EPT1_HUMAN - dbPTM
EPT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAGYEYVSP
------CCCCCCCCH
29.3122223895
4Phosphorylation----MAGYEYVSPEQ
----CCCCCCCCHHH
8.4423663014
6Phosphorylation--MAGYEYVSPEQLA
--CCCCCCCCHHHHC
9.5723663014
8PhosphorylationMAGYEYVSPEQLAGF
CCCCCCCCHHHHCCC
23.0923663014
17UbiquitinationEQLAGFDKYKYSAVD
HHHCCCCCCCCCCCC
41.1921890473
18PhosphorylationQLAGFDKYKYSAVDT
HHCCCCCCCCCCCCC
19.6023663014
19UbiquitinationLAGFDKYKYSAVDTN
HCCCCCCCCCCCCCC
38.17-
31PhosphorylationDTNPLSLYVMHPFWN
CCCCCEEEEECHHHH
7.73-
247UbiquitinationLNFFRSYKNNTLKLN
HHHHHHHCCCCEEEC
44.9927667366

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPT1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EPT1_HUMAN !!

Drug and Disease Associations
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.
Regulatory Network of EPT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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