UniProt ID | SNA3_YEAST | |
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UniProt AC | P14359 | |
Protein Name | Protein SNA3 | |
Gene Name | SNA3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 133 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. Late endosome membrane Multi-pass membrane protein. Vacuole lumen. Cytoplasmic vesicle membrane Multi-pass membrane protein . Sorted via late endosomes to the vacuolar lumen in a ubiquitin-independent manner. |
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Protein Description | ||
Protein Sequence | MDRDHINDHDHRMSYSINKDDLLLMVLAVFIPPVAVWKRKGMFNRDTLLNLLLFLLLFFPAIIHACYVVYETSSERSYDLSRRHATAPAVDRDLEAHPAEESQAQPPAYDEDDEAGADVPLMDNKQQLSSGRT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of SNA3_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of SNA3_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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 THR-86, 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-125, AND MASSSPECTROMETRY. |