| UniProt ID | SYS1_YEAST | |
|---|---|---|
| UniProt AC | P41544 | |
| Protein Name | Protein SYS1 | |
| Gene Name | SYS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 203 | |
| Subcellular Localization |
Golgi apparatus membrane Multi-pass membrane protein. |
|
| Protein Description | Necessary for the targeting of ARL3 to the Golgi. Involved in protein trafficking. May serve as a receptor for acetylated ARL3.. | |
| Protein Sequence | MVSIRRYLRVPNELKPSQIFKQDSLSPSKIGLQIVLLQIFYYTTAIVLFYCWAKLAGYDLNIKEWLFSWENIDFTNAYGLSISLLWLLDSLICVFFLTVIVGRSKLAWDFAITIHAINFIVVFLYTRKFPSFSWFFLQILSSLILIFLGTWTTRWRELRDTFFEGLVDPNEGEVGLVTPSQQHSNHSELEQSPIQLKDLESQI | |
| 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 |
|---|---|---|---|---|---|
| 15 | Ubiquitination | LRVPNELKPSQIFKQ CCCCCCCCHHHCCCC | 36.12 | 23749301 | |
| 24 | Phosphorylation | SQIFKQDSLSPSKIG HHCCCCCCCCHHHHH | 28.40 | 21126336 | |
| 192 | Phosphorylation | NHSELEQSPIQLKDL CCHHHHCCCCCHHHH | 18.00 | 28889911 |
| 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 SYS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SYS1_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 SYS1_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-192, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery."; Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15, AND MASSSPECTROMETRY. | |