UniProt ID | FIG4_YEAST | |
---|---|---|
UniProt AC | P42837 | |
Protein Name | Polyphosphoinositide phosphatase | |
Gene Name | FIG4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 879 | |
Subcellular Localization |
Vacuole membrane Peripheral membrane protein . Localized to the limiting membrane of the vacuole. Localization requires VAC14 and FAB1. |
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Protein Description | The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Major enzyme required for hyperosmotic shock-induced turnover of PtdIns(3,5)P2 and requires VAC14 for this function. In vivo, mediates turnover of PtdIns(3,5)P2 at the vacuole membrane necessary for vacuolar size control. In vitro, catalyzes the removal of phosphate from the fifth hydroxyl of the myo-inositol ring of phosphatidylinositol 3,5-bisphosphate.. | |
Protein Sequence | MNNDAMEHTLGGGILTTSGSKQRKTSKFVMGKYTLYETKDRMYIVGSNKRETMFRILEIDLTVPRGELTVLEDNVFFTRNEIMNVLASLEEATEDGLHKKITGYGLLGFIKFTCWYYLIMVTKYSQVAVIGGHGIYHIDGIDIIPITNNYKKPEKSSDEARLLNIFKDLDLTKTFYFSYTYDITNTLQTNILREKLKAVDRCDITIPCGITDYNEMFVWNNNLLSPIFACIDTVFDWFQCIIHGFIDQVNVSVLGKSIYITLIARRSHHFAGARFLKRGVNNKGHVANEVETEQIVTDMILTPFHQPGNGFFDSDRYTSFVQHRGSIPLYWTQDASNLTTKPPIRINVVDPFFSPAALHFDNLFQRYGGGTIQILNLIKTKEKTPRETKLLWEFEQCIDYLNEFLPTLKKLDYTSWDMSRASKQDGQGVIEFLEKYAVNTVTTTGIFHNGPDFASTKIQEGICRSNCIDCLDRTNAAQFVIGKRALGCQLKSLGIIDNSYLEYDSDIVNILTELFHDLGDTIALQYGGSHLVNTMETYRKINQWSSHSRDMIESIKRFYSNSFVDAQRQDAINLFLGHYSWREGFPSLWEMNTDFYLHNAYSLNMPKRSYIHWWNDYNIKSVKELINEELIATGNDVTREKIIKNVRGYPGAFDNYWNEYYLPRSVTWIRDLFAYNMNSTRRYHNALSKQDKAMSPFTSRKQSWLNNKLKMITSSKSLEKAEGRVVETTDLDRDTSPKQELELYEHYLHIISDRSQKLEEKMNSFSYSKYPIFISHESSEIPPMRKVIGEPLVDIAEDFTDVYDDDDDGDDENDEMTTEALLIAPDHVSVDEKFYEKVLNVDDYKPALDDYSAVIHIKPDNLQLYRDLCFSKDIQLDFQ | |
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 |
---|---|---|---|---|---|
9 | Phosphorylation | NNDAMEHTLGGGILT CCCHHCCCCCCCEEC | 17.50 | 25882841 | |
17 | Phosphorylation | LGGGILTTSGSKQRK CCCCEECCCCCCCCC | 27.87 | 25882841 | |
18 | Phosphorylation | GGGILTTSGSKQRKT CCCEECCCCCCCCCC | 35.52 | 28889911 | |
554 | Phosphorylation | HSRDMIESIKRFYSN CCHHHHHHHHHHHHC | 23.61 | 27017623 | |
695 | Phosphorylation | SKQDKAMSPFTSRKQ CCCCCCCCCCCHHHH | 23.01 | 27214570 | |
728 | Phosphorylation | AEGRVVETTDLDRDT HCCCEEEECCCCCCC | 17.63 | 30377154 | |
768 | Phosphorylation | KMNSFSYSKYPIFIS HHHCCCCCCCCEEEE | 25.23 | 27017623 | |
775 | Phosphorylation | SKYPIFISHESSEIP CCCCEEEEECCCCCC | 15.51 | 27017623 | |
779 | Phosphorylation | IFISHESSEIPPMRK EEEEECCCCCCCHHH | 36.24 | 27017623 | |
829 | Phosphorylation | LIAPDHVSVDEKFYE EECCCCCCCCHHHHH | 22.04 | 17572665 |
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 FIG4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FIG4_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 FIG4_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-829, AND MASSSPECTROMETRY. |