EF1A_CAEEL - dbPTM
EF1A_CAEEL - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1A_CAEEL
UniProt AC P53013
Protein Name Elongation factor 1-alpha
Gene Name eft-3
Organism Caenorhabditis elegans.
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 MGKEKVHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAQEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETAKYYITIIDAPGHRDFIKNMITGTSQADCAVLVVACGTGEFEAGISKNGQTREHALLAQTLGVKQLIVACNKMDSTEPPFSEARFTEITNEVSGFIKKIGYNPKAVPFVPISGFNGDNMLEVSSNMPWFKGWAVERKEGNASGKTLLEALDSIIPPQRPTDRPLRLPLQDVYKIGGIGTVPVGRVETGIIKPGMVVTFAPQNVTTEVKSVEMHHESLPEAVPGDNVGFNVKNVSVKDIRRGSVCSDSKQDPAKEARTFHAQVIIMNHPGQISNGYTPVLDCHTAHIACKFNELKEKVDRRTGKKVEDFPKFLKSGDAGIVELIPTKPLCVESFTDYAPLGRFAVRDMRQTVAVGVIKSVEKSDGSSGKVTKSAQKAAPKKK
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
29PhosphorylationTTTGHLIYKCGGIDK
CCCCEEEEECCCCCH		13.4427067626
142PhosphorylationEHALLAQTLGVKQLI
HHHHHHHHHCCHHHH		21.6328854356
157PhosphorylationVACNKMDSTEPPFSE
HHHCCCCCCCCCCCH		31.0430078680
158PhosphorylationACNKMDSTEPPFSEA
HHCCCCCCCCCCCHH		48.5230078680
163PhosphorylationDSTEPPFSEARFTEI
CCCCCCCCHHHHHHH		35.8030078680
175PhosphorylationTEITNEVSGFIKKIG
HHHHHHHHHHHHHHC		23.0830078680
254PhosphorylationRLPLQDVYKIGGIGT
CCCHHHEEEECCCEE		12.7427067626
261PhosphorylationYKIGGIGTVPVGRVE
EEECCCEEEECCEEE		21.5128854356
269PhosphorylationVPVGRVETGIIKPGM
EECCEEECCCCCCCE		30.7230078680
284N-linked_GlycosylationVVTFAPQNVTTEVKS
EEEECCCCCEEEEEE		31.8517761667
286PhosphorylationTFAPQNVTTEVKSVE
EECCCCCEEEEEEEE		25.4519530675
287PhosphorylationFAPQNVTTEVKSVEM
ECCCCCEEEEEEEEE		34.2019530675
3015-glutamyl glycerylphosphorylethanolamineMHHESLPEAVPGDNV
ECHHCCCCCCCCCCC		68.54-
301Formation of an isopeptide bondMHHESLPEAVPGDNV
ECHHCCCCCCCCCCC		68.54-
324PhosphorylationVKDIRRGSVCSDSKQ
HHHHCCCCCCCCCCC		20.3822923814
357PhosphorylationPGQISNGYTPVLDCH
CCCCCCCEECCHHCC		16.4827067626
3745-glutamyl glycerylphosphorylethanolamineHIACKFNELKEKVDR
HHHHHHHHHHHHHHH		65.44-
374Formation of an isopeptide bondHIACKFNELKEKVDR
HHHHHHHHHHHHHHH		65.44-
396PhosphorylationDFPKFLKSGDAGIVE
HHHHHHHCCCCCEEE		44.0130078680
418PhosphorylationCVESFTDYAPLGRFA
EEEECCCCCCCCHHH		13.6827067626
432PhosphorylationAVRDMRQTVAVGVIK
HHHCHHHHEEEEEEE		10.4828854356
440PhosphorylationVAVGVIKSVEKSDGS
EEEEEEEEEECCCCC		25.1219530675
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 EF1A_CAEEL !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1A_CAEEL !!
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 EF1A_CAEEL !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EF1A_CAEEL !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1A_CAEEL

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Related Literatures of Post-Translational Modification

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