UniProt ID | VPS17_YEAST | |
---|---|---|
UniProt AC | P32913 | |
Protein Name | Vacuolar protein sorting-associated protein 17 | |
Gene Name | VPS17 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 551 | |
Subcellular Localization |
Endomembrane system Peripheral membrane protein Cytoplasmic side. Membrane-associated on the cytoplasmic side of either the Golgi complex or an intermediate in Golgi to vacuole transport. |
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Protein Description | Plays a role in vesicular protein sorting. Required for the sorting and delivery of a subset of soluble vacuolar hydrolases. Required for retention of late Golgi membrane proteins and vacuolar biogenesis. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS5-VPS17 subcomplex may assemble onto the membrane to promote vesicle formation.. | |
Protein Sequence | MTSAVPYDPYDDLDNNPFAEPQEEDSEPAATTTDGSSSMSEERVGTEQTAASVQDNGTANNIQNGLGEEGNATRSKTSNEHNENQQPSQPSERVILPERSDEKKKYTLLAKVTGLERFGSATGKKENPTIIFDCSTNLPTFRKQQYKNVKKSYEEFHQLFKYLNVAIQESFVPTLPSAYTTFGINSEEDRMKVTRNFQLWFNRLSQDPLIIRNEEVAFFIESDFNTYTPINKSKSLASGLKRKTLKQLAPPYDEITELAEFRPLVKSIYVVSQSLQEKLLRVSRNRKMMVQEENAFGQDFVNLDEHNKLYRRYGKILTAVGDIDSIIATMDMATLYDGLEWIVRDAYAVKEALTNRHFIMRNLVQAQQNSKAKQEQARRFRSRRDINPMKIDEALRQLKAAAKNEQVLTLKLQRITSNMIIERKQWISWYEEWIRSSIKEFTLRKIEYERKKLTLLERVRSDIRKADENGGLSRLGRHAVSNNNSDTSQTLKGDSWTGESNRKSQIPINKIAHTEFDDELFTEDDGYNSQDSDTTSLNARHAASLLGMSTK | |
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 |
---|---|---|---|---|---|
52 | Phosphorylation | GTEQTAASVQDNGTA CCCCCCHHHHCCCCC | 20.18 | 19779198 | |
58 | Phosphorylation | ASVQDNGTANNIQNG HHHHCCCCCCCCCCC | 32.25 | 28889911 | |
77 | Phosphorylation | GNATRSKTSNEHNEN CCCCCCCCCCCCCCC | 37.72 | 28889911 | |
88 | Phosphorylation | HNENQQPSQPSERVI CCCCCCCCCCCCEEE | 50.84 | 28889911 | |
278 | Acetylation | VSQSLQEKLLRVSRN HCHHHHHHHHHHHHC | 39.60 | 24489116 | |
350 | Acetylation | VRDAYAVKEALTNRH HHHHHHHHHHHHCCH | 29.15 | 24489116 | |
417 | Phosphorylation | LKLQRITSNMIIERK EEEEEHHCCCEEEEH | 23.25 | 28889911 | |
485 | Phosphorylation | HAVSNNNSDTSQTLK HCCCCCCCCCCCCCC | 44.37 | 28889911 | |
488 | Phosphorylation | SNNNSDTSQTLKGDS CCCCCCCCCCCCCCC | 26.59 | 28889911 | |
492 | Ubiquitination | SDTSQTLKGDSWTGE CCCCCCCCCCCCCCC | 65.15 | 23749301 | |
514 | Phosphorylation | PINKIAHTEFDDELF CCCHHCCCCCCCCCC | 29.35 | 19779198 | |
522 | Phosphorylation | EFDDELFTEDDGYNS CCCCCCCCCCCCCCC | 51.64 | 21440633 | |
527 | Phosphorylation | LFTEDDGYNSQDSDT CCCCCCCCCCCCCCC | 20.73 | 20377248 | |
529 | Phosphorylation | TEDDGYNSQDSDTTS CCCCCCCCCCCCCCH | 27.21 | 21082442 | |
532 | Phosphorylation | DGYNSQDSDTTSLNA CCCCCCCCCCCHHHH | 29.26 | 21082442 | |
534 | Phosphorylation | YNSQDSDTTSLNARH CCCCCCCCCHHHHHH | 23.41 | 21440633 | |
535 | Phosphorylation | NSQDSDTTSLNARHA CCCCCCCCHHHHHHH | 35.89 | 21440633 | |
536 | Phosphorylation | SQDSDTTSLNARHAA CCCCCCCHHHHHHHH | 23.01 | 19684113 | |
544 | Phosphorylation | LNARHAASLLGMSTK HHHHHHHHHHCCCCC | 25.55 | 22369663 | |
549 | Phosphorylation | AASLLGMSTK----- HHHHHCCCCC----- | 31.11 | 23749301 | |
550 | Phosphorylation | ASLLGMSTK------ HHHHCCCCC------ | 31.70 | 21440633 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of VPS17_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS17_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 VPS17_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-417 AND SER-544, ANDMASS 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-544, AND MASSSPECTROMETRY. |