDWCSFGHRFLERSGHLNSDIRFHDNTMHSNFNDVDTNGDDLDIGVNTQDDYAEDDEGGEDETNLINLSRISKKFNENFKLNKKSLKFVSPVFQQFLDCVYQLLTQNPDLFEFNERFLRRLVYHLYSCQYGTFLSNSEKEKFQQNLPNKTKSVWDYFRSRRKQFINPNFIQRKRSGMNEHDQNLEEEEKVEWISPDLKKVQWWWQLYGRKDSEMNDELRHKRDSVPISVDKKSKEHSNSDGGKGLNLSIFGFDMFNRK | |
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 |
---|---|---|---|---|---|
82 | Ubiquitination | GTDSQNYKLYQGKDL CCCCCCEEEECCCCC | 48.55 | 23749301 | |
152 | Phosphorylation | NLERKLPSPDSWDIY CHHHCCCCCCCCCCC | 52.34 | 28889911 | |
155 | Phosphorylation | RKLPSPDSWDIYDPI HCCCCCCCCCCCHHH | 29.99 | 28889911 | |
173 | Ubiquitination | RRQGLDSKDETCPWR HHCCCCCCCCCCCCC | 60.29 | 23749301 | |
203 | Phosphorylation | SKLFVPRSTSDILLK CCCCCCCCHHHHHHH | 26.62 | 30377154 | |
378 | Phosphorylation | LNTLILKSVDMLLKS HHHHHHHHHHHHHHH | 21.65 | 27214570 | |
642 | Phosphorylation | QLYGRKDSEMNDELR HHHCCCCHHHCHHHH | 41.60 | 30377154 | |
654 | Phosphorylation | ELRHKRDSVPISVDK HHHHCCCCCCCCCCC | 33.55 | 19823750 | |
658 | Phosphorylation | KRDSVPISVDKKSKE CCCCCCCCCCCCCCC | 20.42 | 28889911 | |
663 | Phosphorylation | PISVDKKSKEHSNSD CCCCCCCCCCCCCCC | 49.36 | 28889911 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of YMR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YMR1_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 YMR1_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-654, AND MASSSPECTROMETRY. |