dbPTM

EF1A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1A1_HUMAN
UniProt AC	P68104
Protein Name	Elongation factor 1-alpha 1
Gene Name	EEF1A1
Organism	Homo sapiens (Human).
Sequence Length	462
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleolus . Cell membrane . Colocalizes with DLC1 at actin-rich regions in the cell periphery (PubMed:19158340). Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitog
Protein Description	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production..
Protein Sequence	MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MGKEKTHIN ------CCCCCCEEE	46.99	26545399
5	Methylation	---MGKEKTHINIVV ---CCCCCCEEEEEE	49.22	24129315
6	Phosphorylation	--MGKEKTHINIVVI --CCCCCCEEEEEEE	29.13	20068231
18	Phosphorylation	VVIGHVDSGKSTTTG EEEEECCCCCCCCCC	47.21	20068231
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	Nitration	TTTGHLIYKCGGIDK CCCCEEEEECCCCCH	13.44	-
29	Phosphorylation	TTTGHLIYKCGGIDK CCCCEEEEECCCCCH	13.44	21945579
30	Acetylation	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	68965
30	Methylation	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	-
30	Ubiquitination	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	-
36	"N6,N6,N6-trimethyllysine"	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
36	Acetylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	26051181
36	Methylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	28520920
37	Methylation	KCGGIDKRTIEKFEK ECCCCCHHHHHHHHH	36.87	-
41	Sumoylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	-
41	Acetylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	23749302
41	Malonylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	26320211
41	Ubiquitination	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	-
41	Ubiquitination	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	21890473
44	Acetylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	23954790
44	Malonylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	26320211
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	-
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	21890473
51	"N6,N6-dimethyllysine"	KEAAEMGKGSFKYAW HHHHHCCCCCEEHHH	50.50	-
51	Methylation	KEAAEMGKGSFKYAW HHHHHCCCCCEEHHH	50.50	24129315
53	Phosphorylation	AAEMGKGSFKYAWVL HHHCCCCCEEHHHHH	23.27	24961811
55	"N6,N6-dimethyllysine"	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
55	Acetylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	19608861
55	Methylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	23644510
55	Ubiquitination	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	19608861
56	Phosphorylation	MGKGSFKYAWVLDKL CCCCCEEHHHHHHHH	12.04	29496907
62	"N6,N6-dimethyllysine"	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	-
62	Methylation	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	24129315
62	Ubiquitination	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	21890473
62	Ubiquitination	KYAWVLDKLKAERER EHHHHHHHHHHHHHH	47.96	21890473
64	Ubiquitination	AWVLDKLKAERERGI HHHHHHHHHHHHHCC	54.67	-
76	Phosphorylation	RGITIDISLWKFETS HCCEEEEEEEEEECC	25.16	25367160
79	"N6,N6,N6-trimethyllysine"	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	-
79	Acetylation	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	21466224
79	Methylation	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	26545399
82	Phosphorylation	ISLWKFETSKYYVTI EEEEEEECCCEEEEE	33.38	28152594
83	Phosphorylation	SLWKFETSKYYVTII EEEEEECCCEEEEEE	16.09	28152594
84	"N6,N6-dimethyllysine"	LWKFETSKYYVTIID EEEEECCCEEEEEEE	48.28	-
84	Acetylation	LWKFETSKYYVTIID EEEEECCCEEEEEEE	48.28	21466224
84	Methylation	LWKFETSKYYVTIID EEEEECCCEEEEEEE	48.28	24129315
84	Ubiquitination	LWKFETSKYYVTIID EEEEECCCEEEEEEE	48.28	21906983
85	Phosphorylation	WKFETSKYYVTIIDA EEEECCCEEEEEEEC	11.70	25159151
86	Phosphorylation	KFETSKYYVTIIDAP EEECCCEEEEEEECC	8.54	25159151
88	Phosphorylation	ETSKYYVTIIDAPGH ECCCEEEEEEECCCC	8.97	28152594
96	Methylation	IIDAPGHRDFIKNMI EEECCCCHHHHHHHC	46.58	-
104	Phosphorylation	DFIKNMITGTSQADC HHHHHHCCCCCHHCE	24.52	19690332
106	Phosphorylation	IKNMITGTSQADCAV HHHHCCCCCHHCEEE	14.71	22817900
107	Phosphorylation	KNMITGTSQADCAVL HHHCCCCCHHCEEEE	25.39	19690332
111	S-nitrosylation	TGTSQADCAVLIVAA CCCCHHCEEEEEEEE	2.94	22178444
128	Phosphorylation	GEFEAGISKNGQTRE CCHHCCCCCCCCCHH	21.10	27251275
129	Ubiquitination	EFEAGISKNGQTREH CHHCCCCCCCCCHHH	64.28	-
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	21466224
146	Ubiquitination	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	21890473
151	Ubiquitination	GVKQLIVGVNKMDST CCCEEEECCCCCCCC	15.41	21890473
154	Acetylation	QLIVGVNKMDSTEPP EEEECCCCCCCCCCC	41.50	26051181
154	Methylation	QLIVGVNKMDSTEPP EEEECCCCCCCCCCC	41.50	-
154	Ubiquitination	QLIVGVNKMDSTEPP EEEECCCCCCCCCCC	41.50	21906983
155	Sulfoxidation	LIVGVNKMDSTEPPY EEECCCCCCCCCCCC	4.08	21406390
157	Phosphorylation	VGVNKMDSTEPPYSQ ECCCCCCCCCCCCCH	31.04	20068231
158	Phosphorylation	GVNKMDSTEPPYSQK CCCCCCCCCCCCCHH	48.52	20068231
158	Ubiquitination	GVNKMDSTEPPYSQK CCCCCCCCCCCCCHH	48.52	21890473
162	Phosphorylation	MDSTEPPYSQKRYEE CCCCCCCCCHHHHHH	34.15	20068231
163	Phosphorylation	DSTEPPYSQKRYEEI CCCCCCCCHHHHHHH	34.69	20068231
165	"N6,N6-dimethyllysine"	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	-
165	Acetylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	25953088
165	Methylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	28108655
165	Ubiquitination	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	21906983
166	Dimethylation	EPPYSQKRYEEIVKE CCCCCHHHHHHHHHH	36.14	-
166	Methylation	EPPYSQKRYEEIVKE CCCCCHHHHHHHHHH	36.14	-
167	Phosphorylation	PPYSQKRYEEIVKEV CCCCHHHHHHHHHHH	25.58	28152594
172	Acetylation	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	23954790
172	Malonylation	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	26320211
172	Methylation	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	-
172	Ubiquitination	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	21890473
175	Phosphorylation	EEIVKEVSTYIKKIG HHHHHHHHHHHHHHC	19.31	30266825
176	Phosphorylation	EIVKEVSTYIKKIGY HHHHHHHHHHHHHCC	34.15	30266825
177	Phosphorylation	IVKEVSTYIKKIGYN HHHHHHHHHHHHCCC	11.84	27155012
179	Acetylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	23954790
179	Malonylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	26320211
179	Methylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	-
179	Ubiquitination	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	21890473
180	Acetylation	EVSTYIKKIGYNPDT HHHHHHHHHCCCCCC	31.63	7369453
180	Malonylation	EVSTYIKKIGYNPDT HHHHHHHHHCCCCCC	31.63	26320211
180	Ubiquitination	EVSTYIKKIGYNPDT HHHHHHHHHCCCCCC	31.63	21906983
212	Acetylation	SANMPWFKGWKVTRK CCCCCCCCCEEEEEC	61.05	89005
212	Ubiquitination	SANMPWFKGWKVTRK CCCCCCCCCEEEEEC	61.05	-
215	Ubiquitination	MPWFKGWKVTRKDGN CCCCCCEEEEECCCC	42.25	-
219	Acetylation	KGWKVTRKDGNASGT CCEEEEECCCCCCCC	61.70	26051181
219	Ubiquitination	KGWKVTRKDGNASGT CCEEEEECCCCCCCC	61.70	21906983
223	Ubiquitination	VTRKDGNASGTTLLE EEECCCCCCCCCHHH	18.18	21890473
224	Phosphorylation	TRKDGNASGTTLLEA EECCCCCCCCCHHHH	40.44	25159151
226	Phosphorylation	KDGNASGTTLLEALD CCCCCCCCCHHHHHH	16.27	22199227
227	Phosphorylation	DGNASGTTLLEALDC CCCCCCCCHHHHHHH	32.63	26657352
234	S-nitrosocysteine	TLLEALDCILPPTRP CHHHHHHHHCCCCCC	3.42	-
234	Glutathionylation	TLLEALDCILPPTRP CHHHHHHHHCCCCCC	3.42	22555962
234	S-nitrosylation	TLLEALDCILPPTRP CHHHHHHHHCCCCCC	3.42	22178444
234	Ubiquitination	TLLEALDCILPPTRP CHHHHHHHHCCCCCC	3.42	21890473
239	Phosphorylation	LDCILPPTRPTDKPL HHHHCCCCCCCCCCC	47.55	20068231
242	Phosphorylation	ILPPTRPTDKPLRLP HCCCCCCCCCCCCCC	54.05	20068231
244	Acetylation	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	26051181
244	Malonylation	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	26320211
244	Ubiquitination	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	-
252	Ubiquitination	PLRLPLQDVYKIGGI CCCCCHHHEEEECCC	54.09	21890473
254	Nitration	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	-
254	Phosphorylation	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	25159151
255	Acetylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	23954790
255	Malonylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	26320211
255	Methylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
255	Ubiquitination	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	20639865
261	O-linked_Glycosylation	YKIGGIGTVPVGRVE EEECCCEEEECCEEE	21.51	31373491
261	Phosphorylation	YKIGGIGTVPVGRVE EEECCCEEEECCEEE	21.51	28450419
266	Methylation	IGTVPVGRVETGVLK CEEEECCEEECCCCC	24.27	-
269	Phosphorylation	VPVGRVETGVLKPGM EECCEEECCCCCCCE	29.72	27273156
273	Acetylation	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	23954790
273	Malonylation	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	26320211
273	Ubiquitination	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	21890473
276	Sulfoxidation	TGVLKPGMVVTFAPV CCCCCCCEEEEEECC	2.73	21406390
279	O-linked_Glycosylation	LKPGMVVTFAPVNVT CCCCEEEEEECCCEE	11.58	31373491
279	Phosphorylation	LKPGMVVTFAPVNVT CCCCEEEEEECCCEE	11.58	27080861
286	Phosphorylation	TFAPVNVTTEVKSVE EEECCCEEEEEEEEE	16.43	28857561
287	Phosphorylation	FAPVNVTTEVKSVEM EECCCEEEEEEEEEH	34.20	28857561
290	Ubiquitination	VNVTTEVKSVEMHHE CCEEEEEEEEEHHHH	42.42	-
291	Phosphorylation	NVTTEVKSVEMHHEA CEEEEEEEEEHHHHH	28.61	29900121
300	Phosphorylation	EMHHEALSEALPGDN EHHHHHHHHHCCCCC	28.07	25159151
301	5-glutamyl glycerylphosphorylethanolamine	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
301	Formation of an isopeptide bond	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	2569467
316	Phosphorylation	GFNVKNVSVKDVRRG CEEEEECCHHHHHCC	32.61	26074081
318	"N6,N6,N6-trimethyllysine"	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	-
318	Acetylation	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	16916647
318	Methylation	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	25144183
318	Ubiquitination	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	21906983
330	Acetylation	GNVAGDSKNDPPMEA CCCCCCCCCCCCHHC	70.84	26051181
330	Phosphoglycerylation	GNVAGDSKNDPPMEA CCCCCCCCCCCCHHC	70.84	-
341	O-linked_Glycosylation	PMEAAGFTAQVIILN CHHCCCEEEEEEEEC	18.43	OGP
354	Phosphorylation	LNHPGQISAGYAPVL ECCCCCCCCCCCCCC	14.04	-
357	Phosphorylation	PGQISAGYAPVLDCH CCCCCCCCCCCCCCH	13.88	-
365	Phosphorylation	APVLDCHTAHIACKF CCCCCCHHHHHHHHH	26.68	-
371	Ubiquitination	HTAHIACKFAELKEK HHHHHHHHHHHHHHH	38.29	21890473
374	5-glutamyl glycerylphosphorylethanolamine	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
374	Formation of an isopeptide bond	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	2569467
374	Ubiquitination	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	21890473
376	Acetylation	ACKFAELKEKIDRRS HHHHHHHHHHHHHCC	48.76	26051181
383	Phosphorylation	KEKIDRRSGKKLEDG HHHHHHCCCCCCCCC	56.72	29496963
385	Ubiquitination	KIDRRSGKKLEDGPK HHHHCCCCCCCCCCC	56.27	21906983
386	Acetylation	IDRRSGKKLEDGPKF HHHCCCCCCCCCCCH	61.71	23749302
386	Ubiquitination	IDRRSGKKLEDGPKF HHHCCCCCCCCCCCH	61.71	19608861
392	Acetylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	23954790
392	Malonylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	26320211
392	Succinylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	-
392	Succinylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	-
392	Ubiquitination	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	21890473
395	Acetylation	EDGPKFLKSGDAAIV CCCCCHHCCCCEEEE	56.37	19608861
395	Malonylation	EDGPKFLKSGDAAIV CCCCCHHCCCCEEEE	56.37	26320211
395	Ubiquitination	EDGPKFLKSGDAAIV CCCCCHHCCCCEEEE	56.37	21890473
396	Phosphorylation	DGPKFLKSGDAAIVD CCCCHHCCCCEEEEE	44.01	30140170
404	Sulfoxidation	GDAAIVDMVPGKPMC CCEEEEECCCCCEEE	2.44	21406390
408	Acetylation	IVDMVPGKPMCVESF EEECCCCCEEEEEEC	24.41	26822725
408	Methylation	IVDMVPGKPMCVESF EEECCCCCEEEEEEC	24.41	-
408	Ubiquitination	IVDMVPGKPMCVESF EEECCCCCEEEEEEC	24.41	21906983
411	S-glutathionyl cysteine	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	-
411	Glutathionylation	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	22833525
411	S-nitrosylation	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	22178444
411	S-palmitoylation	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	26865113
414	Phosphorylation	GKPMCVESFSDYPPL CCEEEEEECCCCCCC	15.06	28857561
416	Phosphorylation	PMCVESFSDYPPLGR EEEEEECCCCCCCCH	45.58	28857561
418	Phosphorylation	CVESFSDYPPLGRFA EEEECCCCCCCCHHH	12.92	23898821
418	Ubiquitination	CVESFSDYPPLGRFA EEEECCCCCCCCHHH	12.92	21890473
430	Methylation	RFAVRDMRQTVAVGV HHHHHCHHHHHHHEE	33.05	-
432	Phosphorylation	AVRDMRQTVAVGVIK HHHCHHHHHHHEEEE	10.48	21712546
439	Acetylation	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	21466224
439	Malonylation	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	26320211
439	Ubiquitination	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	21890473
443	Acetylation	GVIKAVDKKAAGAGK EEEEECCHHHCCCCC	37.40	21466224
444	Acetylation	VIKAVDKKAAGAGKV EEEECCHHHCCCCCC	38.72	21466224
444	Ubiquitination	VIKAVDKKAAGAGKV EEEECCHHHCCCCCC	38.72	21906983
450	Acetylation	KKAAGAGKVTKSAQK HHHCCCCCCCHHHHH	46.31	129291
450	Ubiquitination	KKAAGAGKVTKSAQK HHHCCCCCCCHHHHH	46.31	21906983
452	Phosphorylation	AAGAGKVTKSAQKAQ HCCCCCCCHHHHHHH	23.83	28985074
453	Acetylation	AGAGKVTKSAQKAQK CCCCCCCHHHHHHHH	46.94	26051181
454	Phosphorylation	GAGKVTKSAQKAQKA CCCCCCHHHHHHHHC	26.94	24719451
457	Acetylation	KVTKSAQKAQKAK-- CCCHHHHHHHHCC--	53.13	129299
460	Acetylation	KSAQKAQKAK----- HHHHHHHHCC-----	64.10	129295

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
88	T	Phosphorylation	Kinase	BRAF	P15056	PSP
261	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS
300	S	Phosphorylation	Kinase	TGFBR1	P36897	Uniprot
432	T	Phosphorylation	Kinase	PASK	Q96RG2	Uniprot
432	T	Phosphorylation	Kinase	ROCK2	O75116	PSP
432	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
432	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	G	Methylation	26545399
Trimethylated at Gly-2 by EEF1AKNMT.
36	K	Methylation	25144183
Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant.
55	K	Methylation
Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant.
79	K	Methylation	25144183
Trimethylated at Lys-79 by EEF1AKMT1.
165	K	Methylation
Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation.
318	K	Methylation	25144183
Trimethylated at Lys-318 by EEF1AKMT2.

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 EF1A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PROF2_HUMAN	PFN2	physical	16169070
PLCG1_HUMAN	PLCG1	physical	11886851
ZPR1_HUMAN	ZPR1	physical	9852145
ABTB2_HUMAN	ABTB2	physical	18459963
RAF1_HUMAN	RAF1	physical	17332776
NEMO_HUMAN	IKBKG	physical	20211142
GA45G_HUMAN	GADD45G	physical	15383276
TRI18_HUMAN	MID1	physical	18172692
HS90A_HUMAN	HSP90AA1	physical	18172692
HSP7C_HUMAN	HSPA8	physical	18172692
EF1A1_HUMAN	EEF1A1	physical	18172692
2AAA_HUMAN	PPP2R1A	physical	18172692
ZBT7A_HUMAN	ZBTB7A	physical	19471103
MDM2_HUMAN	MDM2	physical	17373842
LRRK2_HUMAN	LRRK2	physical	19559761
EF1G_HUMAN	EEF1G	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
EF2_HUMAN	EEF2	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL12_HUMAN	RPL12	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
TBB5_HUMAN	TUBB	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
EF1B_HUMAN	EEF1B2	physical	22939629
MBB1A_HUMAN	MYBBP1A	physical	22939629
YBOX1_HUMAN	YBX1	physical	22939629
FBRL_HUMAN	FBL	physical	22939629
NOP56_HUMAN	NOP56	physical	22939629
ILF2_HUMAN	ILF2	physical	22939629
HNRL1_HUMAN	HNRNPUL1	physical	22939629
HNRPK_HUMAN	HNRNPK	physical	22939629
PABP1_HUMAN	PABPC1	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
U5S1_HUMAN	EFTUD2	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22939629
RBMX_HUMAN	RBMX	physical	22939629
FUS_HUMAN	FUS	physical	22939629
PUF60_HUMAN	PUF60	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
HNRDL_HUMAN	HNRNPDL	physical	22939629
HNRPL_HUMAN	HNRNPL	physical	22939629
PCBP2_HUMAN	PCBP2	physical	22939629
G3P_HUMAN	GAPDH	physical	22939629
SEPT2_HUMAN	SEPT2	physical	22939629
RBM4_HUMAN	RBM4	physical	22939629
RUVB2_HUMAN	RUVBL2	physical	22939629
RL10L_HUMAN	RPL10L	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
RT07_HUMAN	MRPS7	physical	22939629
RAB7A_HUMAN	RAB7A	physical	22939629
SOSB1_HUMAN	NABP2	physical	22939629
PICAL_HUMAN	PICALM	physical	22939629
PSB4_HUMAN	PSMB4	physical	22939629
SSBP_HUMAN	SSBP1	physical	22939629
CCAR2_HUMAN	CCAR2	physical	22939629
MK67I_HUMAN	NIFK	physical	22939629
HSP72_HUMAN	HSPA2	physical	22939629
GTF2I_HUMAN	GTF2I	physical	22939629
MRP2_HUMAN	ABCC2	physical	22939629
STRN4_HUMAN	STRN4	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
SERA_HUMAN	PHGDH	physical	22939629
NU214_HUMAN	NUP214	physical	22939629
RANB9_HUMAN	RANBP9	physical	22939629
SP16H_HUMAN	SUPT16H	physical	22939629
PSA6_HUMAN	PSMA6	physical	22939629
ENOB_HUMAN	ENO3	physical	22939629
IF4A1_HUMAN	EIF4A1	physical	22939629
QCR6_HUMAN	UQCRH	physical	22939629
H2A1D_HUMAN	HIST1H2AD	physical	22939629
GORS2_HUMAN	GORASP2	physical	22939629
RBM3_HUMAN	RBM3	physical	22939629
RM14_HUMAN	MRPL14	physical	22939629
RGS12_HUMAN	RGS12	genetic	17124247
UBD_HUMAN	UBD	physical	22569823
CD81_HUMAN	CD81	physical	23463506
CTIP_HUMAN	RBBP8	physical	21988832
STAT6_HUMAN	STAT6	physical	21988832
TRAP1_HUMAN	TRAP1	physical	24113185
G3P_HUMAN	GAPDH	physical	22863883
PFKAP_HUMAN	PFKP	physical	22863883
PP1B_HUMAN	PPP1CB	physical	22863883
RBX1_HUMAN	RBX1	physical	25423367
CUL4A_HUMAN	CUL4A	physical	25423367
SAMH1_HUMAN	SAMHD1	physical	25423367
THIL_HUMAN	ACAT1	physical	26344197
CBS_HUMAN	CBS	physical	26344197
DDX17_HUMAN	DDX17	physical	26344197
EF1G_HUMAN	EEF1G	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
FA98B_HUMAN	FAM98B	physical	26344197
PUR2_HUMAN	GART	physical	26344197
GMPPB_HUMAN	GMPPB	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
GORS2_HUMAN	GORASP2	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
GRP75_HUMAN	HSPA9	physical	26344197
ECM29_HUMAN	KIAA0368	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
PABP3_HUMAN	PABPC3	physical	26344197
PABP4_HUMAN	PABPC4	physical	26344197
ODPB_HUMAN	PDHB	physical	26344197
KPYM_HUMAN	PKM	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
RPAB1_HUMAN	POLR2E	physical	26344197
PSMD1_HUMAN	PSMD1	physical	26344197
RAB2A_HUMAN	RAB2A	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
RTCB_HUMAN	RTCB	physical	26344197
RUVB1_HUMAN	RUVBL1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
STAT6_HUMAN	STAT6	physical	26344197
FCL_HUMAN	TSTA3	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
UBR5_HUMAN	UBR5	physical	26344197
SYVC_HUMAN	VARS	physical	26344197
VP13A_HUMAN	VPS13A	physical	26344197
SYYC_HUMAN	YARS	physical	26344197
EF1A2_HUMAN	EEF1A2	physical	28514442
EF1D_HUMAN	EEF1D	physical	28514442
TTL12_HUMAN	TTLL12	physical	28514442
SYVC_HUMAN	VARS	physical	28514442
SYCC_HUMAN	CARS	physical	28514442
EF1B_HUMAN	EEF1B2	physical	28514442
PP2AA_HUMAN	PPP2CA	physical	28514442
FHL2_HUMAN	FHL2	physical	28514442
ZPR1_HUMAN	ZPR1	physical	28514442

Drug and Disease Associations

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

Regulatory Network of EF1A1_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-41; LYS-44; LYS-55; LYS-146;LYS-172; LYS-179; LYS-255; LYS-318; LYS-392; LYS-395 AND LYS-439, ANDMASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibitionof mRNA translation."; Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S.; Curr. Biol. 20:1615-1625(2010). Cited for: PHOSPHORYLATION AT SER-300.	20832312 [Abstract]
"Male germ cell expression of the PAS domain kinase PASKIN and itsnovel target eukaryotic translation elongation factor eEF1A1."; Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F.,Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P.,Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.; Cell. Physiol. Biochem. 20:227-240(2007). Cited for: PHOSPHORYLATION AT THR-432, AND MUTAGENESIS OF THR-432.	17595531 [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 TYR-162, AND MASSSPECTROMETRY.	17287340 [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; TYR-86 AND TYR-141,AND MASS SPECTROMETRY.	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 MASSSPECTROMETRY.	15592455 [Abstract]

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