| UniProt ID | MKAR_YEAST | |
|---|---|---|
| UniProt AC | P38286 | |
| Protein Name | Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_03107} | |
| Gene Name | IFA38 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 347 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Single-pass membrane protein . |
|
| Protein Description | Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.. | |
| Protein Sequence | MTFMQQLQEAGERFRCINGLLWVVFGLGVLKCTTLSLRFLALIFDLFLLPAVNFDKYGAKTGKYCAITGASDGIGKEFARQMAKRGFNLVLISRTQSKLEALQKELEDQHHVVVKILAIDIAEDKESNYESIKELCAQLPITVLVNNVGQSHSIPVPFLETEEKELRNIITINNTATLLITQIIAPKIVETVKAENKKSGTRGLILTMGSFGGLIPTPLLATYSGSKSFLQGWSNSLAGELSKDAIDVELIISYLVTSSMSKIRRSSLMIPNPQQFVKSTLRSVGRRCGSQERYATMTPYWAHAVYQFVITETFGVYSKIVNSINYSFHKSIRIRALKKAARQVKKE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 60 | Ubiquitination | NFDKYGAKTGKYCAI CHHHCCCCCCCEEEE | 54.14 | 22817900 | |
| 63 | Ubiquitination | KYGAKTGKYCAITGA HCCCCCCCEEEECCC | 42.25 | 23749301 | |
| 63 | Acetylation | KYGAKTGKYCAITGA HCCCCCCCEEEECCC | 42.25 | 24489116 | |
| 76 | Ubiquitination | GASDGIGKEFARQMA CCCCCCHHHHHHHHH | 47.97 | 23749301 | |
| 76 | Acetylation | GASDGIGKEFARQMA CCCCCCHHHHHHHHH | 47.97 | 24489116 | |
| 97 | Phosphorylation | VLISRTQSKLEALQK EEEECCHHHHHHHHH | 38.30 | 28889911 | |
| 98 | Acetylation | LISRTQSKLEALQKE EEECCHHHHHHHHHH | 40.29 | 24489116 | |
| 177 | Phosphorylation | ITINNTATLLITQII EEECCHHHHHHHHHH | 21.76 | 27017623 | |
| 181 | Phosphorylation | NTATLLITQIIAPKI CHHHHHHHHHHHHHH | 17.43 | 27017623 | |
| 278 | Acetylation | PNPQQFVKSTLRSVG CCHHHHHHHHHHHHH | 38.72 | 24489116 |
| 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 MKAR_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MKAR_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 MKAR_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-97, AND MASSSPECTROMETRY. | |