| UniProt ID | EKI1_YEAST | |
|---|---|---|
| UniProt AC | Q03764 | |
| Protein Name | Ethanolamine kinase | |
| Gene Name | EKI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 534 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the committed step of phosphatidylethanolamine synthesis via the CDP-ethanolamine pathway. Also exhibits choline kinase activity but its preferred substrate is ethanolamine.. | |
| Protein Sequence | MYTNYSLTSSDAMPRTYLVGTASPEMSKKKRQSANCDKPTRRVIHIIDTNEHSEVDLKNELPITCTNEDGEMTSSSWTSQTANDFLKLAYVNAKLDPSLPSQYFKQDIINVLQSLEIPGWSVPGSKESSLNKNLLTLTQIKGALTNVIYKIHYPNLPPLLMRIFGDSIDSVIDREYELKVIARLSFYDLGPKLEGFFENGRFEKYIEGSRTSTQADFIDRDTSIKIAKKLKELHCTVPLTHKEITDQPSCWTTFDQWIKLIDSHKEWVSNNVNISENLRCSSWNFFLKSFKNYKRWLYNDSAFTSKLLREDDKDSMINSGLKMVFCHNDLQHGNLLFKSKGKDDISVGDLTIIDFEYAGPNPVVFDLSNHLNEWMQDYNDVQSFKSHIDKYPKEEDILVFAQSYINHMNENHVKIASQEVRILYNLIIEWRPCTQLFWCLWALLQSGRLPQRPLIEGEKLMSEKAGLGDETHLMEHKNKENGKYDCSEDDSFNYLGFCKEKMSVFWGDLITLGVIDKDCPDIGKTDYLDTKLIF | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MYTNYSLTS ------CCCCCCCCC | 12.05 | 23607784 | |
| 3 | Phosphorylation | -----MYTNYSLTSS -----CCCCCCCCCC | 26.78 | 23607784 | |
| 5 | Phosphorylation | ---MYTNYSLTSSDA ---CCCCCCCCCCCC | 9.39 | 23607784 | |
| 6 | Phosphorylation | --MYTNYSLTSSDAM --CCCCCCCCCCCCC | 27.52 | 23607784 | |
| 8 | Phosphorylation | MYTNYSLTSSDAMPR CCCCCCCCCCCCCCC | 21.90 | 23607784 | |
| 9 | Phosphorylation | YTNYSLTSSDAMPRT CCCCCCCCCCCCCCE | 31.36 | 23607784 | |
| 10 | Phosphorylation | TNYSLTSSDAMPRTY CCCCCCCCCCCCCEE | 24.93 | 23607784 | |
| 16 | Phosphorylation | SSDAMPRTYLVGTAS CCCCCCCEEEEECCC | 18.48 | 23607784 | |
| 17 | Phosphorylation | SDAMPRTYLVGTASP CCCCCCEEEEECCCH | 10.73 | 23607784 | |
| 21 | Phosphorylation | PRTYLVGTASPEMSK CCEEEEECCCHHHHH | 19.24 | 21440633 | |
| 23 | Phosphorylation | TYLVGTASPEMSKKK EEEEECCCHHHHHHH | 22.64 | 21082442 | |
| 27 | Phosphorylation | GTASPEMSKKKRQSA ECCCHHHHHHHHHHC | 39.39 | 23607784 | |
| 132 | Acetylation | SKESSLNKNLLTLTQ CCHHHCCCCHHHHHH | 55.02 | 24489116 | |
| 301 | Phosphorylation | KRWLYNDSAFTSKLL HHHHHCCCHHHHHHC | 22.96 | 28889911 | |
| 313 | Acetylation | KLLREDDKDSMINSG HHCCCCCHHHCHHHC | 65.11 | 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 EKI1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EKI1_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 EKI1_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-23 AND SER-301, AND MASSSPECTROMETRY. | |