UniProt ID | EKI1_HUMAN | |
---|---|---|
UniProt AC | Q9HBU6 | |
Protein Name | Ethanolamine kinase 1 | |
Gene Name | ETNK1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 452 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis.. | |
Protein Sequence | MLCGRPRSSSDNRNFLRERAGLSSAAVQTRIGNSAASRRSPAARPPVPAPPALPRGRPGTEGSTSLSAPAVLVVAVAVVVVVVSAVAWAMANYIHVPPGSPEVPKLNVTVQDQEEHRCREGALSLLQHLRPHWDPQEVTLQLFTDGITNKLIGCYVGNTMEDVVLVRIYGNKTELLVDRDEEVKSFRVLQAHGCAPQLYCTFNNGLCYEFIQGEALDPKHVCNPAIFRLIARQLAKIHAIHAHNGWIPKSNLWLKMGKYFSLIPTGFADEDINKRFLSDIPSSQILQEEMTWMKEILSNLGSPVVLCHNDLLCKNIIYNEKQGDVQFIDYEYSGYNYLAYDIGNHFNEFAGVSDVDYSLYPDRELQSQWLRAYLEAYKEFKGFGTEVTEKEVEILFIQVNQFALASHFFWGLWALIQAKYSTIEFDFLGYAIVRFNQYFKMKPEVTALKVPE | |
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 |
---|---|---|---|---|---|
34 | Phosphorylation | VQTRIGNSAASRRSP HHHHHCCCHHHCCCC | 21.72 | 23532336 | |
37 | Phosphorylation | RIGNSAASRRSPAAR HHCCCHHHCCCCCCC | 28.13 | 23532336 | |
40 | Phosphorylation | NSAASRRSPAARPPV CCHHHCCCCCCCCCC | 20.13 | 28555341 | |
100 | Phosphorylation | YIHVPPGSPEVPKLN CCCCCCCCCCCCCCE | 24.54 | 22199227 | |
172 | Ubiquitination | LVRIYGNKTELLVDR EEEEECCCEEEEECC | 38.73 | 21890473 | |
179 | Methylation | KTELLVDRDEEVKSF CEEEEECCCHHHHHH | 45.84 | - | |
184 | Acetylation | VDRDEEVKSFRVLQA ECCCHHHHHHHHHHH | 47.35 | 25953088 | |
184 | Ubiquitination | VDRDEEVKSFRVLQA ECCCHHHHHHHHHHH | 47.35 | 21906983 | |
255 | Ubiquitination | PKSNLWLKMGKYFSL CCCCEEEECCCEEEE | 33.74 | 21906983 | |
258 | Acetylation | NLWLKMGKYFSLIPT CEEEECCCEEEECCC | 39.36 | 25953088 | |
258 | Ubiquitination | NLWLKMGKYFSLIPT CEEEECCCEEEECCC | 39.36 | - | |
274 | Ubiquitination | FADEDINKRFLSDIP CCCHHHHHHHHHCCC | 44.88 | 21906983 | |
314 | Ubiquitination | CHNDLLCKNIIYNEK ECCCEEHHHCCEECC | 51.67 | - | |
321 | Ubiquitination | KNIIYNEKQGDVQFI HHCCEECCCCCEEEE | 56.81 | - | |
360 | Phosphorylation | SDVDYSLYPDRELQS CCCCCCCCCCHHHHH | 9.35 | 27196784 | |
378 | Ubiquitination | RAYLEAYKEFKGFGT HHHHHHHHHHCCCCC | 64.82 | 21906983 | |
381 | Ubiquitination | LEAYKEFKGFGTEVT HHHHHHHCCCCCCCC | 55.19 | - | |
446 | Phosphorylation | FKMKPEVTALKVPE- CCCCCCCEEEECCC- | 25.30 | 28857561 | |
449 | Acetylation | KPEVTALKVPE---- CCCCEEEECCC---- | 53.96 | 19608861 | |
449 | Ubiquitination | KPEVTALKVPE---- CCCCEEEECCC---- | 53.96 | 19608861 |
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_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EKI1_HUMAN !! |
* 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_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EKI1_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, AND MASS SPECTROMETRY. |