EKI1_HUMAN - dbPTM
EKI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
34PhosphorylationVQTRIGNSAASRRSP
HHHHHCCCHHHCCCC
21.7223532336
37PhosphorylationRIGNSAASRRSPAAR
HHCCCHHHCCCCCCC
28.1323532336
40PhosphorylationNSAASRRSPAARPPV
CCHHHCCCCCCCCCC
20.1328555341
100PhosphorylationYIHVPPGSPEVPKLN
CCCCCCCCCCCCCCE
24.5422199227
172UbiquitinationLVRIYGNKTELLVDR
EEEEECCCEEEEECC
38.7321890473
179MethylationKTELLVDRDEEVKSF
CEEEEECCCHHHHHH
45.84-
184AcetylationVDRDEEVKSFRVLQA
ECCCHHHHHHHHHHH
47.3525953088
184UbiquitinationVDRDEEVKSFRVLQA
ECCCHHHHHHHHHHH
47.3521906983
255UbiquitinationPKSNLWLKMGKYFSL
CCCCEEEECCCEEEE
33.7421906983
258AcetylationNLWLKMGKYFSLIPT
CEEEECCCEEEECCC
39.3625953088
258UbiquitinationNLWLKMGKYFSLIPT
CEEEECCCEEEECCC
39.36-
274UbiquitinationFADEDINKRFLSDIP
CCCHHHHHHHHHCCC
44.8821906983
314UbiquitinationCHNDLLCKNIIYNEK
ECCCEEHHHCCEECC
51.67-
321UbiquitinationKNIIYNEKQGDVQFI
HHCCEECCCCCEEEE
56.81-
360PhosphorylationSDVDYSLYPDRELQS
CCCCCCCCCCHHHHH
9.3527196784
378UbiquitinationRAYLEAYKEFKGFGT
HHHHHHHHHHCCCCC
64.8221906983
381UbiquitinationLEAYKEFKGFGTEVT
HHHHHHHCCCCCCCC
55.19-
446PhosphorylationFKMKPEVTALKVPE-
CCCCCCCEEEECCC-
25.3028857561
449AcetylationKPEVTALKVPE----
CCCCEEEECCC----
53.9619608861
449UbiquitinationKPEVTALKVPE----
CCCCEEEECCC----
53.9619608861

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 EKI1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EKI1_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 EKI1_HUMAN !!

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

Oops, there are no PPI records of EKI1_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 EKI1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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