UniProt ID | DS1P1_YEAST | |
---|---|---|
UniProt AC | P47013 | |
Protein Name | Dihydrosphingosine 1-phosphate phosphatase LCB3 | |
Gene Name | LCB3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 409 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
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Protein Description | Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases. Involved in endocytosis and calcium-mediated signaling.. | |
Protein Sequence | MVDGLNTSNIRKRARTLSNPNDFQEPNYLLDPGNHPSDHFRTRMSKFRFNIREKLLVFTNNQSFTLSRWQKKYRSAFNDLYFTYTSLMGSHTFYVLCLPMPVWFGYFETTKDMVYILGYSIYLSGFFKDYWCLPRPRAPPLHRITLSEYTTKEYGAPSSHTANATGVSLLFLYNIWRMQESSVMVQLLLSCVVLFYYMTLVFGRIYCGMHGILDLVSGGLIGIVCFIVRMYFKYRFPGLRIEEHWWFPLFSVGWGLLLLFKHVKPVDECPCFQDSVAFMGVVSGIECCDWLGKVFGVTLVYNLEPNCGWRLTLARLLVGLPCVVIWKYVISKPMIYTLLIKVFHLKDDRNVAARKRLEATHKEGASKYECPLYIGEPKIDILGRFIIYAGVPFTVVMCSPVLFSLLNIA | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MVDGLNTSNIRKRAR CCCCCCHHHHHHHHH | 29.23 | 30377154 | |
16 | Phosphorylation | NIRKRARTLSNPNDF HHHHHHHCCCCCCCC | 33.29 | 22369663 | |
18 | Phosphorylation | RKRARTLSNPNDFQE HHHHHCCCCCCCCCC | 50.02 | 12786943 | |
28 | Phosphorylation | NDFQEPNYLLDPGNH CCCCCCCCCCCCCCC | 21.25 | 22369663 | |
37 | Phosphorylation | LDPGNHPSDHFRTRM CCCCCCCCHHHHHCH | 35.85 | 28889911 | |
42 | Phosphorylation | HPSDHFRTRMSKFRF CCCHHHHHCHHHHCC | 29.76 | 24961812 | |
45 | Phosphorylation | DHFRTRMSKFRFNIR HHHHHCHHHHCCCCC | 25.92 | 24961812 | |
115 | Phosphorylation | ETTKDMVYILGYSIY CCCHHHHHHHHHHHH | 5.47 | 24930733 | |
119 | Phosphorylation | DMVYILGYSIYLSGF HHHHHHHHHHHHCCC | 6.61 | 24930733 | |
366 | Phosphorylation | ATHKEGASKYECPLY HHHHCCCCCCCCCEE | 46.78 | 28889911 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of DS1P1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DS1P1_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 DS1P1_YEAST !! |
Kegg Drug | ||||||
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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-18, 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-18, AND MASSSPECTROMETRY. | |
"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 THR-16 AND SER-18, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY. |