UniProt ID | EPT1_HUMAN | |
---|---|---|
UniProt AC | Q9C0D9 | |
Protein Name | Ethanolaminephosphotransferase 1 {ECO:0000305} | |
Gene Name | SELENOI {ECO:0000312|HGNC:HGNC:29361} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 397 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the formation of phosphatidylethanolamine via 'Kennedy' pathway.. | |
Protein Sequence | MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLLVVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPLGELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGILFLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLLNFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAFANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIHYGVRVVKQLSSHFQIYPFSLRKPNSDULGMEEKNIGL | |
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 | Acetylation | ------MAGYEYVSP ------CCCCCCCCH | 29.31 | 22223895 | |
4 | Phosphorylation | ----MAGYEYVSPEQ ----CCCCCCCCHHH | 8.44 | 23663014 | |
6 | Phosphorylation | --MAGYEYVSPEQLA --CCCCCCCCHHHHC | 9.57 | 23663014 | |
8 | Phosphorylation | MAGYEYVSPEQLAGF CCCCCCCCHHHHCCC | 23.09 | 23663014 | |
17 | Ubiquitination | EQLAGFDKYKYSAVD HHHCCCCCCCCCCCC | 41.19 | 21890473 | |
18 | Phosphorylation | QLAGFDKYKYSAVDT HHCCCCCCCCCCCCC | 19.60 | 23663014 | |
19 | Ubiquitination | LAGFDKYKYSAVDTN HCCCCCCCCCCCCCC | 38.17 | - | |
31 | Phosphorylation | DTNPLSLYVMHPFWN CCCCCEEEEECHHHH | 7.73 | - | |
247 | Ubiquitination | LNFFRSYKNNTLKLN HHHHHHHCCCCEEEC | 44.99 | 27667366 |
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 EPT1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EPT1_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 EPT1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EPT1_HUMAN !! |
Kegg Disease | ||||||
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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 |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. |