UniProt ID | AYR1_YEAST | |
---|---|---|
UniProt AC | P40471 | |
Protein Name | NADPH-dependent 1-acyldihydroxyacetone phosphate reductase | |
Gene Name | AYR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 297 | |
Subcellular Localization | Lipid droplet. Endoplasmic reticulum. | |
Protein Description | Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP) into glycerolipids and ether lipids, respectively. Required for the biosynthesis of phosphatidic acid via the DHAP pathway, where it reduces 1-acyl DHAP to lysophosphatidic acid (LPA). Required for spore germination.. | |
Protein Sequence | MSELQSQPKKIAVVTGASGGIGYEVTKELARNGYLVYACARRLEPMAQLAIQFGNDSIKPYKLDISKPEEIVTFSGFLRANLPDGKLDLLYNNAGQSCTFPALDATDAAVEQCFKVNVFGHINMCRELSEFLIKAKGTIVFTGSLAGVVSFPFGSIYSASKAAIHQYARGLHLEMKPFNVRVINAITGGVATDIADKRPLPETSIYNFPEGREAFNSRKTMAKDNKPMPADAYAKQLVKDILSTSDPVDVYRGTFANIMRFVMIFVPYWLLEKGLSKKFKLDKVNNALKSKQKNKDD | |
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 |
---|---|---|---|---|---|
9 | Ubiquitination | SELQSQPKKIAVVTG HHHHCCCCEEEEEEC | 49.53 | 17644757 | |
10 | Ubiquitination | ELQSQPKKIAVVTGA HHHCCCCEEEEEECC | 42.45 | 17644757 | |
27 | Ubiquitination | GIGYEVTKELARNGY CCCHHHHHHHHHCCC | 56.77 | 17644757 | |
134 | Acetylation | ELSEFLIKAKGTIVF HHHHHHHHCCCEEEE | 46.31 | 24489116 | |
176 | Acetylation | RGLHLEMKPFNVRVI CCCCCEECCCCCEEE | 36.76 | 24489116 | |
176 | Ubiquitination | RGLHLEMKPFNVRVI CCCCCEECCCCCEEE | 36.76 | 24961812 | |
197 | Acetylation | VATDIADKRPLPETS CCCCCCCCCCCCCCC | 47.06 | 24489116 | |
197 | Ubiquitination | VATDIADKRPLPETS CCCCCCCCCCCCCCC | 47.06 | 17644757 | |
226 | Ubiquitination | KTMAKDNKPMPADAY CCCCCCCCCCCHHHH | 53.48 | 23749301 | |
235 | Acetylation | MPADAYAKQLVKDIL CCHHHHHHHHHHHHH | 31.33 | 24489116 | |
235 | Ubiquitination | MPADAYAKQLVKDIL CCHHHHHHHHHHHHH | 31.33 | 22817900 | |
239 | Acetylation | AYAKQLVKDILSTSD HHHHHHHHHHHHCCC | 47.87 | 24489116 | |
239 | Ubiquitination | AYAKQLVKDILSTSD HHHHHHHHHHHHCCC | 47.87 | 23749301 | |
243 | Phosphorylation | QLVKDILSTSDPVDV HHHHHHHHCCCCCHH | 26.63 | 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 AYR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of AYR1_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 AYR1_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-243, AND MASSSPECTROMETRY. |