UniProt ID | VAC14_YEAST | |
---|---|---|
UniProt AC | Q06708 | |
Protein Name | Vacuole morphology and inheritance protein 14 | |
Gene Name | VAC14 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 880 | |
Subcellular Localization |
Vacuole membrane Peripheral membrane protein . Limiting membrane of the vacuole. Localization requires FAB1 and FIG4. |
|
Protein Description | The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock. Essential for the control of trafficking of some proteins to the vacuole lumen via the multivesicular body (MVB), and for maintenance of vacuole size and acidity.. | |
Protein Sequence | MEKSIAKGLSDKLYEKRKAAALELEKLVKQCVLEGDYDRIDKIIDELCRDYAYALHQPMARNAGLMGLAATAIALGINDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISADTENSVRGAAELLDRLIKDIVAERASNYISIVNNGSHGLLPAIKTDPISGDVYQEEYEQDNQLAFSLPKFIPLLTERIYAINPDTRVFLVDWLKVLLNTPGLELISYLPSFLGGLFTFLGDSHKDVRTVTHTLMDSLLHEVDRISKLQTEIKMKRLERLKMLEDKYNNSSTPTKKADGALIAEKKKTLMTALGGLSKPLSMETDDTKLSNTNETDDERHLTSQEQLLDSEATSQEPLRDGEEYIPGQDINLNFPEVITVLVNNLASSEAEIQLIALHWIQVILSISPNVFIPFLSKILSVLLKLLSDSDPHITEIAQLVNGQLLSLCSSYVGKETDGKIAYGPIVNSLTLQFFDSRIDAKIACLDWLILIYHKAPNQILKHNDSMFLTLLKSLSNRDSVLIEKALSLLQSLCSDSNDNYLRQFLQDLLTLFKRDTKLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLRTCEDGMFFNSLFKSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILMIIPQSKAFETLNRRLNSLNIWTSQSYVMNNYIRQRENSNFCDSNSDISQRSVSQSKLHFQELINHFKAVSEEDEYSSDMIRLDHGANNKSLLLGSFLDGIDEDKQEIVTPISPMNEAINEEMESPNDNSSVILKDSGSLPFNRNVSDKLKK | |
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 |
---|---|---|---|---|---|
302 | Ubiquitination | RLKMLEDKYNNSSTP HHHHHHHHCCCCCCC | 40.27 | 23749301 | |
303 | Phosphorylation | LKMLEDKYNNSSTPT HHHHHHHCCCCCCCC | 31.72 | 23749301 | |
306 | Phosphorylation | LEDKYNNSSTPTKKA HHHHCCCCCCCCCCC | 31.76 | 30377154 | |
307 | Phosphorylation | EDKYNNSSTPTKKAD HHHCCCCCCCCCCCC | 40.30 | 23749301 | |
308 | Phosphorylation | DKYNNSSTPTKKADG HHCCCCCCCCCCCCC | 34.49 | 21082442 | |
310 | Phosphorylation | YNNSSTPTKKADGAL CCCCCCCCCCCCCCC | 45.31 | 23749301 | |
311 | Acetylation | NNSSTPTKKADGALI CCCCCCCCCCCCCCH | 47.36 | 25381059 | |
337 | Phosphorylation | GGLSKPLSMETDDTK CCCCCCCCCCCCCCC | 24.09 | 21440633 | |
340 | Phosphorylation | SKPLSMETDDTKLSN CCCCCCCCCCCCCCC | 30.45 | 27017623 | |
351 | Phosphorylation | KLSNTNETDDERHLT CCCCCCCCCCHHHHC | 51.31 | 27214570 | |
358 | Phosphorylation | TDDERHLTSQEQLLD CCCHHHHCCHHHHHC | 23.41 | 30377154 | |
359 | Phosphorylation | DDERHLTSQEQLLDS CCHHHHCCHHHHHCC | 37.77 | 28889911 | |
370 | Phosphorylation | LLDSEATSQEPLRDG HHCCCCCCCCCCCCC | 39.33 | 25704821 | |
767 | Phosphorylation | YIRQRENSNFCDSNS HHHHHCCCCCCCCCC | 26.91 | 17563356 | |
772 | Phosphorylation | ENSNFCDSNSDISQR CCCCCCCCCCCCHHH | 39.14 | 23749301 | |
774 | Phosphorylation | SNFCDSNSDISQRSV CCCCCCCCCCHHHHH | 40.03 | 28889911 | |
777 | Phosphorylation | CDSNSDISQRSVSQS CCCCCCCHHHHHHHH | 25.24 | 23749301 | |
780 | Phosphorylation | NSDISQRSVSQSKLH CCCCHHHHHHHHHHH | 20.62 | 23749301 | |
782 | Phosphorylation | DISQRSVSQSKLHFQ CCHHHHHHHHHHHHH | 29.95 | 28889911 | |
799 | Phosphorylation | INHFKAVSEEDEYSS HHHHHHCCCCCCCCC | 39.88 | 21440633 | |
804 | Phosphorylation | AVSEEDEYSSDMIRL HCCCCCCCCCCCEEE | 26.29 | 19823750 | |
805 | Phosphorylation | VSEEDEYSSDMIRLD CCCCCCCCCCCEEEC | 20.15 | 19823750 | |
806 | Phosphorylation | SEEDEYSSDMIRLDH CCCCCCCCCCEEECC | 30.23 | 25752575 | |
819 | Phosphorylation | DHGANNKSLLLGSFL CCCCCCCHHHHHHHC | 26.77 | 21551504 | |
824 | Phosphorylation | NKSLLLGSFLDGIDE CCHHHHHHHCCCCCC | 23.70 | 21440633 | |
841 | Phosphorylation | QEIVTPISPMNEAIN CCCCCCCCHHHHHHH | 21.21 | 21551504 | |
853 | Phosphorylation | AINEEMESPNDNSSV HHHHHCCCCCCCCCE | 27.91 | 28889911 | |
858 | Phosphorylation | MESPNDNSSVILKDS CCCCCCCCCEEEECC | 28.92 | 21551504 | |
859 | Phosphorylation | ESPNDNSSVILKDSG CCCCCCCCEEEECCC | 21.30 | 28889911 | |
865 | Phosphorylation | SSVILKDSGSLPFNR CCEEEECCCCCCCCC | 28.79 | 21551504 | |
867 | Phosphorylation | VILKDSGSLPFNRNV EEEECCCCCCCCCCH | 36.50 | 24961812 | |
875 | Phosphorylation | LPFNRNVSDKLKK-- CCCCCCHHHHHCC-- | 32.36 | 20377248 |
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 VAC14_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VAC14_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 VAC14_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 THR-308; SER-805; SER-806;SER-853; SER-859 AND SER-867, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767, AND MASSSPECTROMETRY. |