| UniProt ID | VPS74_YEAST | |
|---|---|---|
| UniProt AC | Q06385 | |
| Protein Name | Vacuolar protein sorting-associated protein 74 | |
| Gene Name | VPS74 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 345 | |
| Subcellular Localization |
Golgi apparatus, Golgi stack membrane Peripheral membrane protein Cytoplasmic side . Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. |
|
| Protein Description | Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting.. | |
| Protein Sequence | MSTLQRRRVNRADSGDTSSIHSSANNTKGDKIANIAVDGDDDNGTNKKIAYDPEESKLRDNINIPTLTLMEEVLLMGLRDREGYLSFWNDSISYALRGCIIIELALRGKIRILDDSARKRFDLSERLIEVIDSSKTGEVLLDETLQLMKNDEPLSISNWIDLLSGETWNLLKINYQLKQVRERLAKGLVDKGVLRTEMKNFFLFDMATHPIADASCKEAIKRRVLSVLVSRNMELSYNEYFPETTSFKIIRTLALICGSYGANVLENVLTTLEYEKRDKAISRAEEIMAQFSQYPFDLEKETELGVSVNLNKEVKEEIENNPGHDLQLEVIAGVFEVFSRMDMLL | |
| 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 | ------MSTLQRRRV ------CCHHHHHCC | 37.51 | 19823750 | |
| 3 | Phosphorylation | -----MSTLQRRRVN -----CCHHHHHCCC | 26.13 | 19823750 | |
| 14 | Phosphorylation | RRVNRADSGDTSSIH HCCCCCCCCCCCCCC | 37.27 | 22369663 | |
| 17 | Phosphorylation | NRADSGDTSSIHSSA CCCCCCCCCCCCCCC | 28.09 | 22369663 | |
| 18 | Phosphorylation | RADSGDTSSIHSSAN CCCCCCCCCCCCCCC | 31.84 | 22369663 | |
| 19 | Phosphorylation | ADSGDTSSIHSSANN CCCCCCCCCCCCCCC | 26.81 | 22369663 | |
| 22 | Phosphorylation | GDTSSIHSSANNTKG CCCCCCCCCCCCCCC | 29.49 | 22369663 | |
| 23 | Phosphorylation | DTSSIHSSANNTKGD CCCCCCCCCCCCCCC | 22.36 | 22369663 | |
| 27 | Phosphorylation | IHSSANNTKGDKIAN CCCCCCCCCCCEEEE | 35.89 | 22890988 | |
| 28 | Ubiquitination | HSSANNTKGDKIANI CCCCCCCCCCEEEEE | 68.20 | 23749301 | |
| 31 | Ubiquitination | ANNTKGDKIANIAVD CCCCCCCEEEEEEEC | 53.00 | 23749301 | |
| 45 | Phosphorylation | DGDDDNGTNKKIAYD CCCCCCCCCCCEECC | 50.55 | 21440633 | |
| 47 | Ubiquitination | DDDNGTNKKIAYDPE CCCCCCCCCEECCHH | 45.45 | 22817900 | |
| 47 | Acetylation | DDDNGTNKKIAYDPE CCCCCCCCCEECCHH | 45.45 | 25381059 | |
| 48 | Ubiquitination | DDNGTNKKIAYDPEE CCCCCCCCEECCHHH | 34.34 | 23749301 | |
| 56 | Phosphorylation | IAYDPEESKLRDNIN EECCHHHHHCCCCCC | 35.02 | 30377154 | |
| 57 | Ubiquitination | AYDPEESKLRDNINI ECCHHHHHCCCCCCC | 51.31 | 23749301 | |
| 57 | Acetylation | AYDPEESKLRDNINI ECCHHHHHCCCCCCC | 51.31 | 24489116 | |
| 133 | Phosphorylation | RLIEVIDSSKTGEVL HHHHHHHCCCCCCEE | 23.70 | 27017623 | |
| 134 | Phosphorylation | LIEVIDSSKTGEVLL HHHHHHCCCCCCEEH | 30.41 | 27017623 | |
| 217 | Ubiquitination | PIADASCKEAIKRRV CCCCHHHHHHHHHHH | 47.92 | 23749301 | |
| 226 | Phosphorylation | AIKRRVLSVLVSRNM HHHHHHHHHHHHCCC | 15.56 | 30377154 |
| 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 VPS74_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS74_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 VPS74_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-14; SER-18; SER-19 ANDSER-22, 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-14; THR-17; SER-19 ANDTHR-27, AND MASS SPECTROMETRY. | |
| "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-14 AND SER-19, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-19 AND SER-23,AND MASS SPECTROMETRY. | |
