dbPTM

EF2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF2_RAT
UniProt AC	P05197
Protein Name	Elongation factor 2
Gene Name	Eef2
Organism	Rattus norvegicus (Rat).
Sequence Length	858
Subcellular Localization	Cytoplasm . Nucleus . Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.
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..
Protein Sequence	MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGAAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDAIMNFRKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKARARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Acetylation	QIRAIMDKKANIRNM HHHHHHHHCCCCCCE	36.08	22902405
38	Phosphorylation	GKSTLTDSLVCKAGI CCCCCCHHHHHHHHH	19.91	23984901
42	Acetylation	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	22902405
48	Phosphorylation	CKAGIIASARAGETR HHHHHHHHCCCCCCC	14.10	30181290
54	Phosphorylation	ASARAGETRFTDTRK HHCCCCCCCCCCCCH	30.11	29779826
57	Phosphorylation	RAGETRFTDTRKDEQ CCCCCCCCCCCHHHH	32.92	23984901
59	Phosphorylation	GETRFTDTRKDEQER CCCCCCCCCHHHHHH	36.24	29779826
152	Acetylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	22902405
152	Succinylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	26843850
152	Succinylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	-
159	Acetylation	KPVLMMNKMDRALLE HHHHCCCHHHHHHHH	25.04	22902405
235	Acetylation	FAEMYVAKFAAKGEG HHHHHHHHHHHCCCC	26.03	-
239	Acetylation	YVAKFAAKGEGQLGA HHHHHHHCCCCCCCH	54.81	-
239	Ubiquitination	YVAKFAAKGEGQLGA HHHHHHHCCCCCCCH	54.81	-
251	Acetylation	LGAAERAKKVEDMMK CCHHHHHHHHHHHHH	64.67	22902405
252	Acetylation	GAAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	22902405
258	Acetylation	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	22902405
259	Acetylation	KVEDMMKKLWGDRYF HHHHHHHHHHCCCCC	31.41	22902405
265	Phosphorylation	KKLWGDRYFDPANGK HHHHCCCCCCCCCCC	19.64	-
272	Succinylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	-
272	Succinylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	-
272	Ubiquitination	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	-
272	Acetylation	YFDPANGKFSKSANS CCCCCCCCCCCCCCC	46.39	25786129
275	Acetylation	PANGKFSKSANSPDG CCCCCCCCCCCCCCC	57.64	22902405
279	Phosphorylation	KFSKSANSPDGKKLP CCCCCCCCCCCCCCC	24.88	25403869
314	Acetylation	FRKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	22902405
318	Acetylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	22902405
322	Acetylation	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	22902405
325	Phosphorylation	KLDIKLDSEDKDKEG HCCCCCCCCCCCCCC	59.12	22673903
328	Acetylation	IKLDSEDKDKEGKPL CCCCCCCCCCCCHHH	67.65	22902405
337	Acetylation	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	22902405
373	Phosphorylation	KYRCELLYEGPPDDE CEEEEEEECCCCCCH	31.31	-
426	Acetylation	GVVSTGLKVRIMGPN CCCCCCCEEEEECCC	30.71	22902405
434	Phosphorylation	VRIMGPNYTPGKKED EEEECCCCCCCCHHH	19.90	23984901
435	Phosphorylation	RIMGPNYTPGKKEDL EEECCCCCCCCHHHC	32.00	27097102
439	Acetylation	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	-
445	Succinylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	26843850
445	Acetylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	22902405
498	Acetylation	AHNMRVMKFSVSPVV CCCCEEEEEEECCEE	31.46	22902405
500	Phosphorylation	NMRVMKFSVSPVVRV CCEEEEEEECCEEEE	19.03	23984901
502	Phosphorylation	RVMKFSVSPVVRVAV EEEEEEECCEEEEEE	15.69	25403869
512	Acetylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	22902405
512	Ubiquitination	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	-
525	Methylation	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	-
525	"N6,N6,N6-trimethyllysine"	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	-
571	Succinylation	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	26843850
572	Succinylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
572	Succinylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
595	Phosphorylation	NVLCLSKSPNKHNRL CEEEEECCCCCCCCE	30.26	-
619	Acetylation	GLAEDIDKGEVSARQ CCHHCCCCCCCCHHH	58.25	-
715	Diphthamide	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	-
715	Amidation	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	4368673
845	Acetylation	TRKRKGLKEGIPALD HHHHCCHHHCCHHHH	63.66	22902405
857	Succinylation	ALDNFLDKL------ HHHHHHHHC------	59.24	26843850

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
57	T	Phosphorylation	Kinase	EEF2K	P70531	Uniprot
265	Y	Phosphorylation	Kinase	CSK	P32577	Uniprot
373	Y	Phosphorylation	Kinase	CSK	P32577	Uniprot
595	S	Phosphorylation	Kinase	CDK2	Q63699	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
595	S	Phosphorylation		-
Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase.

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 EF2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EF2_RAT !!

Drug and Disease Associations

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

Regulatory Network of EF2_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57 AND THR-59, AND MASSSPECTROMETRY.	16396499 [Abstract]

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