EF1A1_DROME - dbPTM
EF1A1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1A1_DROME
UniProt AC P08736
Protein Name Elongation factor 1-alpha 1 {ECO:0000312|FlyBase:FBgn0284245}
Gene Name eEF1alpha1 {ECO:0000312|FlyBase:FBgn0284245}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 463
Subcellular Localization Cytoplasm.
Protein Description This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis..
Protein Sequence MGKEKIHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGTGEFEAGISKNGQTREHALLAFTLGVKQLIVGVNKMDSSEPPYSEARYEEIKKEVSSYIKKIGYNPAAVAFVPISGWHGDNMLEPSTNMPWFKGWKVERKEGNADGKTLIDALDAILPPARPTDKALRLPLQDVYKIGGIGTVPVGRVETGVLKPGTVVVFAPANITTEVKSVEMHHEALQEAVPGDNVGFNVKNVSVKELRRGYVAGDSKANPPKGAADFTAQVIVLNHPGQIANGYTPVLDCHTAHIACKFAEIKEKVDRRSGKTTEENPKFIKSGDAAIVNLVPSKPLCVEAFQEFPPLGRFAVRDMRQTVAVGVIKAVNFKDASGGKVTKAAEKATKGKK
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
23PhosphorylationVDSGKSTTTGHLIYK
CCCCCCCCCCEEEEE
37.5627794539
29PhosphorylationTTTGHLIYKCGGIDK
CCCCEEEEECCCCCH
13.4419429919
30AcetylationTTGHLIYKCGGIDKR
CCCEEEEECCCCCHH
21.2919608861
41AcetylationIDKRTIEKFEKEAQE
CCHHHHHHHHHHHHH
55.7819608861
44AcetylationRTIEKFEKEAQEMGK
HHHHHHHHHHHHCCC
62.5719608861
55AcetylationEMGKGSFKYAWVLDK
HCCCCCHHHHHHHHH
35.4419608861
172AcetylationARYEEIKKEVSSYIK
HHHHHHHHHHHHHHH
69.8419608861
255AcetylationLPLQDVYKIGGIGTV
CCHHHEEEECCCEEE
34.4219608861
269PhosphorylationVPVGRVETGVLKPGT
EECCEEECCCCCCCE
29.7221082442
276PhosphorylationTGVLKPGTVVVFAPA
CCCCCCCEEEEEECC
20.7521082442
286PhosphorylationVFAPANITTEVKSVE
EEECCCCCCEEEEEH
19.4021082442
3015-glutamyl glycerylphosphorylethanolamineMHHEALQEAVPGDNV
HHHHHHHHHCCCCCC
53.11-
301Formation of an isopeptide bondMHHEALQEAVPGDNV
HHHHHHHHHCCCCCC
53.118500545
330AcetylationGYVAGDSKANPPKGA
CCCCCCCCCCCCCCC
57.8521791702
3745-glutamyl glycerylphosphorylethanolamineHIACKFAEIKEKVDR
HHHHHHHHHHHHHHH
58.70-
374Formation of an isopeptide bondHIACKFAEIKEKVDR
HHHHHHHHHHHHHHH
58.70-
383PhosphorylationKEKVDRRSGKTTEEN
HHHHHHCCCCCCCCC
45.6025749252
386PhosphorylationVDRRSGKTTEENPKF
HHHCCCCCCCCCCCE
42.8621082442
392AcetylationKTTEENPKFIKSGDA
CCCCCCCCEEECCCE
71.8921791702
395AcetylationEENPKFIKSGDAAIV
CCCCCEEECCCEEEE
52.0621791702
432PhosphorylationAVRDMRQTVAVGVIK
HHHCHHHHHEEEEEE
10.4818511481
439UbiquitinationTVAVGVIKAVNFKDA
HHEEEEEEECCCCCC
43.8231113955
444AcetylationVIKAVNFKDASGGKV
EEEECCCCCCCCCCC
47.3721791702
447PhosphorylationAVNFKDASGGKVTKA
ECCCCCCCCCCCCHH
59.2027626673

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 EF1A1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1A1_DROME !!

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 EF1A1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F206_DROMECG9288physical
14605208

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1A1_DROME

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Related Literatures of Post-Translational Modification

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