EF1A2_ARATH - dbPTM
EF1A2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1A2_ARATH
UniProt AC Q8W4H7
Protein Name Elongation factor 1-alpha 2
Gene Name A2
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
34.99-
79MethylationTIDIALWKFETTKYY
EEEEEEEEEECCEEE
33.89-
85PhosphorylationWKFETTKYYCTVIDA
EEEECCEEEEEEEEC
11.1522074104
176PhosphorylationEIIKEVSSYLKKVGY
HHHHHHHHHHHHHCC
39.3925561503
177PhosphorylationIIKEVSSYLKKVGYN
HHHHHHHHHHHHCCC
18.2925561503
183PhosphorylationSYLKKVGYNPDKIPF
HHHHHHCCCCCCCCE
26.8925368622
187MethylationKVGYNPDKIPFVPIS
HHCCCCCCCCEEECC
54.24-
194PhosphorylationKIPFVPISGFEGDNM
CCCEEECCCCCCCCC
31.2125368622
261MethylationRVETGMIKPGMVVTF
EEECCCCCCCEEEEE
26.99-
267PhosphorylationIKPGMVVTFAPTGLT
CCCCEEEEECCCCCC
11.5824299221
279PhosphorylationGLTTEVKSVEMHHES
CCCCEEEEEEEHHHH
28.6129797451
286PhosphorylationSVEMHHESLLEALPG
EEEEHHHHHHHHCCC
33.6229797451
306MethylationNVKNVAVKDLKRGYV
EEEEEEHHHHCCCEE
47.83-
312PhosphorylationVKDLKRGYVASNSKD
HHHHCCCEECCCCCC
9.2524299221
393PhosphorylationDAGMVKMTPTKPMVV
CCCCCCCCCCCCEEE
23.3023776212
395PhosphorylationGMVKMTPTKPMVVET
CCCCCCCCCCEEEEE
38.3223776212
396MethylationMVKMTPTKPMVVETF
CCCCCCCCCEEEEEC
32.11-
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 EF1A2_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1A2_ARATH !!

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 EF1A2_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 EF1A2_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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