UniProt ID | HFD1_YEAST | |
---|---|---|
UniProt AC | Q04458 | |
Protein Name | Fatty aldehyde dehydrogenase HFD1 | |
Gene Name | HFD1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 532 | |
Subcellular Localization |
Mitochondrion outer membrane Single-pass membrane protein . Endosome membrane Single-pass membrane protein . Cytoplasmic granule membrane Single-pass membrane protein . |
|
Protein Description | Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid.. | |
Protein Sequence | MSNDGSKILNYTPVSKIDEIVEISRNFFFEKQLKLSHENNPRKKDLEFRQLQLKKLYYAVKDHEEELIDAMYKDFHRNKIESVLNETTKLMNDILHLIEILPKLIKPRRVSDSSPPFMFGKTIVEKISRGSVLIIAPFNFPLLLAFAPLAAALAAGNTIVLKPSELTPHTAVVMENLLTTAGFPDGLIQVVQGAIDETTRLLDCGKFDLIFYTGSPRVGSIVAEKAAKSLTPCVLELGGKSPTFITENFKASNIKIALKRIFFGAFGNSGQICVSPDYLLVHKSIYPKVIKECESVLNEFYPSFDEQTDFTRMIHEPAYKKAVASINSTNGSKIVPSKISINSDTEDLCLVPPTIVYNIGWDDPLMKQENFAPVLPIIEYEDLDETINKIIEEHDTPLVQYIFSDSQTEINRILTRLRSGDCVVGDTVIHVGITDAPFGGIGTSGYGNYGGYYGFNTFSHERTIFKQPYWNDFTLFMRYPPNSAQKEKLVRFAMERKPWFDRNGNNKWGLRQYFSLSAAVILISTIYAHCSS | |
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 |
---|---|---|---|---|---|
11 | Phosphorylation | DGSKILNYTPVSKID CCCCCCCCCCCCHHH | 14.69 | 29688323 | |
12 | Phosphorylation | GSKILNYTPVSKIDE CCCCCCCCCCCHHHH | 19.01 | 29688323 | |
15 | Phosphorylation | ILNYTPVSKIDEIVE CCCCCCCCHHHHHHH | 25.71 | 29688323 | |
16 | Ubiquitination | LNYTPVSKIDEIVEI CCCCCCCHHHHHHHH | 55.18 | 24961812 | |
73 | Acetylation | ELIDAMYKDFHRNKI HHHHHHHHHHHHHHH | 40.61 | 24489116 | |
82 | Phosphorylation | FHRNKIESVLNETTK HHHHHHHHHHHHHHH | 35.06 | 29734811 | |
111 | Phosphorylation | LIKPRRVSDSSPPFM HHCCCCCCCCCCCCC | 29.93 | 22369663 | |
113 | Phosphorylation | KPRRVSDSSPPFMFG CCCCCCCCCCCCCCC | 36.92 | 28889911 | |
114 | Phosphorylation | PRRVSDSSPPFMFGK CCCCCCCCCCCCCCH | 41.40 | 27717283 | |
121 | Acetylation | SPPFMFGKTIVEKIS CCCCCCCHHHHHHHH | 24.66 | 24489116 | |
220 | Phosphorylation | TGSPRVGSIVAEKAA ECCCCHHHHHHHHHH | 15.84 | 27214570 | |
225 | Ubiquitination | VGSIVAEKAAKSLTP HHHHHHHHHHHHCCC | 43.86 | 23749301 | |
231 | Phosphorylation | EKAAKSLTPCVLELG HHHHHHCCCEEHHCC | 23.02 | 27214570 | |
241 | Phosphorylation | VLELGGKSPTFITEN EHHCCCCCCEEECCC | 32.23 | 28889911 | |
243 | Phosphorylation | ELGGKSPTFITENFK HCCCCCCEEECCCCH | 34.46 | 28889911 | |
250 | Ubiquitination | TFITENFKASNIKIA EEECCCCHHHCHHHH | 63.59 | 23749301 | |
252 | Phosphorylation | ITENFKASNIKIALK ECCCCHHHCHHHHHH | 39.41 | 28889911 | |
295 | Phosphorylation | KVIKECESVLNEFYP HHHHHHHHHHHHHCC | 43.49 | 27214570 | |
328 | Phosphorylation | KAVASINSTNGSKIV HHHEECCCCCCCEEC | 22.91 | 28889911 | |
333 | Ubiquitination | INSTNGSKIVPSKIS CCCCCCCEECCCEEE | 49.47 | 23749301 | |
406 | Phosphorylation | VQYIFSDSQTEINRI HHHHCCCCHHHHHHH | 37.49 | 27214570 |
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 HFD1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HFD1_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 HFD1_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-111, 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-111, 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 SER-111, AND MASSSPECTROMETRY. |