EF2_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EF2_DROME
• UniProt AC: P13060
• Protein Name: Elongation factor 2
• Gene Name: EF2
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 844
• Subcellular Localization: Cytoplasm.
• Protein Description: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity)..
• Protein Sequence: MVNFTVDEIRGLMDKKRNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAGAKAGETRFTDTRKDEQERCITIKSTAISMYFEVEEKDLVFITHPDQREKECKGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPILFMNKMDRALLELQLDAEELYQTFQRIVENVNVIIATYNDDGGPMGEVRVDPSKGSVGFGSGLHGWAFTLKQFSEMYSEKFKIDVVKLMNRLWGENFFNAKTKKWQKQKEADNKRSFCMYILDPIYKVFDAIMNYKKEEIGTLLEKIGVTLKHEDKDKDGKALLKTVMRTWLPAGEALLQMIAIHLPSPVVAQKYRMEMLYEGPHDDEAAIAVKSCDPDGPLMMYISKMVPTSDKGRFYAFGRVFAGKVATGQKCRIMGPNYTPGKKEDLYEKAIQRTILMMGRYVEAIEDVPSGNICGLVGVDQFLVKTGTITTFKDAHNMKVMKFSVSPVVRVAVEPKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPLKKSDPVVSYRETVSEESDQMCLSKSPNKHNRLLMKALPMPDGLPEDIDNGDVSAKDEFKARARYLSEKYDYDVTEARKIWCFGPDGTGPNFILDCTKSVQYLNEIKDSVVAGFQWASKEGILADENLRGVRFNIYDVTLHADAIHRGGGQIIPTTRRCLYAAAITAKPRLMEPVYLCEIQCPEVAVGGIYGVLNRRRGHVFEENQVVGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQVLPGDPSEPSSKPYAIVQDTRKRKGLKEGLPDLSQYLDKL

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
57	Phosphorylation	KAGETRFTDTRKDEQ CCCCCCCCCCCHHHH	32.92	18511481
59	Phosphorylation	GETRFTDTRKDEQER CCCCCCCCCHHHHHH	36.24	-
238	Acetylation	FSEMYSEKFKIDVVK HHHHHHHCCCHHHHH	46.12	21791702
245	Acetylation	KFKIDVVKLMNRLWG CCCHHHHHHHHHHHC	41.70	21791702
245	Ubiquitination	KFKIDVVKLMNRLWG CCCHHHHHHHHHHHC	41.70	31113955
259	Acetylation	GENFFNAKTKKWQKQ CCCCCCCCCHHHHHH	63.08	21791702
310	Acetylation	EKIGVTLKHEDKDKD HHHCCEEEECCCCCC	35.27	21791702
323	Acetylation	KDGKALLKTVMRTWL CCHHHHHHHHHHHHC	39.67	21791702
421	Phosphorylation	RIMGPNYTPGKKEDL EEECCCCCCCCHHHH	32.00	21082442
431	Acetylation	KKEDLYEKAIQRTIL CHHHHHHHHHHHHHH	36.91	21791702
475	Acetylation	TGTITTFKDAHNMKV CCCEEEEECCCCCEE	52.49	21791702
486	Phosphorylation	NMKVMKFSVSPVVRV CCEEEEEEECCEEEE	19.03	21082442
488	Phosphorylation	KVMKFSVSPVVRVAV EEEEEEECCEEEEEE	15.69	19429919
498	Acetylation	VRVAVEPKNPADLPK EEEEECCCCHHHHHH	63.16	21791702
624	Acetylation	RARYLSEKYDYDVTE HHHHHHHHCCCCCCC	39.79	21791702
654	Phosphorylation	FILDCTKSVQYLNEI CEEECHHHHHHHHHH	9.04	19429919
701	Diphthamide	TLHADAIHRGGGQII EEECHHEECCCCCEE	24.85	-
701	Amidation	TLHADAIHRGGGQII EEECHHEECCCCCEE	24.85	-

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

Oops, there are no upstream regulatory protein records of EF2_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EF2_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EF2_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNAS_DROME	Galphas	physical	14605208
ESCA_DROME	esg	physical	14605208
CYPR_DROME	ninaA	physical	14605208
NHP2_DROME	NHP2	physical	14605208
SMD3_DROME	SmD3	physical	14605208
SXL_DROME	Sxl	physical	14605208
HMX_DROME	Hmx	physical	14605208
CALR_DROME	Crc	physical	22036573
NLP_DROME	Nlp	physical	22036573
SH3BG_DROME	Sh3beta	physical	22036573
INO1_DROME	Inos	physical	22036573
MOEH_DROME	Moe	physical	22036573
ENO_DROME	Eno	physical	22036573
NACA_DROME	Nacalpha	physical	22036573

Drug and Disease Associations

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