| UniProt ID | LDB16_YEAST | |
|---|---|---|
| UniProt AC | P25587 | |
| Protein Name | Protein LDB16 | |
| Gene Name | LDB16 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 256 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein . Lipid droplet . |
|
| Protein Description | May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface.. | |
| Protein Sequence | MFVVDWSVQLCMGVISPLFRALVQLPLSIFVWNGFQLVALPINIPLRLFLGTSLSRLVAQTSTLDFYVVLTLFQYFAVLCAFGSIIGLIFGFILGVFHSICGVPSVYISLEWKRWFAPIRTVLERASTSIVNIMRGQTIAPIPMPKPNPTHISKPNMKKFHDEPGADDMTITHDVNCYITPCQTPTNEKIQHYNNDSFNTTTTDDEPTDIWDRSDTYQNSFVTNETLMSLSNRAKLRRNASDADIVNIKILRRNSR | |
| 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 |
|---|---|---|---|---|---|
| 178 | Phosphorylation | ITHDVNCYITPCQTP EECCCEEEEECCCCC | 11.57 | 19779198 | |
| 180 | Phosphorylation | HDVNCYITPCQTPTN CCCEEEEECCCCCCC | 7.49 | 20377248 | |
| 184 | Phosphorylation | CYITPCQTPTNEKIQ EEEECCCCCCCCCCC | 38.50 | 20377248 | |
| 186 | Phosphorylation | ITPCQTPTNEKIQHY EECCCCCCCCCCCCC | 60.44 | 21551504 | |
| 200 | Phosphorylation | YNNDSFNTTTTDDEP CCCCCCCCCCCCCCC | 24.41 | 28889911 | |
| 202 | Phosphorylation | NDSFNTTTTDDEPTD CCCCCCCCCCCCCCC | 26.62 | 27017623 | |
| 203 | Phosphorylation | DSFNTTTTDDEPTDI CCCCCCCCCCCCCCC | 39.08 | 23749301 | |
| 214 | Phosphorylation | PTDIWDRSDTYQNSF CCCCCCCCCCCCCCC | 31.65 | 28889911 | |
| 216 | Phosphorylation | DIWDRSDTYQNSFVT CCCCCCCCCCCCCCC | 28.40 | 28889911 | |
| 217 | Phosphorylation | IWDRSDTYQNSFVTN CCCCCCCCCCCCCCH | 15.64 | 28889911 | |
| 220 | Phosphorylation | RSDTYQNSFVTNETL CCCCCCCCCCCHHHH | 12.93 | 28889911 | |
| 226 | Phosphorylation | NSFVTNETLMSLSNR CCCCCHHHHHHHHHH | 29.81 | 28889911 | |
| 229 | Phosphorylation | VTNETLMSLSNRAKL CCHHHHHHHHHHHHH | 31.58 | 28889911 | |
| 241 | Phosphorylation | AKLRRNASDADIVNI HHHHCCCCHHHHEEE | 36.56 | 22369663 | |
| 255 | Phosphorylation | IKILRRNSR------ EEEEECCCC------ | 37.24 | 19795423 |
| 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 LDB16_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LDB16_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 LDB16_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-241, 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-241, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY. | |
