UniProt ID | AVO2_YEAST | |
---|---|---|
UniProt AC | Q04749 | |
Protein Name | Target of rapamycin complex 2 subunit AVO2 | |
Gene Name | AVO2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 426 | |
Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side . Vacuole membrane Peripheral membrane protein Cytoplasmic side . |
|
Protein Description | Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway.. | |
Protein Sequence | MLKEPSVRLREAIIEGNLLIVKRLLRRNPDLLTNIDSENGWSSLHYASYHGRYLICVYLIQLGHDKHELIKTFKGNTCVHLALMKGHEQTLHLLLQQFPRFINHRGENGRAPIHIACMNDYYQCLSLLIGVGADLWVMDTNGDTPLHVCLEYGSISCMKMLLNEGEVSLDDNVRDKGNWKPIDVAQTFEVGNIYSKVLKEVKKKGPPLGAGKKPSSFRTPILNAKATFEDGPSPVLSMNSPYSLYSNNSPLPVLPRRISTHTTSGNGGNRRSSITNPVFNPRKPTLSTDSFSSSSNSSSRLRVNSINVKTPVGVSPKKELVSESVRHSATPTSPHNNIALINRYLLPNKSNDNVRGDSQTATINDDGGGGNGGDATIGMGLRKDPDDENENKYKIKVNNGEPRRRVSLLNIPISKLRNSNNTRAED | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MLKEPSVRLREAI --CCCCCCHHHHHHH | 22.44 | 28889911 | |
219 | Phosphorylation | KKPSSFRTPILNAKA CCCCCCCCCCCCCEE | 16.81 | 21440633 | |
259 | Phosphorylation | PVLPRRISTHTTSGN CCCCCEEEECCCCCC | 16.60 | 30377154 | |
272 | Phosphorylation | GNGGNRRSSITNPVF CCCCCCCCCCCCCCC | 23.90 | 22369663 | |
273 | Phosphorylation | NGGNRRSSITNPVFN CCCCCCCCCCCCCCC | 31.46 | 22369663 | |
275 | Phosphorylation | GNRRSSITNPVFNPR CCCCCCCCCCCCCCC | 35.10 | 19779198 | |
287 | Phosphorylation | NPRKPTLSTDSFSSS CCCCCCCCCCCCCCC | 32.42 | 28889911 | |
290 | Phosphorylation | KPTLSTDSFSSSSNS CCCCCCCCCCCCCCC | 27.41 | 23749301 | |
297 | Phosphorylation | SFSSSSNSSSRLRVN CCCCCCCCCCCEEEE | 31.47 | 28889911 | |
298 | Phosphorylation | FSSSSNSSSRLRVNS CCCCCCCCCCEEEEE | 24.59 | 28132839 | |
299 | Phosphorylation | SSSSNSSSRLRVNSI CCCCCCCCCEEEEEE | 34.84 | 28132839 | |
305 | Phosphorylation | SSRLRVNSINVKTPV CCCEEEEEEEECCCC | 16.81 | 23749301 | |
310 | Phosphorylation | VNSINVKTPVGVSPK EEEEEECCCCCCCCC | 20.94 | 22369663 | |
315 | Phosphorylation | VKTPVGVSPKKELVS ECCCCCCCCCHHHCC | 25.69 | 22369663 | |
328 | Phosphorylation | VSESVRHSATPTSPH CCHHHHCCCCCCCCC | 24.23 | 22369663 | |
330 | Phosphorylation | ESVRHSATPTSPHNN HHHHCCCCCCCCCCC | 30.07 | 22369663 | |
332 | Phosphorylation | VRHSATPTSPHNNIA HHCCCCCCCCCCCEE | 51.00 | 22369663 | |
333 | Phosphorylation | RHSATPTSPHNNIAL HCCCCCCCCCCCEEE | 25.93 | 22369663 | |
350 | Phosphorylation | RYLLPNKSNDNVRGD EEECCCCCCCCCCCC | 56.93 | 22369663 | |
358 | Phosphorylation | NDNVRGDSQTATIND CCCCCCCCCCEEEEC | 32.05 | 22369663 | |
360 | Phosphorylation | NVRGDSQTATINDDG CCCCCCCCEEEECCC | 29.71 | 22369663 | |
362 | Phosphorylation | RGDSQTATINDDGGG CCCCCCEEEECCCCC | 24.57 | 22369663 | |
376 | Phosphorylation | GGNGGDATIGMGLRK CCCCCCCEEECCCCC | 23.85 | 22369663 | |
407 | Phosphorylation | GEPRRRVSLLNIPIS CCCCEEEEEEECCHH | 25.90 | 21440633 |
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 AVO2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AVO2_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 AVO2_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-273; THR-330; THR-332AND SER-350, AND MASS SPECTROMETRY. |