EF3_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EF3_SCHPO
• UniProt AC: O94489
• Protein Name: Elongation factor 3
• Gene Name: tef3
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1047
• Protein Description: The main role of EF-3 may be to transduce nucleoside triphosphate energy into mechanical energy for translocation during translation. EF-3 stimulates EF-1-alpha-dependent binding of aminoacyl-tRNA to the ribosome..
• Protein Sequence: MSAKSENKQSVKALEELLKHLTVCDAAEEADAAKALASFVNGPIEEQDAPSQVFSAISKQLNDKNATARERVLKGLEAVANHGSVAADVEPYLVELLPAVIAKVADKQNAVRDAAIAASKAIVRCTTPYAVKAIVPSVLESIHTTGKWNEKMNSLQLLDVLVEVAPSQLSYSLPQIIPVVSESMWDTKAEVKKQSKETMTKVCTLIANADIDRFIPELINCIAHPEEVPETIHSLGATTFVTEVQAPTLSIMVPLLARGLNERSTPIKRKTAVIIDNMSKLVEDPQVVAPFLPKLLPGLYHIKDTIGDPECRSVVQRAITTLERVGNVVDGKIPEVSTAANPEVCLETLKAVLGEIKVPTNEEVIAKYVANIAAQLVEEKDNENESWVLNITPYLTAFIDEAHIHKIVEQLRTRSIAKIPGGASHAEEEEEGEDLCNCEFSLAYGAKILLNRTRLRLKRGRRYGLCGPNGSGKSTLMRAIVNGQVEGFPTHLRTVYVEHDIDESEADTPSVDFILQDPAVPIKDRDEIVKALKENSFTDELINMPIGSLSGGWKMKLALTRAMFKNPDILLLDEPTNHLDVVNVAWLENFLVNQKDVSSIIVSHDSGFLDHVVQAIIHYERFKLRKYLGNMSEFVKKVPSAKSYYELGASEMEFKFPEPGFLEGVKTKQRAIIKVQHMSFQYPGTSKPQLNDISFQVSLSSRIAVIGPNGAGKSTLIKVLTGELLPTVGEIYQHENCRIAYVAQAAFTHLGHHPDKTPSEYIQWRFQSGEDLEAMDKASRVISEADEEAMKNKIFKIEGTQRKILGIHSRRKLKNSYEYECSFLVGENIGMKSERWVPMMSSDNAWLPRGELMETHAKMVAEVDRAEALKSGQFRPLVRKEIEEHCSLLGLDAELVSHSRIKGLSGGQKVKLVLAACTWLRPHVIVLDEPTNYLDRDSLGALSKGLKNFGGGVVLVTHSREFTEGLTEEVWAVNNGHMTPSGHNWVSGQGSGPRIQEKEEGDTFDAFGNKIEKAKKAKKLTGAELRKKKKERMARRKAGLEVSDDEL

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
38	Phosphorylation	DAAKALASFVNGPIE HHHHHHHHHHCCCCC	30.49	25720772
55	Phosphorylation	DAPSQVFSAISKQLN CCHHHHHHHHHHHHC	26.32	25720772
424	Phosphorylation	AKIPGGASHAEEEEE CCCCCCCCCCCHHHC	26.89	27738172
471	Phosphorylation	GLCGPNGSGKSTLMR CCCCCCCCCHHHHHH	50.08	28889911
627	Phosphorylation	ERFKLRKYLGNMSEF HHHHHHHHHCCHHHH	17.26	25720772
632	Phosphorylation	RKYLGNMSEFVKKVP HHHHCCHHHHHHHCC	31.70	28889911
643	Phosphorylation	KKVPSAKSYYELGAS HHCCCCCCHHHCCCC	32.44	25720772
644	Phosphorylation	KVPSAKSYYELGASE HCCCCCCHHHCCCCC	10.55	25720772
650	Phosphorylation	SYYELGASEMEFKFP CHHHCCCCCCEEECC	35.36	21712547
714	Phosphorylation	GPNGAGKSTLIKVLT CCCCCCHHHHHHHHH	27.77	28889911
768	Phosphorylation	YIQWRFQSGEDLEAM HHHHHCCCCCCHHHH	41.25	28889911
783	Phosphorylation	DKASRVISEADEEAM HHHHHHHCHHCHHHH	24.71	28889911
809	Phosphorylation	RKILGIHSRRKLKNS HHCCCCCCCCCCCCC	31.68	25720772
822	Phosphorylation	NSYEYECSFLVGENI CCCEEEEEEEEECCC	15.07	27738172
871	Phosphorylation	DRAEALKSGQFRPLV HHHHHHHCCCCHHHH	38.38	21712547
943	Phosphorylation	RDSLGALSKGLKNFG HHHHHHHHHHHHHCC	24.92	28889911
1043	Phosphorylation	RKAGLEVSDDEL--- HHCCCCCCCCCC---	29.93	28889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EF3_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EF3_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EF3_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of EF3_SCHPO !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714; SER-768; SER-783AND SER-1043, AND MASS SPECTROMETRY.
PubMed: 18257517