UniProt ID | VPS64_YEAST | |
---|---|---|
UniProt AC | Q03944 | |
Protein Name | Vacuolar protein sorting-associated protein 64 | |
Gene Name | VPS64 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 604 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type IV membrane protein . |
|
Protein Description | Participates in the control of the reentry into the cell cycle following pheromone treatment. Involved in vacuolar protein sorting.. | |
Protein Sequence | MVELEKRRRPPPQLQHSPYVRDQSNSQGMTKTPETSPPKRPMGRARSNSRSSGSRSNVDIDQYTIPPGLDLLPTASSPPSVHQVSQQQQLSPILANKIRSPFENQSQDQNDNSIDPTPAGQVTIPVEAVSPPALDELSKFQNGSTETLFRTGSPRKKHTHIIILKSLNATFETKFLVVPFKPDGLKLGRPVTNSVNKNNSGSKRDLFSQQVRPDNGNFDSRVLSRNHACLSCDPTSGKIYIRDLKSSNGTFVNGVKIRQNDVELKVGDTVDLGTDIDSKFEHRKISAYVEEISVIPLMNTVSDPTNLVMKKQDHTNKNNGNSTNINGIKIDRGHHNQHIPIRSHLKENYTEAGVTSATTAQRAAFEAAMFGDINNSELDDDILGPETEVLSGIFINNSAGTSINLINMIKTLTTELSLEKQELEKLHSMQNFMQNYTINLDFINKHMIDMNEKHLLKLSTALQKTLSENNDALLKESEDQLKEIKQQNNKVKSACSLKEKQNHEKLQELESELRELNLQIEEERGKNLVLTQSNFNGGINNDNNAKVKQNDSREEKKDTEDTLISTEELGVVEGKRTRVSKGMLFGVVAISFGLVATAVKQLPQ | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | PPPQLQHSPYVRDQS CCCCCCCCCCCCCCC | 12.64 | 25704821 | |
32 | Phosphorylation | NSQGMTKTPETSPPK CCCCCCCCCCCCCCC | 19.72 | 28889911 | |
35 | Phosphorylation | GMTKTPETSPPKRPM CCCCCCCCCCCCCCC | 47.97 | 21440633 | |
36 | Phosphorylation | MTKTPETSPPKRPMG CCCCCCCCCCCCCCC | 37.23 | 28889911 | |
76 | Phosphorylation | LDLLPTASSPPSVHQ CCCCCCCCCCCCHHH | 45.94 | 21440633 | |
85 | Phosphorylation | PPSVHQVSQQQQLSP CCCHHHHCCHHCHHH | 18.72 | 21440633 | |
91 | Phosphorylation | VSQQQQLSPILANKI HCCHHCHHHHHHHHC | 12.93 | 27214570 | |
144 | Phosphorylation | LSKFQNGSTETLFRT HHHCCCCCCCCEECC | 30.53 | 22369663 | |
145 | Phosphorylation | SKFQNGSTETLFRTG HHCCCCCCCCEECCC | 34.09 | 22369663 | |
151 | Phosphorylation | STETLFRTGSPRKKH CCCCEECCCCCCCCC | 34.38 | 21440633 | |
153 | Phosphorylation | ETLFRTGSPRKKHTH CCEECCCCCCCCCEE | 22.40 | 17287358 | |
467 | Phosphorylation | TALQKTLSENNDALL HHHHHHHHHCCHHHH | 43.43 | 30377154 | |
511 | Phosphorylation | EKLQELESELRELNL HHHHHHHHHHHHHHH | 55.33 | 27214570 | |
565 | Phosphorylation | DTEDTLISTEELGVV CCCCCEEEHHHHCEE | 32.64 | 27214570 |
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 VPS64_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS64_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 VPS64_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-144, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASSSPECTROMETRY. |