| UniProt ID | AUR1_YEAST | |
|---|---|---|
| UniProt AC | P36107 | |
| Protein Name | Inositol phosphorylceramide synthase catalytic subunit AUR1 | |
| Gene Name | AUR1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 401 | |
| Subcellular Localization |
Golgi apparatus, Golgi stack membrane Multi-pass membrane protein . |
|
| Protein Description | Catalytic component of the inositol phosphorylceramide synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis.. | |
| Protein Sequence | MANPFSRWFLSERPPNCHVADLETSLDPHQTLLKVQKYKPALSDWVHYIFLGSIMLFVFITNPAPWIFKILFYCFLGTLFIIPATSQFFFNALPILTWVALYFTSSYFPDDRRPPITVKVLPAVETILYGDNLSDILATSTNSFLDILAWLPYGLFHFGAPFVVAAILFVFGPPTVLQGYAFAFGYMNLFGVIMQNVFPAAPPWYKILYGLQSANYDMHGSPGGLARIDKLLGINMYTTAFSNSSVIFGAFPSLHSGCATMEALFFCYCFPKLKPLFIAYVCWLWWSTMYLTHHYFVDLMAGSVLSYVIFQYTKYTHLPIVDTSLFCRWSYTSIEKYDISKSDPLAADSNDIESVPLSNLELDFDLNMTDEPSVSPSLFDGSTSVSRSSATSITSLGVKRA | |
| 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 |
|---|---|---|---|---|---|
| 34 | Ubiquitination | DPHQTLLKVQKYKPA CHHHHHHHHHHHHHH | 45.81 | 17644757 | |
| 132 | N-linked_Glycosylation | ETILYGDNLSDILAT EEHHCCCCHHHHHHH | 36.76 | - | |
| 388 | Phosphorylation | GSTSVSRSSATSITS CCCCCCCCCCCCCHH | 19.47 | 22369663 | |
| 389 | Phosphorylation | STSVSRSSATSITSL CCCCCCCCCCCCHHC | 34.16 | 22369663 | |
| 391 | Phosphorylation | SVSRSSATSITSLGV CCCCCCCCCCHHCCC | 23.70 | 22369663 | |
| 392 | Phosphorylation | VSRSSATSITSLGVK CCCCCCCCCHHCCCC | 24.48 | 22369663 | |
| 394 | Phosphorylation | RSSATSITSLGVKRA CCCCCCCHHCCCCCC | 20.05 | 22369663 | |
| 395 | Phosphorylation | SSATSITSLGVKRA- CCCCCCHHCCCCCC- | 22.81 | 22369663 | |
| 399 | Ubiquitination | SITSLGVKRA----- CCHHCCCCCC----- | 40.59 | 23749301 |
| 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 AUR1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AUR1_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 AUR1_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-389; SER-392 ANDSER-395, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-395, ANDMASS SPECTROMETRY. | |
