EF1A4_ARATH - dbPTM
EF1A4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1A4_ARATH
UniProt AC Q8GTY0
Protein Name Elongation factor 1-alpha 4
Gene Name A4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 449
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 MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK
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
21PhosphorylationGHVDSGKSTTTGHLI
EECCCCCCCCCCCHH		34.2125561503
22PhosphorylationHVDSGKSTTTGHLIY
ECCCCCCCCCCCHHE		31.6825561503
29PhosphorylationTTTGHLIYKLGGIDK
CCCCCHHEECCCCCH		13.4022074104
55MethylationEMNKRSFKYAWVLDK
HHHHHHHHHHHHHHH		34.9921245040
79MethylationTIDIALWKFETTKYY
EEEEEEEEEECCEEE		33.8921245040
85PhosphorylationWKFETTKYYCTVIDA
EEEECCEEEEEEEEC		11.1522074104
176PhosphorylationEIIKEVSSYLKKVGY
HHHHHHHHHHHHHCC		39.3925561503
177PhosphorylationIIKEVSSYLKKVGYN
HHHHHHHHHHHHCCC		18.2925561503
183PhosphorylationSYLKKVGYNPDKIPF
HHHHHHCCCCCCCCE		26.8925368622
187MethylationKVGYNPDKIPFVPIS
HHCCCCCCCCEEECC		54.2421245040
194PhosphorylationKIPFVPISGFEGDNM
CCCEEECCCCCCCCC		31.2125368622
261MethylationRVETGMIKPGMVVTF
EEECCCCCCCEEEEE		26.9921245040
267PhosphorylationIKPGMVVTFAPTGLT
CCCCEEEEECCCCCC		11.5824299221
279PhosphorylationGLTTEVKSVEMHHES
CCCCEEEEEEEHHHH		28.6129797451
286PhosphorylationSVEMHHESLLEALPG
EEEEHHHHHHHHCCC		33.6229797451
306MethylationNVKNVAVKDLKRGYV
EEEEEEHHHHCCCEE		47.8321245040
312PhosphorylationVKDLKRGYVASNSKD
HHHHCCCEECCCCCC		9.2524299221
393PhosphorylationDAGMVKMTPTKPMVV
CCCCCCCCCCCCEEE		23.3023776212
395PhosphorylationGMVKMTPTKPMVVET
CCCCCCCCCCEEEEE		38.3223776212
396MethylationMVKMTPTKPMVVETF
CCCCCCCCCEEEEEC		32.1121245040
402PhosphorylationTKPMVVETFSEYPPL
CCCEEEEECCCCCCC		22.3523776212
420PhosphorylationAVRDMRQTVAVGVIK
HHCCHHHHEEEEEEE		10.4823111157
428PhosphorylationVAVGVIKSVDKKDPT
EEEEEEEECCCCCCC		25.1523111157
438UbiquitinationKKDPTGAKVTKAAVK
CCCCCCCCHHHHHHH		52.3519292762
440PhosphorylationDPTGAKVTKAAVKKG
CCCCCCHHHHHHHHC		17.7925561503
441UbiquitinationPTGAKVTKAAVKKGA
CCCCCHHHHHHHHCC		37.0219292762
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 EF1A4_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
396KMethylation

21245040
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 EF1A4_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO3_ARATHSUMO3physical
20855607
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1A4_ARATH

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Tandem affinity purification and mass spectrometric analysis ofubiquitylated proteins in Arabidopsis.";
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M.,Vierstra R.D.;
Plant J. 59:344-358(2009).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-438 AND LYS-441, ANDIDENTIFICATION BY MASS SPECTROMETRY.

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