dbPTM

EF1A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1A2_HUMAN
UniProt AC	Q05639
Protein Name	Elongation factor 1-alpha 2
Gene Name	EEF1A2
Organism	Homo sapiens (Human).
Sequence Length	463
Subcellular Localization	Nucleus.
Protein Description	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis..
Protein Sequence	MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNVCGDSKSDPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MGKEKTHIN ------CCCCCCEEE	46.99	-
3	Ubiquitination	-----MGKEKTHINI -----CCCCCCEEEE	55.53	32015554
5	Ubiquitination	---MGKEKTHINIVV ---CCCCCCEEEEEE	49.22	33845483
6	Phosphorylation	--MGKEKTHINIVVI --CCCCCCEEEEEEE	29.13	20068231
18	Phosphorylation	VVIGHVDSGKSTTTG EEEEECCCCCCCCCC	47.21	20068231
20	Ubiquitination	IGHVDSGKSTTTGHL EEECCCCCCCCCCEE	48.89	33845483
21	Phosphorylation	GHVDSGKSTTTGHLI EECCCCCCCCCCEEE	34.21	21945579
22	Phosphorylation	HVDSGKSTTTGHLIY ECCCCCCCCCCEEEE	31.68	21945579
23	Phosphorylation	VDSGKSTTTGHLIYK CCCCCCCCCCEEEEE	37.56	21945579
24	Phosphorylation	DSGKSTTTGHLIYKC CCCCCCCCCEEEEEC	23.77	21945579
29	Phosphorylation	TTTGHLIYKCGGIDK CCCCEEEEECCCCCH	13.44	21945579
30	Acetylation	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	69029
30	Methylation	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	-
30	Neddylation	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	32015554
30	Ubiquitination	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	21963094
36	Trimethylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
36	Acetylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	69033
36	Methylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	28520920
36	Ubiquitination	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	23000965
37	Methylation	KCGGIDKRTIEKFEK ECCCCCHHHHHHHHH	36.87	-
41	Sumoylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	-
41	Acetylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	69037
41	Sumoylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	-
41	Ubiquitination	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	23000965
44	Acetylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	90423
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	23000965
51	"N6,N6-dimethyllysine"	KEAAEMGKGSFKYAW HHHHHCCCCCEEHHH	50.50	-
51	Methylation	KEAAEMGKGSFKYAW HHHHHCCCCCEEHHH	50.50	-
51	Ubiquitination	KEAAEMGKGSFKYAW HHHHHCCCCCEEHHH	50.50	22817900
53	Phosphorylation	AAEMGKGSFKYAWVL HHHCCCCCEEHHHHH	23.27	24961811
55	"N6,N6,N6-trimethyllysine"	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
55	Acetylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	18582431
55	Methylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	30612740
55	Sumoylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
55	Ubiquitination	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	21906983
56	Phosphorylation	MGKGSFKYAWVLDKL CCCCCEEHHHHHHHH	12.04	29496907
62	"N6,N6-dimethyllysine"	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	-
62	Methylation	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	-
62	Ubiquitination	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	21906983
64	Neddylation	AWVLDKLKAERERGI HHHHHHHHHHHHHCC	54.67	32015554
64	Ubiquitination	AWVLDKLKAERERGI HHHHHHHHHHHHHCC	54.67	22817900
69	Methylation	KLKAERERGITIDIS HHHHHHHHCCEEEEE	48.30	-
76	Phosphorylation	RGITIDISLWKFETT HCCEEEEEEEEEECC	25.16	25367160
79	"N6,N6,N6-trimethyllysine"	TIDISLWKFETTKYY EEEEEEEEEECCEEE	38.32	-
79	Acetylation	TIDISLWKFETTKYY EEEEEEEEEECCEEE	38.32	12437787
79	Methylation	TIDISLWKFETTKYY EEEEEEEEEECCEEE	38.32	24129315
84	"N6,N6-dimethyllysine"	LWKFETTKYYITIID EEEEECCEEEEEEEE	43.40	-
84	Methylation	LWKFETTKYYITIID EEEEECCEEEEEEEE	43.40	23644510
85	Phosphorylation	WKFETTKYYITIIDA EEEECCEEEEEEEEC	9.67	28152594
86	Phosphorylation	KFETTKYYITIIDAP EEECCEEEEEEEECC	7.98	28152594
88	Phosphorylation	ETTKYYITIIDAPGH ECCEEEEEEEECCCC	8.85	29396449
104	Phosphorylation	DFIKNMITGTSQADC HHHHHHCCCCCHHCE	24.52	19690332
106	Phosphorylation	IKNMITGTSQADCAV HHHHCCCCCHHCEEE	14.71	22817900
107	Phosphorylation	KNMITGTSQADCAVL HHHCCCCCHHCEEEE	25.39	19690332
128	Phosphorylation	GEFEAGISKNGQTRE CCHHCCCCCCCCCHH	21.10	26126808
129	Ubiquitination	EFEAGISKNGQTREH CHHCCCCCCCCCHHH	64.28	21963094
133	Phosphorylation	GISKNGQTREHALLA CCCCCCCCHHHHHHH	39.15	-
134	Methylation	ISKNGQTREHALLAY CCCCCCCHHHHHHHH	26.30	-
141	Phosphorylation	REHALLAYTLGVKQL HHHHHHHHHHCCCEE	11.49	25159151
142	Phosphorylation	EHALLAYTLGVKQLI HHHHHHHHHCCCEEE	16.07	21945579
146	Acetylation	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	129483
146	Ubiquitination	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	23000965
154	Ubiquitination	QLIVGVNKMDSTEPA EEEECCCCCCCCCCC	41.50	23000965
163	Phosphorylation	DSTEPAYSEKRYDEI CCCCCCCCHHHHHHH	38.45	26437602
165	"N6,N6,N6-trimethyllysine"	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	-
165	Acetylation	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	30583049
165	Methylation	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	24129315
165	Ubiquitination	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	22817900
166	Methylation	EPAYSEKRYDEIVKE CCCCCHHHHHHHHHH	39.83	-
172	Ubiquitination	KRYDEIVKEVSAYIK HHHHHHHHHHHHHHH	59.04	23000965
175	Phosphorylation	DEIVKEVSAYIKKIG HHHHHHHHHHHHHHC	19.22	28152594
177	Phosphorylation	IVKEVSAYIKKIGYN HHHHHHHHHHHHCCC	13.03	28152594
179	2-Hydroxyisobutyrylation	KEVSAYIKKIGYNPA HHHHHHHHHHCCCCC	26.18	-
179	Acetylation	KEVSAYIKKIGYNPA HHHHHHHHHHCCCCC	26.18	19608861
179	Ubiquitination	KEVSAYIKKIGYNPA HHHHHHHHHHCCCCC	26.18	27667366
205	Phosphorylation	GDNMLEPSPNMPWFK CCCCCCCCCCCCCCC	21.38	-
219	Ubiquitination	KGWKVERKEGNASGV CCEEEEEECCCCCCH	57.37	29967540
224	Phosphorylation	ERKEGNASGVSLLEA EEECCCCCCHHHHHH	43.67	24173317
227	Phosphorylation	EGNASGVSLLEALDT CCCCCCHHHHHHHHH	30.66	24173317
234	Phosphorylation	SLLEALDTILPPTRP HHHHHHHHCCCCCCC	25.84	24144214
239	Phosphorylation	LDTILPPTRPTDKPL HHHCCCCCCCCCCCC	47.55	24144214
242	Phosphorylation	ILPPTRPTDKPLRLP CCCCCCCCCCCCCCC	54.05	20068231
244	Ubiquitination	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	29967540
254	Phosphorylation	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	17192257
255	Acetylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	22643111
255	Methylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
255	Neddylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	32015554
255	Sumoylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
255	Ubiquitination	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	23000965
261	Phosphorylation	YKIGGIGTVPVGRVE EEECCCEEEECCEEE	21.51	28450419
266	Methylation	IGTVPVGRVETGILR CEEEECCEEECCCCC	24.27	-
269	Phosphorylation	VPVGRVETGILRPGM EECCEEECCCCCCCE	27.02	28464451
276	Sulfoxidation	TGILRPGMVVTFAPV CCCCCCCEEEEEECC	2.13	28183972
279	Phosphorylation	LRPGMVVTFAPVNIT CCCCEEEEEECCCEE	11.58	28464451
287	Phosphorylation	FAPVNITTEVKSVEM EECCCEEEEEEEEEH	34.68	-
291	Phosphorylation	NITTEVKSVEMHHEA CEEEEEEEEEHHHHH	28.61	28464451
300	Phosphorylation	EMHHEALSEALPGDN EHHHHHHHHHCCCCC	28.07	28464451
301	5-glutamyl glycerylphosphorylethanolamine	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
301	Formation of an isopeptide bond	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
313	Sumoylation	DNVGFNVKNVSVKDI CCCCEEEEECCHHHC	53.38	-
313	Ubiquitination	DNVGFNVKNVSVKDI CCCCEEEEECCHHHC	53.38	-
316	Phosphorylation	GFNVKNVSVKDIRRG CEEEEECCHHHCCCC	32.61	26074081
318	"N6,N6-dimethyllysine"	NVKNVSVKDIRRGNV EEEECCHHHCCCCCC	39.67	-
318	Acetylation	NVKNVSVKDIRRGNV EEEECCHHHCCCCCC	39.67	22424773
318	Methylation	NVKNVSVKDIRRGNV EEEECCHHHCCCCCC	39.67	24129315
318	Ubiquitination	NVKNVSVKDIRRGNV EEEECCHHHCCCCCC	39.67	29967540
358	Phosphorylation	GQISAGYSPVIDCHT CCCCCCCCCCCCHHH	16.27	-
374	5-glutamyl glycerylphosphorylethanolamine	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
374	Formation of an isopeptide bond	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
376	Ubiquitination	ACKFAELKEKIDRRS HHHHHHHHHHHHHHC	48.76	32142685
383	Phosphorylation	KEKIDRRSGKKLEDN HHHHHHHCCCCCCCC	56.72	-
392	Succinylation	KKLEDNPKSLKSGDA CCCCCCCCCCCCCCE	74.75	23954790
392	Ubiquitination	KKLEDNPKSLKSGDA CCCCCCCCCCCCCCE	74.75	32015554
396	Phosphorylation	DNPKSLKSGDAAIVE CCCCCCCCCCEEEEE	47.39	26126808
411	Glutathionylation	MVPGKPMCVESFSQY ECCCCCEEECCHHHC	4.10	22555962
414	Phosphorylation	GKPMCVESFSQYPPL CCCEEECCHHHCCCC	15.14	26126808
416	Phosphorylation	PMCVESFSQYPPLGR CEEECCHHHCCCCCC	37.78	26126808
429	Sulfoxidation	GRFAVRDMRQTVAVG CCHHHCCHHHHEEEE	2.10	28183972
430	Methylation	RFAVRDMRQTVAVGV CHHHCCHHHHEEEEE	33.05	-
432	Phosphorylation	AVRDMRQTVAVGVIK HHCCHHHHEEEEEEE	10.48	21082442
439	Acetylation	TVAVGVIKNVEKKSG HEEEEEEECCEECCC	53.16	19608861
450	Ubiquitination	KKSGGAGKVTKSAQK ECCCCCCCCCHHHHH	46.31	30230243
452	Phosphorylation	SGGAGKVTKSAQKAQ CCCCCCCCHHHHHHH	23.83	-
453	Ubiquitination	GGAGKVTKSAQKAQK CCCCCCCHHHHHHHH	46.94	27667366
454	Phosphorylation	GAGKVTKSAQKAQKA CCCCCCHHHHHHHHC	26.94	-

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
21	S	Phosphorylation	Kinase	BRAF	P15056	PSP
21	S	Phosphorylation	Kinase	RAF1	P04049	PSP
205	S	Phosphorylation	Kinase	JNK1	P45983	PSP
205	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS
358	S	Phosphorylation	Kinase	JNK1	P45983	PSP
358	S	Phosphorylation	Kinase	MAPK8	Q91Y86	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
36	K	Methylation	28520920
Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant.
55	K	Methylation	30612740
Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant.
165	K	Methylation	24129315
Trimethylated at Lys-165 by EEF1AKMT3.

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 EF1A2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYVC_HUMAN	VARS	physical	17353931
EF1D_HUMAN	EEF1D	physical	17353931
EF1B_HUMAN	EEF1B2	physical	17353931
TTL12_HUMAN	TTLL12	physical	22939629
ABTB1_HUMAN	ABTB1	physical	25416956
EF1B_HUMAN	EEF1B2	physical	26344197
EF1G_HUMAN	EEF1G	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
U5S1_HUMAN	EFTUD2	physical	26344197
GMPPB_HUMAN	GMPPB	physical	26344197
GORS2_HUMAN	GORASP2	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
PABP3_HUMAN	PABPC3	physical	26344197
KPYR_HUMAN	PKLR	physical	26344197
KPYM_HUMAN	PKM	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
PSMD1_HUMAN	PSMD1	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
EF1D_HUMAN	EEF1D	physical	28514442
SYCC_HUMAN	CARS	physical	28514442
SYVC_HUMAN	VARS	physical	28514442
TTL12_HUMAN	TTLL12	physical	28514442
EF1B_HUMAN	EEF1B2	physical	28514442
VGFR3_HUMAN	FLT4	physical	28514442
TCTP_HUMAN	TPT1	physical	25635048

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616409	Epileptic encephalopathy, early infantile, 33 (EIEE33)
616393	Mental retardation, autosomal dominant 38 (MRD38)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EF1A2_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-179 AND LYS-439, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASSSPECTROMETRY.	19690332 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-141, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-141, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-141, AND MASSSPECTROMETRY.	15592455 [Abstract]

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