| UniProt ID | MON1_YEAST | |
|---|---|---|
| UniProt AC | P53129 | |
| Protein Name | Vacuolar fusion protein MON1 | |
| Gene Name | MON1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 644 | |
| Subcellular Localization |
Endosome, multivesicular body membrane Peripheral membrane protein. Prevacuolar compartment membrane Peripheral membrane protein. Vacuole membrane Peripheral membrane protein. The association of the CCZ1-MON1 complex with the vacuole is regulat |
|
| Protein Description | In complex with CCZ1, is required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. The CCZ1-MON1 complex acts at the fusion of vesicles with the vacuole, through its regulation of the SNARE complex during the coordinated priming and docking stages of fusion, and particularly at the stage of tethering/docking.. | |
| Protein Sequence | MNLNESYLDAEIPKGQLKHSKSGNFEGIPIVATTSEPTTSVNLDETFFKKAPIAMPICDDHSVSKSTSVNSLNTTSLASRRSPLQTKKLQAKNNLLSADLAKSNDDTTRALNSPKKDFGPYLDSENDIRSRLAESIYSMETSIRGSELQRRPYVSNEIPNVFKFSKFNSNCKLNESQTLCDKNFFIFTSAGKPIYCMHGKDEQIMSYTGLVNTVISYFQVNGPSELKTISTLTSGKRLTFLDKSPILLMAQSERGESSNELLNQLDFLYSYILSSLSERQLLRLFSKRENFDLRNYLESTDFENLDEICSLICNRMFPDLLLNSLQCLPFNHSSRLKLQNVVLQQLEKRQDIPRGTLLYGLIIAPQNKLCCVLRPRGHTLHTTDLHLLFCLISHQFQNLDETQELWVPICFPKFNSSGFLYCYIKFLPNDTHSNEKSALVLISAQKDAFFSLKSFSDELIIKLEEEKLLKKINTSKGFKLSDIPAPMVHHFIYKSKQNVQYVMPHFEVNSNIALDSSQGLEYELKLKTYYQQLHGTVVRDNGNLLSRSMLNFVRWSSKDNEDLAMDETQMDFSELDEYIIGNSSFKQESVNMVGMAWVTPTFELYLIGNNGIVDKRVLFKSARKVANWCQKHESRLFISDGAVF | |
| 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 |
|---|---|---|---|---|---|
| 20 | Phosphorylation | PKGQLKHSKSGNFEG CCCCCCCCCCCCCCC | 27.25 | 21440633 | |
| 22 | Phosphorylation | GQLKHSKSGNFEGIP CCCCCCCCCCCCCCC | 41.82 | 22369663 | |
| 35 | Phosphorylation | IPIVATTSEPTTSVN CCEEEECCCCCCCCC | 36.90 | 21440633 | |
| 62 | Phosphorylation | MPICDDHSVSKSTSV CEECCCCCCCCCCCC | 34.77 | 21440633 | |
| 64 | Phosphorylation | ICDDHSVSKSTSVNS ECCCCCCCCCCCCCC | 24.73 | 21440633 | |
| 66 | Phosphorylation | DDHSVSKSTSVNSLN CCCCCCCCCCCCCCC | 20.57 | 22369663 | |
| 67 | Phosphorylation | DHSVSKSTSVNSLNT CCCCCCCCCCCCCCC | 40.19 | 22369663 | |
| 68 | Phosphorylation | HSVSKSTSVNSLNTT CCCCCCCCCCCCCCC | 26.79 | 22369663 | |
| 71 | Phosphorylation | SKSTSVNSLNTTSLA CCCCCCCCCCCCCCC | 22.35 | 22369663 | |
| 74 | Phosphorylation | TSVNSLNTTSLASRR CCCCCCCCCCCCCCC | 24.05 | 22369663 | |
| 75 | Phosphorylation | SVNSLNTTSLASRRS CCCCCCCCCCCCCCC | 22.22 | 22369663 | |
| 76 | Phosphorylation | VNSLNTTSLASRRSP CCCCCCCCCCCCCCC | 21.65 | 22369663 | |
| 79 | Phosphorylation | LNTTSLASRRSPLQT CCCCCCCCCCCCCCH | 33.25 | 22369663 | |
| 82 | Phosphorylation | TSLASRRSPLQTKKL CCCCCCCCCCCHHHH | 28.93 | 22369663 | |
| 86 | Phosphorylation | SRRSPLQTKKLQAKN CCCCCCCHHHHHHHC | 37.52 | 22369663 | |
| 103 | Phosphorylation | LSADLAKSNDDTTRA HHHHHHHCCCHHHHH | 39.62 | 23749301 | |
| 113 | Phosphorylation | DTTRALNSPKKDFGP HHHHHHCCCCCCCCC | 38.66 | 21551504 | |
| 121 | Phosphorylation | PKKDFGPYLDSENDI CCCCCCCCCCCHHHH | 24.42 | 22369663 | |
| 124 | Phosphorylation | DFGPYLDSENDIRSR CCCCCCCCHHHHHHH | 35.39 | 22369663 | |
| 130 | Phosphorylation | DSENDIRSRLAESIY CCHHHHHHHHHHHHH | 31.79 | 22369663 | |
| 135 | Phosphorylation | IRSRLAESIYSMETS HHHHHHHHHHHHHCC | 22.63 | 22369663 | |
| 138 | Phosphorylation | RLAESIYSMETSIRG HHHHHHHHHHCCCCC | 14.42 | 22369663 | |
| 141 | Phosphorylation | ESIYSMETSIRGSEL HHHHHHHCCCCCCHH | 22.32 | 22369663 | |
| 142 | Phosphorylation | SIYSMETSIRGSELQ HHHHHHCCCCCCHHH | 9.29 | 23749301 | |
| 230 | Phosphorylation | PSELKTISTLTSGKR CHHHCEEEECCCCCC | 23.69 | 21551504 | |
| 231 | Phosphorylation | SELKTISTLTSGKRL HHHCEEEECCCCCCE | 30.15 | 21551504 |
| 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 MON1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MON1_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 MON1_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-68; SER-71 AND SER-138,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-82, AND MASSSPECTROMETRY. | |
