| UniProt ID | RV167_YEAST | |
|---|---|---|
| UniProt AC | P39743 | |
| Protein Name | Reduced viability upon starvation protein 167 | |
| Gene Name | RVS167 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 482 | |
| Subcellular Localization | Cytoplasm, cytoskeleton. | |
| Protein Description | Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level. Could be implicated in cytoskeletal reorganization in response to environmental stresses and could act in the budding site selection mechanism.. | |
| Protein Sequence | MSFKGFTKAVSRAPQSFRQKFKMGEQTEDPVYEDAERRFQELEQETKKLSEESKRYSTAVNGMLTHQIGFAKSMEEIFKPISGKMSDPNATIPEDNPQGIEASEQYRAIVAELQETLKPDLALVEEKIVTPCQELLKIITYIRKMATKRNHKKLDLDRHLNTYNKHEKKKEPTAKDEERLYKAQAQVEVAQQEYDYYNDLLKTQLPILFSLEAEFVKPLFVSFYFMQLNIFYTLYNRLQDMKIPYFDLNSDIVESYIAKKGNVEEQTDALTITHFKLGYSKAKLEMTRRKYGVATAEGSPVSGASSGVGYGAGYDPATATSPTPTGYGYGAAAPSYAAQPAAQYGTAAAVGTAAAVGTAAGAAAGAVPGTYPQYAAAQSPPLTGLGFQQSPQQQQGPPPAYSNPLTSPVAGTPAAAVAAAPGVETVTALYDYQAQAAGDLSFPAGAVIEIVQRTPDVNEWWTGRYNGQQGVFPGNYVQLNKN | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSFKGFTKA ------CCCCHHHHH | 35.35 | 29136822 | |
| 2 | Acetylation | ------MSFKGFTKA ------CCCCHHHHH | 35.35 | 22814378 | |
| 11 | Phosphorylation | KGFTKAVSRAPQSFR CHHHHHHHHCCHHHH | 27.82 | 21440633 | |
| 16 | Phosphorylation | AVSRAPQSFRQKFKM HHHHCCHHHHHHHCC | 22.72 | 20377248 | |
| 20 | Ubiquitination | APQSFRQKFKMGEQT CCHHHHHHHCCCCCC | 42.57 | 24961812 | |
| 22 | Ubiquitination | QSFRQKFKMGEQTED HHHHHHHCCCCCCCC | 53.70 | 23749301 | |
| 50 | Phosphorylation | EQETKKLSEESKRYS HHHHHHHCHHHHHHH | 48.47 | 28889911 | |
| 72 | Ubiquitination | THQIGFAKSMEEIFK HHHHCCCCCHHHHHH | 48.34 | 17644757 | |
| 73 | Phosphorylation | HQIGFAKSMEEIFKP HHHCCCCCHHHHHHH | 28.17 | 28889911 | |
| 79 | Acetylation | KSMEEIFKPISGKMS CCHHHHHHHCCCCCC | 47.29 | 24489116 | |
| 79 | Ubiquitination | KSMEEIFKPISGKMS CCHHHHHHHCCCCCC | 47.29 | 17644757 | |
| 82 | Phosphorylation | EEIFKPISGKMSDPN HHHHHHCCCCCCCCC | 40.67 | 21440633 | |
| 84 | Ubiquitination | IFKPISGKMSDPNAT HHHHCCCCCCCCCCC | 28.56 | 17644757 | |
| 86 | Phosphorylation | KPISGKMSDPNATIP HHCCCCCCCCCCCCC | 54.09 | 28132839 | |
| 118 | Acetylation | AELQETLKPDLALVE HHHHHHHCCCHHHHH | 43.86 | 24489116 | |
| 165 | Acetylation | RHLNTYNKHEKKKEP HHHHHCCCCCCCCCC | 42.60 | 24489116 | |
| 242 | Ubiquitination | YNRLQDMKIPYFDLN HHHHHHCCCCCCCCC | 49.14 | 23749301 | |
| 267 | Phosphorylation | KGNVEEQTDALTITH CCCHHHHCCCEEEEE | 26.90 | 27214570 | |
| 271 | Phosphorylation | EEQTDALTITHFKLG HHHCCCEEEEEHHHC | 26.08 | 25752575 | |
| 276 | Acetylation | ALTITHFKLGYSKAK CEEEEEHHHCCCHHH | 33.14 | 24489116 | |
| 299 | Phosphorylation | GVATAEGSPVSGASS CEEECCCCCCCCCCC | 17.40 | 27214570 | |
| 321 | Phosphorylation | YDPATATSPTPTGYG CCCCCCCCCCCCCCC | 25.06 | 28889911 | |
| 323 | Phosphorylation | PATATSPTPTGYGYG CCCCCCCCCCCCCCC | 33.00 | 28889911 | |
| 379 | Phosphorylation | PQYAAAQSPPLTGLG HHHHHHCCCCCCCCC | 24.61 | 28889911 | |
| 481 | Ubiquitination | GNYVQLNKN------ CCCEECCCC------ | 73.04 | 23749301 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 299 | S | Phosphorylation | Kinase | FUS3 | P16892 | Uniprot |
| 299 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 321 | S | Phosphorylation | Kinase | FUS3 | P16892 | Uniprot |
| 321 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| 379 | S | Phosphorylation | Kinase | FUS3 | P16892 | Uniprot |
| 379 | S | Phosphorylation | Kinase | PHO85 | P17157 | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | RSP5 | P39940 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RV167_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 RV167_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Regulation of the yeast amphiphysin homologue Rvs167p byphosphorylation."; Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.; Mol. Biol. Cell 14:3027-3040(2003). Cited for: PHOSPHORYLATION AT SER-299; SER-321 AND SER-379. | |
| "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-271, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-481, AND MASSSPECTROMETRY. | |
