| UniProt ID | VPS53_YEAST | |
|---|---|---|
| UniProt AC | P47061 | |
| Protein Name | Vacuolar protein sorting-associated protein 53 | |
| Gene Name | VPS53 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 822 | |
| Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Peripheral membrane protein. Endosome membrane Peripheral membrane protein. |
|
| Protein Description | Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.. | |
| Protein Sequence | MLEGTVDYDPLEDITNILFSKESLNNIDELISITRSYKKQLQEDILKEENELKEHPKNSAEIEASLRKVFQDFKETQDVSASTELTISNLTEGISYLDIAKKNLTHSLTLFQNLKILTDSYIQCNELLSQGSFKKMVSPYKIMCSLAENTFISYKSLDEINYLLSSISRLKGDTLSKIKQNYNALFSGGNISEHDTALTMELREGACELLDCDTSTRAQMIDWCLDKLLFEMKEIFRVDDEAGSLENLSRRYIYFKKILNNFNSKFADYFLKDWEMAVRLTTTFYHITHKDLQTLLKREFKDKNPSIDLFMTALQSTLDFEKYIDVRFSKKIKEPKLSSCFEPYLTLWVSHQNQMMEKKFLSYMSEPKYPSNETESLVLPSSADLFRTYRSVLTQTLELIDNNANDSILTSLANFFSRWLQTYSQKILLPLLLPDNIEVQDKLEAAKYTVLLINTADYCATTIDQLEDKLSEFSGNREKLANSFTKTKNIYDDLLAKGTSFLLNRVIPLDLNFVWREFINNDWSNAAIEDYSRYMVTLKSVLKMPALTDASIKQQQEQPSTLAFILSQFNRDVYKWNFLDKVIDIITTNFVSNTIRLLQPVPPFSLAGSKRKFETRTVVNIGEQLLLDLELLKEIFHTLPESVSNDSDLRENTSYKRVKRHADNNIDQLLKFIKLLMAPLDSADDYYETYSKLTNNNPDSAVWSFVLALKGIPWDLALWKKLWSAYNLETDDTDEGSRPDSNRDLFIFKWDKVLLGQFENNLARMQDPNWSKFVRQDLKISPPVMKRIVSTPQIQQQKEEQKKQSLSVKDFVSHSRFFNRGT | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MLEGTVDYDPLEDIT CCCCCCCCCCHHHHH | 18.35 | 21551504 | |
| 15 | Phosphorylation | YDPLEDITNILFSKE CCCHHHHHHHHCCHH | 28.64 | 21551504 | |
| 20 | Phosphorylation | DITNILFSKESLNNI HHHHHHCCHHHHCCH | 31.87 | 21551504 | |
| 32 | Phosphorylation | NNIDELISITRSYKK CCHHHHHHHHHHHHH | 30.45 | 28889911 | |
| 65 | Phosphorylation | NSAEIEASLRKVFQD CHHHHHHHHHHHHHH | 18.86 | 27017623 | |
| 281 | Phosphorylation | WEMAVRLTTTFYHIT HHHHHHHHHHHHHCC | 17.15 | 30377154 | |
| 282 | Phosphorylation | EMAVRLTTTFYHITH HHHHHHHHHHHHCCH | 21.35 | 30377154 | |
| 283 | Phosphorylation | MAVRLTTTFYHITHK HHHHHHHHHHHCCHH | 19.57 | 30377154 | |
| 285 | Phosphorylation | VRLTTTFYHITHKDL HHHHHHHHHCCHHHH | 7.10 | 30377154 | |
| 288 | Phosphorylation | TTTFYHITHKDLQTL HHHHHHCCHHHHHHH | 15.01 | 30377154 | |
| 294 | Phosphorylation | ITHKDLQTLLKREFK CCHHHHHHHHHHHHC | 41.16 | 30377154 | |
| 303 | Ubiquitination | LKREFKDKNPSIDLF HHHHHCCCCCCHHHH | 71.93 | 19722269 | |
| 322 | Ubiquitination | QSTLDFEKYIDVRFS HHHCCHHHHHCHHCC | 47.72 | 19722269 | |
| 362 | Phosphorylation | MMEKKFLSYMSEPKY HHHHHHHHHHCCCCC | 23.17 | 30377154 | |
| 483 | Phosphorylation | NREKLANSFTKTKNI CHHHHHHHHHHCCCH | 28.78 | 28889911 | |
| 485 | Phosphorylation | EKLANSFTKTKNIYD HHHHHHHHHCCCHHH | 37.31 | 28889911 | |
| 671 | Acetylation | NNIDQLLKFIKLLMA CCHHHHHHHHHHHHC | 54.35 | 24489116 | |
| 790 | Phosphorylation | PVMKRIVSTPQIQQQ HHHHHHHCCHHHHHH | 31.81 | 22369663 | |
| 791 | Phosphorylation | VMKRIVSTPQIQQQK HHHHHHCCHHHHHHH | 14.33 | 22369663 | |
| 813 | Phosphorylation | LSVKDFVSHSRFFNR CCHHHHHHHHHHHCC | 18.75 | 30377154 | |
| 815 | Phosphorylation | VKDFVSHSRFFNRGT HHHHHHHHHHHCCCC | 24.23 | 17287358 | |
| 822 | Phosphorylation | SRFFNRGT------- HHHHCCCC------- | 32.00 | 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 VPS53_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS53_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 VPS53_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-32; SER-790 AND THR-791,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-790 AND SER-815, ANDMASS SPECTROMETRY. | |