| UniProt ID | LAG1_YEAST | |
|---|---|---|
| UniProt AC | P38703 | |
| Protein Name | Sphingosine N-acyltransferase LAG1 | |
| Gene Name | LAG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 411 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein. |
|
| Protein Description | Component of the ceramide synthase complex required for C26-CoA-dependent ceramide synthesis. Redundant with LAC1. Facilitates ER-to-Golgi transport of GPI-anchored proteins. Involved in the aging process. Deletion of LAG1 results in a pronounced increase (approximately 50%) in mean and in maximum life span.. | |
| Protein Sequence | MTSATDKSIDRLVVNAKTRRRNSSVGKIDLGDTVPGFAAMPESAASKNEAKKRMKALTGDSKKDSDLLWKVWFSYREMNYRHSWLTPFFILVCVYSAYFLSGNRTESNPLHMFVAISYQVDGTDSYAKGIKDLSFVFFYMIFFTFLREFLMDVVIRPFTVYLNVTSEHRQKRMLEQMYAIFYCGVSGPFGLYIMYHSDLWLFKTKPMYRTYPVITNPFLFKIFYLGQAAFWAQQACVLVLQLEKPRKDYKELVFHHIVTLLLIWSSYVFHFTKMGLAIYITMDVSDFFLSLSKTLNYLNSVFTPFVFGLFVFFWIYLRHVVNIRILWSVLTEFRHEGNYVLNFATQQYKCWISLPIVFVLIAALQLVNLYWLFLILRILYRLIWQGIQKDERSDSDSDESAENEESKEKCE | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MTSATDKSID -----CCCCCHHCHH | 28.07 | 30377154 | |
| 8 | Phosphorylation | MTSATDKSIDRLVVN CCCCCHHCHHHHHHC | 32.31 | 28889911 | |
| 18 | Phosphorylation | RLVVNAKTRRRNSSV HHHHCCCCCCCCCCC | 27.31 | 24961812 | |
| 23 | Phosphorylation | AKTRRRNSSVGKIDL CCCCCCCCCCCEECC | 25.29 | 22369663 | |
| 24 | Phosphorylation | KTRRRNSSVGKIDLG CCCCCCCCCCEECCC | 38.14 | 22369663 | |
| 33 | Phosphorylation | GKIDLGDTVPGFAAM CEECCCCCCCCCCCC | 27.14 | 22369663 | |
| 43 | Phosphorylation | GFAAMPESAASKNEA CCCCCCHHHCCHHHH | 24.22 | 22369663 | |
| 46 | Phosphorylation | AMPESAASKNEAKKR CCCHHHCCHHHHHHH | 35.41 | 22369663 | |
| 103 | N-linked_Glycosylation | SAYFLSGNRTESNPL HHHHHCCCCCCCCCE | 44.30 | - | |
| 389 | Ubiquitination | LIWQGIQKDERSDSD HHHHHHCCCCCCCCC | 60.68 | 24961812 | |
| 395 | Phosphorylation | QKDERSDSDSDESAE CCCCCCCCCCCHHHH | 40.02 | 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 LAG1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LAG1_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 LAG1_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-8 AND SER-24, AND MASSSPECTROMETRY. | |
| "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-23 AND SER-24, AND MASSSPECTROMETRY. | |