| UniProt ID | ELO3_YEAST | |
|---|---|---|
| UniProt AC | P40319 | |
| Protein Name | Elongation of fatty acids protein 3 {ECO:0000303|PubMed:9211877} | |
| Gene Name | ELO3 {ECO:0000303|PubMed:9211877} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 345 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Component of a microsomal membrane bound long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase III, which synthesizes 20-26-carbon fatty acids from 18-carbon-fatty acyl-CoA primers such as stearoyl-CoA by incorporation of malonyl-CoA. [PubMed: 9211877] | |
| Protein Sequence | MNTTTSTVIAAVADQFQSLNSSSSCFLKVHVPSIENPFGIELWPIFSKVFEYFSGYPAEQFEFIHNKTFLANGYHAVSIIIVYYIIIFGGQAILRALNASPLKFKLLFEIHNLFLTSISLVLWLLMLEQLVPMVYHNGLFWSICSKEAFAPKLVTLYYLNYLTKFVELIDTVFLVLRRKKLLFLHTYHHGATALLCYTQLIGRTSVEWVVILLNLGVHVIMYWYYFLSSCGIRVWWKQWVTRFQIIQFLIDLVFVYFATYTFYAHKYLDGILPNKGTCYGTQAAAAYGYLILTSYLLLFISFYIQSYKKGGKKTVKKESEVSGSVASGSSTGVKTSNTKVSSRKA | |
| 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 |
|---|---|---|---|---|---|
| 2 | N-linked_Glycosylation | ------MNTTTSTVI ------CCCCHHHHH | 46.24 | - | |
| 3 | Phosphorylation | -----MNTTTSTVIA -----CCCCHHHHHH | 30.10 | 30377154 | |
| 4 | Phosphorylation | ----MNTTTSTVIAA ----CCCCHHHHHHH | 17.47 | 30377154 | |
| 20 | N-linked_Glycosylation | ADQFQSLNSSSSCFL HHHHHHCCCCCCCEE | 45.13 | - | |
| 28 | Ubiquitination | SSSSCFLKVHVPSIE CCCCCEEEEECCCCC | 15.28 | 17644757 | |
| 48 | Ubiquitination | ELWPIFSKVFEYFSG CHHHHHHHHHHHHCC | 39.95 | 17644757 | |
| 66 | N-linked_Glycosylation | EQFEFIHNKTFLANG HHHHEECCCCHHHCC | 40.00 | - | |
| 277 | Phosphorylation | GILPNKGTCYGTQAA CCCCCCCCCHHHHHH | 12.26 | 27017623 | |
| 279 | Phosphorylation | LPNKGTCYGTQAAAA CCCCCCCHHHHHHHH | 24.05 | 28132839 | |
| 281 | Phosphorylation | NKGTCYGTQAAAAYG CCCCCHHHHHHHHHH | 6.64 | 27017623 | |
| 287 | Phosphorylation | GTQAAAAYGYLILTS HHHHHHHHHHHHHHH | 11.11 | 28132839 | |
| 289 | Phosphorylation | QAAAAYGYLILTSYL HHHHHHHHHHHHHHH | 4.29 | 27017623 | |
| 294 | Phosphorylation | YGYLILTSYLLLFIS HHHHHHHHHHHHHHH | 15.44 | 27017623 | |
| 295 | Phosphorylation | GYLILTSYLLLFISF HHHHHHHHHHHHHHH | 8.99 | 27017623 | |
| 314 | Phosphorylation | YKKGGKKTVKKESEV HHCCCEEEECEEEEC | 40.83 | 19779198 | |
| 317 | Ubiquitination | GGKKTVKKESEVSGS CCEEEECEEEECCCC | 63.24 | 23749301 | |
| 319 | Phosphorylation | KKTVKKESEVSGSVA EEEECEEEECCCCEE | 52.78 | 21551504 | |
| 322 | Phosphorylation | VKKESEVSGSVASGS ECEEEECCCCEECCC | 22.69 | 30377154 | |
| 324 | Phosphorylation | KESEVSGSVASGSST EEEECCCCEECCCCC | 13.65 | 30377154 | |
| 327 | Phosphorylation | EVSGSVASGSSTGVK ECCCCEECCCCCCCC | 36.73 | 22369663 | |
| 329 | Phosphorylation | SGSVASGSSTGVKTS CCCEECCCCCCCCCC | 23.41 | 22369663 | |
| 330 | Phosphorylation | GSVASGSSTGVKTSN CCEECCCCCCCCCCC | 32.48 | 22369663 | |
| 331 | Phosphorylation | SVASGSSTGVKTSNT CEECCCCCCCCCCCC | 47.92 | 22369663 | |
| 334 | Ubiquitination | SGSSTGVKTSNTKVS CCCCCCCCCCCCCCC | 47.80 | 17644757 | |
| 335 | Phosphorylation | GSSTGVKTSNTKVSS CCCCCCCCCCCCCCC | 25.46 | 28889911 | |
| 336 | Phosphorylation | SSTGVKTSNTKVSSR CCCCCCCCCCCCCCC | 36.46 | 28889911 | |
| 338 | Phosphorylation | TGVKTSNTKVSSRKA CCCCCCCCCCCCCCC | 32.37 | 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 ELO3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ELO3_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 ELO3_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-327, AND MASSSPECTROMETRY. | |
