dbPTM

EF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF2_HUMAN
UniProt AC	P13639
Protein Name	Elongation factor 2
Gene Name	EEF2
Organism	Homo sapiens (Human).
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	MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MVNFTVDQ -------CCCCCHHH	5.12	21406390
10	Methylation	NFTVDQIRAIMDKKA CCCHHHHHHHHHHCC	16.66	-
15	Ubiquitination	QIRAIMDKKANIRNM HHHHHHHHCCCCCCE	36.08	-
22	Sulfoxidation	KKANIRNMSVIAHVD HCCCCCCEEEEEEEC	2.13	21406390
23	Phosphorylation	KANIRNMSVIAHVDH CCCCCCEEEEEEECC	17.58	20873877
32	Ubiquitination	IAHVDHGKSTLTDSL EEEECCCCCCCCHHH	36.53	-
32	Acetylation	IAHVDHGKSTLTDSL EEEECCCCCCCCHHH	36.53	26051181
33	Phosphorylation	AHVDHGKSTLTDSLV EEECCCCCCCCHHHH	32.99	21712546
34	Phosphorylation	HVDHGKSTLTDSLVC EECCCCCCCCHHHHH	36.84	21712546
36	Phosphorylation	DHGKSTLTDSLVCKA CCCCCCCCHHHHHHH	24.51	21712546
38	Phosphorylation	GKSTLTDSLVCKAGI CCCCCCHHHHHHHHH	19.91	25159151
41	S-nitrosocysteine	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	-
41	Glutathionylation	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	22555962
41	S-nitrosylation	TLTDSLVCKAGIIAS CCCHHHHHHHHHHHH	2.79	2212679
42	Acetylation	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	23954790
42	Ubiquitination	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	21890473
42	2-Hydroxyisobutyrylation	LTDSLVCKAGIIASA CCHHHHHHHHHHHHC	42.01	-
48	Phosphorylation	CKAGIIASARAGETR HHHHHHHHCCCCCCC	14.10	30266825
50	Methylation	AGIIASARAGETRFT HHHHHHCCCCCCCCC	40.40	-
54	Phosphorylation	ASARAGETRFTDTRK HHCCCCCCCCCCCCH	30.11	25159151
57	Phosphorylation	RAGETRFTDTRKDEQ CCCCCCCCCCCHHHH	32.92	22167270
57	Dephosphorylation	RAGETRFTDTRKDEQ CCCCCCCCCCCHHHH	32.92	8386634
59	Phosphorylation	GETRFTDTRKDEQER CCCCCCCCCHHHHHH	36.24	29255136
59	Dephosphorylation	GETRFTDTRKDEQER CCCCCCCCCHHHHHH	36.24	8386634
61	Succinylation	TRFTDTRKDEQERCI CCCCCCCHHHHHHEE	68.65	23954790
67	S-nitrosocysteine	RKDEQERCITIKSTA CHHHHHHEEEEEHHH	2.95	-
67	S-nitrosylation	RKDEQERCITIKSTA CHHHHHHEEEEEHHH	2.95	19483679
72	Phosphorylation	ERCITIKSTAISLFY HHEEEEEHHHHHHHH	21.15	-
73	Phosphorylation	RCITIKSTAISLFYE HEEEEEHHHHHHHHH	24.02	-
76	Phosphorylation	TIKSTAISLFYELSE EEEHHHHHHHHHCCC	15.23	-
79	Phosphorylation	STAISLFYELSENDL HHHHHHHHHCCCCCH	22.66	-
82	Phosphorylation	ISLFYELSENDLNFI HHHHHHCCCCCHHHH	23.55	28348404
90	Ubiquitination	ENDLNFIKQSKDGAG CCCHHHHHHCCCCCC	44.36	21906983
92	Phosphorylation	DLNFIKQSKDGAGFL CHHHHHHCCCCCCEE	27.93	28348404
93	Ubiquitination	LNFIKQSKDGAGFLI HHHHHHCCCCCCEEE	58.65	-
152	Succinylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	-
152	Ubiquitination	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	-
152	Succinylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	21906983
152	Acetylation	QAIAERIKPVLMMNK HHHHHHHHHHHCCCH	34.98	26051181
159	Ubiquitination	KPVLMMNKMDRALLE HHHHCCCHHHHHHHH	25.04	21906983
159	Acetylation	KPVLMMNKMDRALLE HHHHCCCHHHHHHHH	25.04	25953088
175	Phosphorylation	QLEPEELYQTFQRIV CCCHHHHHHHHHHHH	14.58	-
177	Phosphorylation	EPEELYQTFQRIVEN CHHHHHHHHHHHHHH	14.26	21712546
197	Phosphorylation	STYGEGESGPMGNIM EECCCCCCCCCCCEE	60.08	-
231	Sulfoxidation	TLKQFAEMYVAKFAA HHHHHHHHHHHHHHH	2.67	28465586
235	Acetylation	FAEMYVAKFAAKGEG HHHHHHHHHHHCCCC	26.03	19608861
235	Ubiquitination	FAEMYVAKFAAKGEG HHHHHHHHHHHCCCC	26.03	21890473
235	Malonylation	FAEMYVAKFAAKGEG HHHHHHHHHHHCCCC	26.03	26320211
239	Acetylation	YVAKFAAKGEGQLGP HHHHHHHCCCCCCCH	54.81	19608861
239	Ubiquitination	YVAKFAAKGEGQLGP HHHHHHHCCCCCCCH	54.81	20639865
239	Sumoylation	YVAKFAAKGEGQLGP HHHHHHHCCCCCCCH	54.81	19608861
239	2-Hydroxyisobutyrylation	YVAKFAAKGEGQLGP HHHHHHHCCCCCCCH	54.81	-
239	Malonylation	YVAKFAAKGEGQLGP HHHHHHHCCCCCCCH	54.81	26320211
251	Ubiquitination	LGPAERAKKVEDMMK CCHHHHHHHHHHHHH	64.67	-
251	Malonylation	LGPAERAKKVEDMMK CCHHHHHHHHHHHHH	64.67	26320211
252	Acetylation	GPAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	23749302
252	Ubiquitination	GPAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	-
252	2-Hydroxyisobutyrylation	GPAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	-
252	Malonylation	GPAERAKKVEDMMKK CHHHHHHHHHHHHHH	50.28	26320211
256	Sulfoxidation	RAKKVEDMMKKLWGD HHHHHHHHHHHHHCC	2.41	30846556
257	Sulfoxidation	AKKVEDMMKKLWGDR HHHHHHHHHHHHCCC	5.53	30846556
258	Acetylation	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	23749302
258	Ubiquitination	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	-
258	2-Hydroxyisobutyrylation	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	-
258	Succinylation	KKVEDMMKKLWGDRY HHHHHHHHHHHCCCC	37.77	23954790
259	Ubiquitination	KVEDMMKKLWGDRYF HHHHHHHHHHCCCCC	31.41	-
259	Acetylation	KVEDMMKKLWGDRYF HHHHHHHHHHCCCCC	31.41	26051181
264	Methylation	MKKLWGDRYFDPANG HHHHHCCCCCCCCCC	30.04	-
265	Phosphorylation	KKLWGDRYFDPANGK HHHHCCCCCCCCCCC	19.64	28152594
272	Methylation	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	19608861
272	Acetylation	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	19608861
272	Succinylation	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	-
272	Ubiquitination	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	21890473
272	2-Hydroxyisobutyrylation	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	-
272	Malonylation	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	26320211
272	Succinylation	YFDPANGKFSKSATS CCCCCCCCCCCCCCC	46.39	-
274	Phosphorylation	DPANGKFSKSATSPE CCCCCCCCCCCCCCC	29.23	28348404
275	Acetylation	PANGKFSKSATSPEG CCCCCCCCCCCCCCC	47.44	19608861
275	Ubiquitination	PANGKFSKSATSPEG CCCCCCCCCCCCCCC	47.44	19608861
275	2-Hydroxyisobutyrylation	PANGKFSKSATSPEG CCCCCCCCCCCCCCC	47.44	-
275	Malonylation	PANGKFSKSATSPEG CCCCCCCCCCCCCCC	47.44	26320211
276	Phosphorylation	ANGKFSKSATSPEGK CCCCCCCCCCCCCCC	35.26	28985074
278	Phosphorylation	GKFSKSATSPEGKKL CCCCCCCCCCCCCCC	52.48	28176443
279	Phosphorylation	KFSKSATSPEGKKLP CCCCCCCCCCCCCCC	22.22	29496963
283	Ubiquitination	SATSPEGKKLPRTFC CCCCCCCCCCCHHHH	49.85	-
283	2-Hydroxyisobutyrylation	SATSPEGKKLPRTFC CCCCCCCCCCCHHHH	49.85	-
283	Succinylation	SATSPEGKKLPRTFC CCCCCCCCCCCHHHH	49.85	23954790
284	Ubiquitination	ATSPEGKKLPRTFCQ CCCCCCCCCCHHHHH	74.67	-
288	Phosphorylation	EGKKLPRTFCQLILD CCCCCCHHHHHHHHH	27.16	21712546
290	S-nitrosocysteine	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	-
290	Glutathionylation	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	22555962
290	S-nitrosylation	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	19483679
290	S-palmitoylation	KKLPRTFCQLILDPI CCCCHHHHHHHHHHH	2.96	29575903
305	Sulfoxidation	FKVFDAIMNFKKEET HHHHHHHHCCCHHHH	5.31	21406390
308	Acetylation	FDAIMNFKKEETAKL HHHHHCCCHHHHHHH	55.03	23954790
308	Ubiquitination	FDAIMNFKKEETAKL HHHHHCCCHHHHHHH	55.03	21890473
308	2-Hydroxyisobutyrylation	FDAIMNFKKEETAKL HHHHHCCCHHHHHHH	55.03	-
309	Ubiquitination	DAIMNFKKEETAKLI HHHHCCCHHHHHHHH	57.56	-
314	Acetylation	FKKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	23749302
314	Ubiquitination	FKKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	21906983
314	2-Hydroxyisobutyrylation	FKKEETAKLIEKLDI CCHHHHHHHHHHCCC	58.37	-
318	Acetylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	23954790
318	Ubiquitination	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	21890473
318	2-Hydroxyisobutyrylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	-
318	Malonylation	ETAKLIEKLDIKLDS HHHHHHHHCCCCCCC	44.45	26320211
322	Acetylation	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	23954790
322	Sumoylation	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	-
322	Ubiquitination	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	21906983
322	Sumoylation	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	24648518
322	2-Hydroxyisobutyrylation	LIEKLDIKLDSEDKD HHHHCCCCCCCCCCC	46.00	-
325	Phosphorylation	KLDIKLDSEDKDKEG HCCCCCCCCCCCCCC	59.12	29214152
328	Acetylation	IKLDSEDKDKEGKPL CCCCCCCCCCCCHHH	67.65	23236377
328	Ubiquitination	IKLDSEDKDKEGKPL CCCCCCCCCCCCHHH	67.65	-
330	Ubiquitination	LDSEDKDKEGKPLLK CCCCCCCCCCHHHHH	74.28	-
330	2-Hydroxyisobutyrylation	LDSEDKDKEGKPLLK CCCCCCCCCCHHHHH	74.28	-
330	Acetylation	LDSEDKDKEGKPLLK CCCCCCCCCCHHHHH	74.28	26051181
333	Ubiquitination	EDKDKEGKPLLKAVM CCCCCCCHHHHHHHH	33.32	21906983
333	Acetylation	EDKDKEGKPLLKAVM CCCCCCCHHHHHHHH	33.32	26822725
337	Acetylation	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	23954790
337	Ubiquitination	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	21890473
337	2-Hydroxyisobutyrylation	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	-
337	Malonylation	KEGKPLLKAVMRRWL CCCHHHHHHHHHHHC	46.77	26320211
353	Sulfoxidation	AGDALLQMITIHLPS HHHHHHHHHEEECCC	2.70	28183972
355	Phosphorylation	DALLQMITIHLPSPV HHHHHHHEEECCCCC	9.30	-
360	Phosphorylation	MITIHLPSPVTAQKY HHEEECCCCCCCCCE	38.06	24719451
366	Acetylation	PSPVTAQKYRCELLY CCCCCCCCEEEEEEE	32.00	30582771
366	Ubiquitination	PSPVTAQKYRCELLY CCCCCCCCEEEEEEE	32.00	-
367	Phosphorylation	SPVTAQKYRCELLYE CCCCCCCEEEEEEEC	14.39	29496907
369	S-nitrosocysteine	VTAQKYRCELLYEGP CCCCCEEEEEEECCC	3.81	-
369	Glutathionylation	VTAQKYRCELLYEGP CCCCCEEEEEEECCC	3.81	22555962
369	S-nitrosylation	VTAQKYRCELLYEGP CCCCCEEEEEEECCC	3.81	22178444
373	Phosphorylation	KYRCELLYEGPPDDE CEEEEEEECCCCCCH	31.31	24648518
383	Sulfoxidation	PPDDEAAMGIKSCDP CCCCHHHHCCCCCCC	8.00	30846556
386	Ubiquitination	DEAAMGIKSCDPKGP CHHHHCCCCCCCCCC	39.02	21906983
386	Acetylation	DEAAMGIKSCDPKGP CHHHHCCCCCCCCCC	39.02	25953088
388	Glutathionylation	AAMGIKSCDPKGPLM HHHCCCCCCCCCCEE	9.85	22555962
391	Acetylation	GIKSCDPKGPLMMYI CCCCCCCCCCEEEEE	60.97	26051181
391	Ubiquitination	GIKSCDPKGPLMMYI CCCCCCCCCCEEEEE	60.97	-
395	Sulfoxidation	CDPKGPLMMYISKMV CCCCCCEEEEEEEEE	1.84	30846556
396	Sulfoxidation	DPKGPLMMYISKMVP CCCCCEEEEEEEEEC	3.37	30846556
397	Phosphorylation	PKGPLMMYISKMVPT CCCCEEEEEEEEECC	6.51	21406692
399	Phosphorylation	GPLMMYISKMVPTSD CCEEEEEEEEECCCC	9.37	20068231
400	Ubiquitination	PLMMYISKMVPTSDK CEEEEEEEEECCCCC	34.07	21906983
400	Acetylation	PLMMYISKMVPTSDK CEEEEEEEEECCCCC	34.07	26051181
401	Sulfoxidation	LMMYISKMVPTSDKG EEEEEEEEECCCCCC	3.31	30846556
404	Phosphorylation	YISKMVPTSDKGRFY EEEEEECCCCCCCEE	37.84	-
407	Methylation	KMVPTSDKGRFYAFG EEECCCCCCCEEEEH	52.32	23748837
407	"N6,N6-dimethyllysine"	KMVPTSDKGRFYAFG EEECCCCCCCEEEEH	52.32	-
407	Acetylation	KMVPTSDKGRFYAFG EEECCCCCCCEEEEH	52.32	23749302
407	Ubiquitination	KMVPTSDKGRFYAFG EEECCCCCCCEEEEH	52.32	-
407	2-Hydroxyisobutyrylation	KMVPTSDKGRFYAFG EEECCCCCCCEEEEH	52.32	-
409	Methylation	VPTSDKGRFYAFGRV ECCCCCCCEEEEHHH	27.43	-
411	Phosphorylation	TSDKGRFYAFGRVFS CCCCCCEEEEHHHHH	10.32	28064214
418	Phosphorylation	YAFGRVFSGLVSTGL EEEHHHHHHHHHCCC	28.49	21712546
422	Phosphorylation	RVFSGLVSTGLKVRI HHHHHHHHCCCEEEE	23.07	28450419
423	Phosphorylation	VFSGLVSTGLKVRIM HHHHHHHCCCEEEEE	38.77	28450419
426	Acetylation	GLVSTGLKVRIMGPN HHHHCCCEEEEECCC	30.71	25953088
426	Ubiquitination	GLVSTGLKVRIMGPN HHHHCCCEEEEECCC	30.71	21890473
426	2-Hydroxyisobutyrylation	GLVSTGLKVRIMGPN HHHHCCCEEEEECCC	30.71	-
426	Malonylation	GLVSTGLKVRIMGPN HHHHCCCEEEEECCC	30.71	26320211
428	Methylation	VSTGLKVRIMGPNYT HHCCCEEEEECCCCC	16.16	-
430	Sulfoxidation	TGLKVRIMGPNYTPG CCCEEEEECCCCCCC	5.24	21406390
434	Phosphorylation	VRIMGPNYTPGKKED EEEECCCCCCCCHHH	19.90	22167270
434	Nitration	VRIMGPNYTPGKKED EEEECCCCCCCCHHH	19.90	-
435	Phosphorylation	RIMGPNYTPGKKEDL EEECCCCCCCCHHHC	32.00	19664994
438	Acetylation	GPNYTPGKKEDLYLK CCCCCCCCHHHCCCH	54.94	25953088
438	Ubiquitination	GPNYTPGKKEDLYLK CCCCCCCCHHHCCCH	54.94	21906983
438	2-Hydroxyisobutyrylation	GPNYTPGKKEDLYLK CCCCCCCCHHHCCCH	54.94	-
439	Acetylation	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	26051181
439	Ubiquitination	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	-
439	2-Hydroxyisobutyrylation	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	-
439	Malonylation	PNYTPGKKEDLYLKP CCCCCCCHHHCCCHH	63.48	26320211
443	Phosphorylation	PGKKEDLYLKPIQRT CCCHHHCCCHHHHHH	25.63	21945579
443	Nitration	PGKKEDLYLKPIQRT CCCHHHCCCHHHHHH	25.63	-
445	Methylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	19608861
445	Acetylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	19608861
445	Ubiquitination	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	21890473
445	2-Hydroxyisobutyrylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	-
445	Malonylation	KKEDLYLKPIQRTIL CHHHCCCHHHHHHHH	26.90	26320211
450	Phosphorylation	YLKPIQRTILMMGRY CCHHHHHHHHHHCCC	11.33	21712546
453	Sulfoxidation	PIQRTILMMGRYVEP HHHHHHHHHCCCCCC	2.06	21406390
454	Sulfoxidation	IQRTILMMGRYVEPI HHHHHHHHCCCCCCC	2.18	30846556
466	Glutathionylation	EPIEDVPCGNIVGLV CCCCCCCCCCEEEEE	7.00	22555962
481	Ubiquitination	GVDQFLVKTGTITTF EEEEEEEECCCEEEE	43.30	21906983
482	Phosphorylation	VDQFLVKTGTITTFE EEEEEEECCCEEEEE	31.88	23186163
484	Phosphorylation	QFLVKTGTITTFEHA EEEEECCCEEEEECC	22.00	28857561
486	Phosphorylation	LVKTGTITTFEHAHN EEECCCEEEEECCCC	25.85	23186163
494	Sulfoxidation	TFEHAHNMRVMKFSV EEECCCCCEEEEEEE	2.16	30846556
495	Methylation	FEHAHNMRVMKFSVS EECCCCCEEEEEEEC	30.60	-
498	Methylation	AHNMRVMKFSVSPVV CCCCEEEEEEECCEE	31.46	-
498	Acetylation	AHNMRVMKFSVSPVV CCCCEEEEEEECCEE	31.46	25825284
498	Ubiquitination	AHNMRVMKFSVSPVV CCCCEEEEEEECCEE	31.46	21906983
500	Phosphorylation	NMRVMKFSVSPVVRV CCEEEEEEECCEEEE	19.03	30266825
502	Phosphorylation	RVMKFSVSPVVRVAV EEEEEEECCEEEEEE	15.69	25159151
512	Ubiquitination	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	20972266
512	Acetylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	23236377
512	2-Hydroxyisobutyrylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	-
512	Malonylation	VRVAVEAKNPADLPK EEEEEEECCHHHHHH	50.38	26320211
519	Methylation	KNPADLPKLVEGLKR CCHHHHHHHHHHHHH	72.90	-
519	Ubiquitination	KNPADLPKLVEGLKR CCHHHHHHHHHHHHH	72.90	-
525	Methylation	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	25231979
525	"N6,N6,N6-trimethyllysine"	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	-
525	Ubiquitination	PKLVEGLKRLAKSDP HHHHHHHHHHHHCCC	57.11	21906983
526	Methylation	KLVEGLKRLAKSDPM HHHHHHHHHHHCCCC	44.94	-
529	Sumoylation	EGLKRLAKSDPMVQC HHHHHHHHCCCCEEE	61.04	-
529	Sumoylation	EGLKRLAKSDPMVQC HHHHHHHHCCCCEEE	61.04	24648518
530	Phosphorylation	GLKRLAKSDPMVQCI HHHHHHHCCCCEEEE	41.14	-
541	Phosphorylation	VQCIIEESGEHIIAG EEEEEEECCCEEEEC	36.37	-
567	S-nitrosocysteine	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	-
567	Glutathionylation	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	22555962
567	S-nitrosylation	DLEEDHACIPIKKSD HHHHCCCEEEECCCC	3.22	22178444
571	Ubiquitination	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	-
571	Malonylation	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	26320211
571	Acetylation	DHACIPIKKSDPVVS CCCEEEECCCCCCEE	40.65	25953088
572	Succinylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
572	Ubiquitination	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
572	2-Hydroxyisobutyrylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	-
572	Succinylation	HACIPIKKSDPVVSY CCEEEECCCCCCEEE	61.89	21906983
573	Phosphorylation	ACIPIKKSDPVVSYR CEEEECCCCCCEEEE	41.99	21815630
578	Phosphorylation	KKSDPVVSYRETVSE CCCCCCEEEEEECCC	20.78	21406692
579	Phosphorylation	KSDPVVSYRETVSEE CCCCCEEEEEECCCC	10.81	21406692
582	Phosphorylation	PVVSYRETVSEESNV CCEEEEEECCCCCCE	21.97	23186163
584	Phosphorylation	VSYRETVSEESNVLC EEEEEECCCCCCEEE	42.96	28450419
587	Phosphorylation	RETVSEESNVLCLSK EEECCCCCCEEEEEC	28.34	21815630
591	S-nitrosocysteine	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	-
591	Glutathionylation	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	22555962
591	S-nitrosylation	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	19483679
591	S-palmitoylation	SEESNVLCLSKSPNK CCCCCEEEEECCCCC	3.34	26865113
593	Phosphorylation	ESNVLCLSKSPNKHN CCCEEEEECCCCCCC	30.05	21815630
594	Methylation	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	23583077
594	Ubiquitination	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	21890473
594	2-Hydroxyisobutyrylation	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	-
594	Acetylation	SNVLCLSKSPNKHNR CCEEEEECCCCCCCC	57.91	25953088
595	Phosphorylation	NVLCLSKSPNKHNRL CEEEEECCCCCCCCE	30.26	21712546
598	Ubiquitination	CLSKSPNKHNRLYMK EEECCCCCCCCEEEE	45.71	-
605	Ubiquitination	KHNRLYMKARPFPDG CCCCEEEEEECCCCC	27.90	-
619	Acetylation	GLAEDIDKGEVSARQ CCCCCCCCCCCCHHH	58.25	26051181
619	Ubiquitination	GLAEDIDKGEVSARQ CCCCCCCCCCCCHHH	58.25	-
623	Phosphorylation	DIDKGEVSARQELKQ CCCCCCCCHHHHHHH	17.27	20068231
629	Ubiquitination	VSARQELKQRARYLA CCHHHHHHHHHHHHH	36.66	-
634	Phosphorylation	ELKQRARYLAEKYEW HHHHHHHHHHHHCCC	14.85	28152594
638	Methylation	RARYLAEKYEWDVAE HHHHHHHHCCCCHHH	42.75	-
638	Acetylation	RARYLAEKYEWDVAE HHHHHHHHCCCCHHH	42.75	23954790
638	Ubiquitination	RARYLAEKYEWDVAE HHHHHHHHCCCCHHH	42.75	21890473
638	2-Hydroxyisobutyrylation	RARYLAEKYEWDVAE HHHHHHHHCCCCHHH	42.75	-
639	Phosphorylation	ARYLAEKYEWDVAEA HHHHHHHCCCCHHHH	17.48	28152594
648	Acetylation	WDVAEARKIWCFGPD CCHHHHHEEEEECCC	47.83	26051181
648	Ubiquitination	WDVAEARKIWCFGPD CCHHHHHEEEEECCC	47.83	21890473
648	Malonylation	WDVAEARKIWCFGPD CCHHHHHEEEEECCC	47.83	26320211
651	S-nitrosocysteine	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	-
651	Glutathionylation	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	22555962
651	S-nitrosylation	AEARKIWCFGPDGTG HHHHEEEEECCCCCC	3.00	22178444
657	Phosphorylation	WCFGPDGTGPNILTD EEECCCCCCCCHHHH	57.77	20068231
657	O-linked_Glycosylation	WCFGPDGTGPNILTD EEECCCCCCCCHHHH	57.77	23301498
663	Phosphorylation	GTGPNILTDITKGVQ CCCCCHHHHHHHHHH	22.89	28787133
666	Phosphorylation	PNILTDITKGVQYLN CCHHHHHHHHHHHHH	25.26	20068231
667	Ubiquitination	NILTDITKGVQYLNE CHHHHHHHHHHHHHH	58.37	-
671	Phosphorylation	DITKGVQYLNEIKDS HHHHHHHHHHHHCHH	14.75	28152594
671	Nitration	DITKGVQYLNEIKDS HHHHHHHHHHHHCHH	14.75	-
676	Ubiquitination	VQYLNEIKDSVVAGF HHHHHHHCHHHEEEC	37.46	21906983
678	Phosphorylation	YLNEIKDSVVAGFQW HHHHHCHHHEEECCC	17.31	21712546
688	Acetylation	AGFQWATKEGALCEE EECCCCCCCCCCCCC	46.53	26051181
688	Ubiquitination	AGFQWATKEGALCEE EECCCCCCCCCCCCC	46.53	21906983
693	Glutathionylation	ATKEGALCEENMRGV CCCCCCCCCCCCCCC	6.46	22555962
697	Sulfoxidation	GALCEENMRGVRFDV CCCCCCCCCCCCCEE	4.45	21406390
698	Methylation	ALCEENMRGVRFDVH CCCCCCCCCCCCEEE	52.62	-
708	Phosphorylation	RFDVHDVTLHADAIH CCEEEECEEEHHHEE	20.91	28555341
715	Diphthamide	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	-
715	ADP-ribosylation	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	16901746
715	Amidation	TLHADAIHRGGGQII EEEHHHEECCCCCCC	24.85	16901746
716	Methylation	LHADAIHRGGGQIIP EEHHHEECCCCCCCC	39.06	-
724	Phosphorylation	GGGQIIPTARRCLYA CCCCCCCCHHHHHHH	23.53	20068231
726	Methylation	GQIIPTARRCLYASV CCCCCCHHHHHHHHH	32.12	-
728	S-nitrosocysteine	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	-
728	Glutathionylation	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	22555962
728	S-nitrosylation	IIPTARRCLYASVLT CCCCHHHHHHHHHHH	2.58	19483679
730	Phosphorylation	PTARRCLYASVLTAQ CCHHHHHHHHHHHCC	10.64	28152594
732	Phosphorylation	ARRCLYASVLTAQPR HHHHHHHHHHHCCCC	12.24	28152594
735	Phosphorylation	CLYASVLTAQPRLME HHHHHHHHCCCCCCC	22.53	28152594
739	Methylation	SVLTAQPRLMEPIYL HHHHCCCCCCCCEEE	34.29	-
741	Sulfoxidation	LTAQPRLMEPIYLVE HHCCCCCCCCEEEEE	6.42	30846556
745	Phosphorylation	PRLMEPIYLVEIQCP CCCCCCEEEEEEECC	18.53	-
760	Phosphorylation	EQVVGGIYGVLNRKR HHHHHHHHHHHCCCC	12.40	28464451
766	Ubiquitination	IYGVLNRKRGHVFEE HHHHHCCCCCCCCCC	62.75	-
767	Methylation	YGVLNRKRGHVFEES HHHHCCCCCCCCCCC	36.89	-
774	Phosphorylation	RGHVFEESQVAGTPM CCCCCCCCCCCCCCE	23.82	28857561
779	Phosphorylation	EESQVAGTPMFVVKA CCCCCCCCCEEEEEE	11.22	25022875
781	Sulfoxidation	SQVAGTPMFVVKAYL CCCCCCCEEEEEEEE	3.90	21406390
785	Ubiquitination	GTPMFVVKAYLPVNE CCCEEEEEEEEECCC	26.47	-
793	Phosphorylation	AYLPVNESFGFTADL EEEECCCCCCCCCCC	26.01	21712546
802	Phosphorylation	GFTADLRSNTGGQAF CCCCCCCCCCCCCCC	46.14	-
842	Ubiquitination	VAETRKRKGLKEGIP HHHHHHHCCHHHCCH	72.18	-
845	Ubiquitination	TRKRKGLKEGIPALD HHHHCCHHHCCHHHH	63.66	21906983
845	2-Hydroxyisobutyrylation	TRKRKGLKEGIPALD HHHHCCHHHCCHHHH	63.66	-
857	Acetylation	ALDNFLDKL------ HHHHHHHHC------	59.24	19608861
857	Ubiquitination	ALDNFLDKL------ HHHHHHHHC------	59.24	19608861
857	Succinylation	ALDNFLDKL------ HHHHHHHHC------	59.24	23954790

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	O00418	Uniprot
265	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
373	Y	Phosphorylation	Kinase	CSK	P41240	Uniprot
435	T	Phosphorylation	Kinase	CDK2	P24941	PSP
595	S	Phosphorylation	Kinase	CDK1	P06493	PSP
595	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
595	S	Phosphorylation	Kinase	NEK2	P51955	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
595	S	Phosphorylation		24648518
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL5_HUMAN	RPL5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL12_HUMAN	RPL12	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
SYTC_HUMAN	TARS	physical	22939629
RT05_HUMAN	MRPS5	physical	22939629
HSP7C_HUMAN	HSPA8	physical	22939629
IF4A1_HUMAN	EIF4A1	physical	22939629
PABP1_HUMAN	PABPC1	physical	22939629
SYFA_HUMAN	FARSA	physical	22939629
XRCC6_HUMAN	XRCC6	physical	22939629
RL10L_HUMAN	RPL10L	physical	22939629
FLOT2_HUMAN	FLOT2	physical	22939629
RIR1_HUMAN	RRM1	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
EPHA2_HUMAN	EPHA2	physical	22939629
ERLN2_HUMAN	ERLIN2	physical	22939629
RBM4_HUMAN	RBM4	physical	22939629
HNRH1_HUMAN	HNRNPH1	physical	22939629
MIRO2_HUMAN	RHOT2	physical	22939629
HNRDL_HUMAN	HNRNPDL	physical	22939629
HNRPL_HUMAN	HNRNPL	physical	22939629
VATH_HUMAN	ATP6V1H	physical	22939629
NUP62_HUMAN	NUP62	physical	22939629
ROA3_HUMAN	HNRNPA3	physical	22939629
BZW1_HUMAN	BZW1	physical	22863883
CASP7_HUMAN	CASP7	physical	22863883
KCRB_HUMAN	CKB	physical	22863883
IF4H_HUMAN	EIF4H	physical	22863883
PSF2_HUMAN	GINS2	physical	22863883
METK2_HUMAN	MAT2A	physical	22863883
PAK2_HUMAN	PAK2	physical	22863883
PUR4_HUMAN	PFAS	physical	22863883
KS6A1_HUMAN	RPS6KA1	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
CALR_HUMAN	CALR	physical	26344197
HCFC1_HUMAN	HCFC1	physical	26344197
DHB4_HUMAN	HSD17B4	physical	26344197
IPO4_HUMAN	IPO4	physical	26344197
INO1_HUMAN	ISYNA1	physical	26344197
OPA1_HUMAN	OPA1	physical	26344197
RADI_HUMAN	RDX	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609306	Spinocerebellar ataxia 26 (SCA26)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EF2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-239; LYS-272;LYS-275; LYS-318; LYS-445 AND LYS-857, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-265, AND MASSSPECTROMETRY.	16097034 [Abstract]

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