UniProt ID | VPS4_YEAST | |
---|---|---|
UniProt AC | P52917 | |
Protein Name | Vacuolar protein sorting-associated protein 4 | |
Gene Name | VPS4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 437 | |
Subcellular Localization |
Endosome membrane Peripheral membrane protein. |
|
Protein Description | Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.. | |
Protein Sequence | MSTGDFLTKGIELVQKAIDLDTATQYEEAYTAYYNGLDYLMLALKYEKNPKSKDLIRAKFTEYLNRAEQLKKHLESEEANAAKKSPSAGSGSNGGNKKISQEEGEDNGGEDNKKLRGALSSAILSEKPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFKGNRKPTSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDALTGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSAIRRRFERRIYIPLPDLAARTTMFEINVGDTPCVLTKEDYRTLGAMTEGYSGSDIAVVVKDALMQPIRKIQSATHFKDVSTEDDETRKLTPCSPGDDGAIEMSWTDIEADELKEPDLTIKDFLKAIKSTRPTVNEDDLLKQEQFTRDFGQEGN | |
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 | Phosphorylation | ------MSTGDFLTK ------CCCHHHHHH | 40.89 | 21126336 | |
59 | Ubiquitination | SKDLIRAKFTEYLNR CHHHHHHHHHHHHHH | 42.86 | 23749301 | |
76 | Phosphorylation | QLKKHLESEEANAAK HHHHHHHHHHHHHHH | 47.28 | 22369663 | |
85 | Phosphorylation | EANAAKKSPSAGSGS HHHHHHHCCCCCCCC | 24.31 | 22369663 | |
87 | Phosphorylation | NAAKKSPSAGSGSNG HHHHHCCCCCCCCCC | 52.96 | 22369663 | |
90 | Phosphorylation | KKSPSAGSGSNGGNK HHCCCCCCCCCCCCC | 38.47 | 22369663 | |
92 | Phosphorylation | SPSAGSGSNGGNKKI CCCCCCCCCCCCCCC | 33.72 | 22369663 | |
100 | Phosphorylation | NGGNKKISQEEGEDN CCCCCCCCHHHCCCC | 40.18 | 28889911 | |
120 | Phosphorylation | KKLRGALSSAILSEK HHHHHHHHHHHHCCC | 19.72 | 17330950 | |
121 | Phosphorylation | KLRGALSSAILSEKP HHHHHHHHHHHCCCC | 21.85 | 25752575 | |
125 | Phosphorylation | ALSSAILSEKPNVKW HHHHHHHCCCCCCCH | 37.14 | 27017623 | |
154 | Acetylation | EAVILPVKFPHLFKG HCCEEECCCCCCCCC | 51.76 | 24489116 | |
160 | Acetylation | VKFPHLFKGNRKPTS CCCCCCCCCCCCCCC | 62.73 | 24489116 | |
212 | Acetylation | KWMGESEKLVKQLFA HHHCCHHHHHHHHHH | 68.79 | 24489116 | |
356 | Phosphorylation | QPIRKIQSATHFKDV HHHHHHHCCCCCCCC | 38.31 | 21440633 | |
358 | Phosphorylation | IRKIQSATHFKDVST HHHHHCCCCCCCCCC | 32.85 | 27717283 | |
361 | Acetylation | IQSATHFKDVSTEDD HHCCCCCCCCCCCCC | 50.01 | 24489116 | |
424 | Acetylation | VNEDDLLKQEQFTRD CCHHHHHHHHHHHHH | 60.12 | 24489116 |
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 VPS4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS4_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 VPS4_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-100 AND SER-120, ANDMASS 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-120, AND MASSSPECTROMETRY. |