| UniProt ID | VPS21_YEAST | |
|---|---|---|
| UniProt AC | P36017 | |
| Protein Name | Vacuolar protein sorting-associated protein 21 | |
| Gene Name | VPS21 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 210 | |
| Subcellular Localization |
Endosome membrane Lipid-anchor . Mitochondrion membrane Lipid-anchor . |
|
| Protein Description | Required for protein transport to the vacuole. Involved in two vesicle trafficking steps to the prevacuolar compartment (PVC), regulating the docking of endosomes and Golgi vesicles to the PVC by interacting with PEP7/VAC1 on the PVC membrane and promoting SNARE complex formation.. | |
| Protein Sequence | MNTSVTSIKLVLLGEAAVGKSSIVLRFVSNDFAENKEPTIGAAFLTQRVTINEHTVKFEIWDTAGQERFASLAPMYYRNAQAALVVYDVTKPQSFIKARHWVKELHEQASKDIIIALVGNKIDMLQEGGERKVAREEGEKLAEEKGLLFFETSAKTGENVNDVFLGIGEKIPLKTAEEQNSASNERESNNQRVDLNAANDGTSANSACSC | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MNTSVTSIKLVLLG -CCCCCCEEEEEEEC | 18.64 | 30377154 | |
| 36 | Ubiquitination | SNDFAENKEPTIGAA CCCCCCCCCCCCEEE | 57.48 | 23749301 | |
| 36 | Acetylation | SNDFAENKEPTIGAA CCCCCCCCCCCCEEE | 57.48 | 24489116 | |
| 50 | Phosphorylation | AFLTQRVTINEHTVK EEEEEEEEECCCEEE | 21.92 | 28889911 | |
| 91 | Acetylation | LVVYDVTKPQSFIKA EEEEECCCCHHHHHH | 40.69 | 24489116 | |
| 97 | Acetylation | TKPQSFIKARHWVKE CCCHHHHHHHHHHHH | 37.04 | 24489116 | |
| 103 | Acetylation | IKARHWVKELHEQAS HHHHHHHHHHHHHHC | 49.74 | 22865919 | |
| 140 | Ubiquitination | VAREEGEKLAEEKGL HHHHHHHHHHHHHCE | 64.95 | 23749301 | |
| 140 | Acetylation | VAREEGEKLAEEKGL HHHHHHHHHHHHHCE | 64.95 | 24489116 | |
| 145 | Acetylation | GEKLAEEKGLLFFET HHHHHHHHCEEEEEC | 46.49 | 24489116 | |
| 170 | Acetylation | VFLGIGEKIPLKTAE EECCCCCCCCCCCHH | 44.40 | 24489116 | |
| 174 | Ubiquitination | IGEKIPLKTAEEQNS CCCCCCCCCHHHHCC | 40.09 | 23749301 | |
| 175 | Phosphorylation | GEKIPLKTAEEQNSA CCCCCCCCHHHHCCC | 47.16 | 29136822 | |
| 181 | Phosphorylation | KTAEEQNSASNERES CCHHHHCCCCCCCCC | 32.54 | 29136822 | |
| 183 | Phosphorylation | AEEQNSASNERESNN HHHHCCCCCCCCCCC | 38.76 | 29136822 | |
| 188 | Phosphorylation | SASNERESNNQRVDL CCCCCCCCCCCCCCC | 47.50 | 21082442 | |
| 206 | Phosphorylation | NDGTSANSACSC--- CCCCCCCCCCCC--- | 30.30 | 27017623 | |
| 208 | Geranylgeranylation | GTSANSACSC----- CCCCCCCCCC----- | 4.24 | - | |
| 209 | Phosphorylation | TSANSACSC------ CCCCCCCCC------ | 23.68 | 27017623 | |
| 210 | Geranylgeranylation | SANSACSC------- CCCCCCCC------- | 6.95 | - | |
| 210 | Methylation | SANSACSC------- CCCCCCCC------- | 6.95 | - |
| 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 VPS21_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VPS21_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 VPS21_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-181 AND SER-188, 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-188, AND MASSSPECTROMETRY. | |
