dbPTM

EF1G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1G_HUMAN
UniProt AC	P26641
Protein Name	Elongation factor 1-gamma
Gene Name	EEF1G
Organism	Homo sapiens (Human).
Sequence Length	437
Subcellular Localization
Protein Description	Probably plays a role in anchoring the complex to other cellular components..
Protein Sequence	MAAGTLYTYPENWRAFKALIAAQYSGAQVRVLSAPPHFHFGQTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSNEELRGSTPEAAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVRRILGLLDAYLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAVLGEVKLCEKMAQFDAKKFAETQPKKDTPRKEKGSREEKQKPQAERKEEKKAAAPAPEEEMDECEQALAAEPKAKDPFAHLPKSTFVLDEFKRKYSNEDTLSVALPYFWEHFDKDGWSLWYSEYRFPEELTQTFMSCNLITGMFQRLDKLRKNAFASVILFGTNNSSSISGVWVFRGQELAFPLSPDWQVDYESYTWRKLDPGSEETQTLVREYFSWEGAFQHVGKAFNQGKIFK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAGTLYTY ------CCCCCEECC	18.01	22223895
5	Phosphorylation	---MAAGTLYTYPEN ---CCCCCEECCCCC	16.32	25693802
7	Phosphorylation	-MAAGTLYTYPENWR -CCCCCEECCCCCHH	12.22	27259358
8	Phosphorylation	MAAGTLYTYPENWRA CCCCCEECCCCCHHH	35.39	27259358
9	Phosphorylation	AAGTLYTYPENWRAF CCCCEECCCCCHHHH	8.59	27259358
17	Acetylation	PENWRAFKALIAAQY CCCHHHHHHHHHHHH	41.10	26051181
17	Methylation	PENWRAFKALIAAQY CCCHHHHHHHHHHHH	41.10	-
17	Ubiquitination	PENWRAFKALIAAQY CCCHHHHHHHHHHHH	41.10	-
24	Phosphorylation	KALIAAQYSGAQVRV HHHHHHHHCCCEEEE	12.35	28152594
25	Phosphorylation	ALIAAQYSGAQVRVL HHHHHHHCCCEEEEE	18.64	28152594
33	Phosphorylation	GAQVRVLSAPPHFHF CCEEEEEECCCCCCC	35.55	30266825
43	Phosphorylation	PHFHFGQTNRTPEFL CCCCCCCCCCCHHHH	27.35	30266825
46	Phosphorylation	HFGQTNRTPEFLRKF CCCCCCCCHHHHHHC	29.28	29255136
51	Methylation	NRTPEFLRKFPAGKV CCCHHHHHHCCCCCC	43.84	-
67	Ubiquitination	AFEGDDGFCVFESNA CCCCCCCEEEEECCE	4.06	-
80	Phosphorylation	NAIAYYVSNEELRGS CEEEEEECCHHHCCC	23.54	29802988
107	Ubiquitination	SFADSDIVPPASTWV HHCCCCCCCCHHHCE	5.80	-
132	2-Hydroxyisobutyrylation	KQATENAKEEVRRIL HHHHHHHHHHHHHHH	67.02	-
132	Acetylation	KQATENAKEEVRRIL HHHHHHHHHHHHHHH	67.02	23749302
132	Ubiquitination	KQATENAKEEVRRIL HHHHHHHHHHHHHHH	67.02	19608861
145	Phosphorylation	ILGLLDAYLKTRTFL HHHHHHHHHHHCEEE	14.38	28152594
147	2-Hydroxyisobutyrylation	GLLDAYLKTRTFLVG HHHHHHHHHCEEECC	24.24	-
147	Acetylation	GLLDAYLKTRTFLVG HHHHHHHHHCEEECC	24.24	19608861
147	Ubiquitination	GLLDAYLKTRTFLVG HHHHHHHHHCEEECC	24.24	21890473
149	Methylation	LDAYLKTRTFLVGER HHHHHHHCEEECCCC	23.15	-
182	Acetylation	VLEPSFRQAFPNTNR HHCHHHHHHCCCCCC	45.40	-
182	Ubiquitination	VLEPSFRQAFPNTNR HHCHHHHHHCCCCCC	45.40	-
194	S-nitrosocysteine	TNRWFLTCINQPQFR CCCEEEHHCCCHHHH	2.75	-
194	S-nitrosylation	TNRWFLTCINQPQFR CCCEEEHHCCCHHHH	2.75	22178444
194	S-palmitoylation	TNRWFLTCINQPQFR CCCEEEHHCCCHHHH	2.75	29575903
197	Acetylation	WFLTCINQPQFRAVL EEEHHCCCHHHHHHH	17.17	-
197	Ubiquitination	WFLTCINQPQFRAVL EEEHHCCCHHHHHHH	17.17	21890473
208	2-Hydroxyisobutyrylation	RAVLGEVKLCEKMAQ HHHHHHHHHHHHHHH	43.02	-
208	Acetylation	RAVLGEVKLCEKMAQ HHHHHHHHHHHHHHH	43.02	23749302
208	Malonylation	RAVLGEVKLCEKMAQ HHHHHHHHHHHHHHH	43.02	26320211
208	Ubiquitination	RAVLGEVKLCEKMAQ HHHHHHHHHHHHHHH	43.02	21906983
210	Glutathionylation	VLGEVKLCEKMAQFD HHHHHHHHHHHHHCC	3.81	22555962
212	2-Hydroxyisobutyrylation	GEVKLCEKMAQFDAK HHHHHHHHHHHCCHH	38.24	-
212	Acetylation	GEVKLCEKMAQFDAK HHHHHHHHHHHCCHH	38.24	23954790
212	Malonylation	GEVKLCEKMAQFDAK HHHHHHHHHHHCCHH	38.24	26320211
212	Ubiquitination	GEVKLCEKMAQFDAK HHHHHHHHHHHCCHH	38.24	21890473
219	2-Hydroxyisobutyrylation	KMAQFDAKKFAETQP HHHHCCHHHHHHCCC	50.71	-
219	Acetylation	KMAQFDAKKFAETQP HHHHCCHHHHHHCCC	50.71	23236377
219	Ubiquitination	KMAQFDAKKFAETQP HHHHCCHHHHHHCCC	50.71	21906983
220	Acetylation	MAQFDAKKFAETQPK HHHCCHHHHHHCCCC	52.07	25953088
220	Ubiquitination	MAQFDAKKFAETQPK HHHCCHHHHHHCCCC	52.07	21906983
224	Phosphorylation	DAKKFAETQPKKDTP CHHHHHHCCCCCCCC	46.90	26270265
227	2-Hydroxyisobutyrylation	KFAETQPKKDTPRKE HHHHCCCCCCCCCCC	54.16	-
230	Phosphorylation	ETQPKKDTPRKEKGS HCCCCCCCCCCCCCC	33.59	17081983
253	Acetylation	AERKEEKKAAAPAPE HHHHHHHHHCCCCCH	46.68	26051181
253	Sumoylation	AERKEEKKAAAPAPE HHHHHHHHHCCCCCH	46.68	25114211
253	Ubiquitination	AERKEEKKAAAPAPE HHHHHHHHHCCCCCH	46.68	-
258	Acetylation	EKKAAAPAPEEEMDE HHHHCCCCCHHHHHH	21.29	-
258	Ubiquitination	EKKAAAPAPEEEMDE HHHHCCCCCHHHHHH	21.29	-
262	Acetylation	AAPAPEEEMDECEQA CCCCCHHHHHHHHHH	50.72	-
262	Ubiquitination	AAPAPEEEMDECEQA CCCCCHHHHHHHHHH	50.72	21890473
263	Sulfoxidation	APAPEEEMDECEQAL CCCCHHHHHHHHHHH	6.26	28465586
266	Glutathionylation	PEEEMDECEQALAAE CHHHHHHHHHHHHHC	4.02	22555962
266	S-palmitoylation	PEEEMDECEQALAAE CHHHHHHHHHHHHHC	4.02	21044946
269	Acetylation	EMDECEQALAAEPKA HHHHHHHHHHHCCCC	4.11	-
269	Ubiquitination	EMDECEQALAAEPKA HHHHHHHHHHHCCCC	4.11	-
270	Ubiquitination	MDECEQALAAEPKAK HHHHHHHHHHCCCCC	4.66	-
275	Acetylation	QALAAEPKAKDPFAH HHHHHCCCCCCCCCC	60.62	26051181
275	Malonylation	QALAAEPKAKDPFAH HHHHHCCCCCCCCCC	60.62	26320211
275	Ubiquitination	QALAAEPKAKDPFAH HHHHHCCCCCCCCCC	60.62	-
277	2-Hydroxyisobutyrylation	LAAEPKAKDPFAHLP HHHCCCCCCCCCCCC	72.55	-
277	Acetylation	LAAEPKAKDPFAHLP HHHCCCCCCCCCCCC	72.55	26051181
277	Malonylation	LAAEPKAKDPFAHLP HHHCCCCCCCCCCCC	72.55	26320211
277	Ubiquitination	LAAEPKAKDPFAHLP HHHCCCCCCCCCCCC	72.55	-
285	2-Hydroxyisobutyrylation	DPFAHLPKSTFVLDE CCCCCCCCCCEEHHH	69.37	-
285	Acetylation	DPFAHLPKSTFVLDE CCCCCCCCCCEEHHH	69.37	23954790
285	Sumoylation	DPFAHLPKSTFVLDE CCCCCCCCCCEEHHH	69.37	28112733
285	Ubiquitination	DPFAHLPKSTFVLDE CCCCCCCCCCEEHHH	69.37	21906983
286	Phosphorylation	PFAHLPKSTFVLDEF CCCCCCCCCEEHHHH	25.74	20068231
287	Phosphorylation	FAHLPKSTFVLDEFK CCCCCCCCEEHHHHH	24.72	30622161
294	2-Hydroxyisobutyrylation	TFVLDEFKRKYSNED CEEHHHHHHHCCCCC	46.03	-
294	Acetylation	TFVLDEFKRKYSNED CEEHHHHHHHCCCCC	46.03	23749302
294	Ubiquitination	TFVLDEFKRKYSNED CEEHHHHHHHCCCCC	46.03	21906983
296	Acetylation	VLDEFKRKYSNEDTL EHHHHHHHCCCCCCH	54.33	23236377
297	Phosphorylation	LDEFKRKYSNEDTLS HHHHHHHCCCCCCHH	22.29	28450419
298	Phosphorylation	DEFKRKYSNEDTLSV HHHHHHCCCCCCHHH	36.46	22617229
302	Phosphorylation	RKYSNEDTLSVALPY HHCCCCCCHHHHHHH	18.11	28450419
303	Ubiquitination	KYSNEDTLSVALPYF HCCCCCCHHHHHHHH	6.32	-
304	Phosphorylation	YSNEDTLSVALPYFW CCCCCCHHHHHHHHH	13.87	28450419
309	Phosphorylation	TLSVALPYFWEHFDK CHHHHHHHHHHHCCC	23.36	20873877
327	Ubiquitination	SLWYSEYRFPEELTQ EEEEEEECCCHHHHH	36.27	-
333	Phosphorylation	YRFPEELTQTFMSCN ECCCHHHHHHHHHHH	28.92	24043423
335	Acetylation	FPEELTQTFMSCNLI CCHHHHHHHHHHHHH	18.97	-
335	Ubiquitination	FPEELTQTFMSCNLI CCHHHHHHHHHHHHH	18.97	21890473
335	Phosphorylation	FPEELTQTFMSCNLI CCHHHHHHHHHHHHH	18.97	24043423
338	Phosphorylation	ELTQTFMSCNLITGM HHHHHHHHHHHHHHH	8.82	24043423
343	Phosphorylation	FMSCNLITGMFQRLD HHHHHHHHHHHHHHH	26.26	24043423
344	Acetylation	MSCNLITGMFQRLDK HHHHHHHHHHHHHHH	14.12	-
344	Ubiquitination	MSCNLITGMFQRLDK HHHHHHHHHHHHHHH	14.12	21890473
346	Acetylation	CNLITGMFQRLDKLR HHHHHHHHHHHHHHH	3.96	-
387	Phosphorylation	QELAFPLSPDWQVDY EEEEEECCCCCEEEH	22.50	30624053
401	Acetylation	YESYTWRKLDPGSEE HHEEEEEECCCCCHH	49.13	21466224
401	Malonylation	YESYTWRKLDPGSEE HHEEEEEECCCCCHH	49.13	26320211
401	Ubiquitination	YESYTWRKLDPGSEE HHEEEEEECCCCCHH	49.13	2190698
406	Phosphorylation	WRKLDPGSEETQTLV EEECCCCCHHHHHHH	37.33	20363803
409	Phosphorylation	LDPGSEETQTLVREY CCCCCHHHHHHHHHH	23.85	20068231
411	Phosphorylation	PGSEETQTLVREYFS CCCHHHHHHHHHHCC	34.34	20068231
416	Phosphorylation	TQTLVREYFSWEGAF HHHHHHHHCCHHHHH	7.73	28152594
418	Phosphorylation	TLVREYFSWEGAFQH HHHHHHCCHHHHHHH	24.26	28152594
428	2-Hydroxyisobutyrylation	GAFQHVGKAFNQGKI HHHHHHHHHHHCCCC	49.03	-
428	Acetylation	GAFQHVGKAFNQGKI HHHHHHHHHHHCCCC	49.03	26051181
428	Ubiquitination	GAFQHVGKAFNQGKI HHHHHHHHHHHCCCC	49.03	21890473
434	N6-malonyllysine	GKAFNQGKIFK---- HHHHHCCCCCC----	34.89	-
434	Acetylation	GKAFNQGKIFK---- HHHHHCCCCCC----	34.89	19608861
434	Malonylation	GKAFNQGKIFK---- HHHHHCCCCCC----	34.89	26320211
434	Ubiquitination	GKAFNQGKIFK---- HHHHHCCCCCC----	34.89	19608861
437	Acetylation	FNQGKIFK------- HHCCCCCC-------	64.00	11922523
451	Acetylation	--------------------- ---------------------		-
451	Ubiquitination	--------------------- ---------------------		21890473
478	Ubiquitination	------------------------------------------------ ------------------------------------------------		21890473
484	Acetylation	------------------------------------------------------ ------------------------------------------------------		-
484	Malonylation	------------------------------------------------------ ------------------------------------------------------		-
484	Ubiquitination	------------------------------------------------------ ------------------------------------------------------		-
487	Ubiquitination	--------------------------------------------------------- ---------------------------------------------------------		-

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
Oops, there are no upstream regulatory protein records of EF1G_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EF1G_HUMAN !!

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 EF1G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ILF2_HUMAN	ILF2	physical	16189514
ABCC9_HUMAN	ABCC9	physical	16189514
EF1G_HUMAN	EEF1G	physical	10094407
MED31_HUMAN	MED31	physical	16169070
ECH1_HUMAN	ECH1	physical	16169070
RECQ5_HUMAN	RECQL5	physical	16169070
EF1B_HUMAN	EEF1B2	physical	16169070
EF1D_HUMAN	EEF1D	physical	16169070
SYLC_HUMAN	LARS	physical	11829477
SYHC_HUMAN	HARS	physical	11829477
EF1G_HUMAN	EEF1G	physical	15383276
GA45G_HUMAN	GADD45G	physical	15383276
RL5_HUMAN	RPL5	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
ROA3_HUMAN	HNRNPA3	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
SRSF9_HUMAN	SRSF9	physical	22939629
PLOD3_HUMAN	PLOD3	physical	22939629
FLNC_HUMAN	FLNC	physical	22939629
STRP1_HUMAN	STRIP1	physical	22939629
TCPG_HUMAN	CCT3	physical	22863883
EF1D_HUMAN	EEF1D	physical	22863883
SYVC_HUMAN	VARS	physical	22863883
ILF2_HUMAN	ILF2	physical	25416956
RBM6_HUMAN	RBM6	physical	25416956
KLH18_HUMAN	KLHL18	physical	25416956
PLRKT_HUMAN	PLGRKT	physical	25416956
KTN1_HUMAN	KTN1	physical	26186194
SYVC_HUMAN	VARS	physical	26186194
SHIP2_HUMAN	INPPL1	physical	26186194
EF1B_HUMAN	EEF1B2	physical	26186194
EF1D_HUMAN	EEF1D	physical	26186194
SYCC_HUMAN	CARS	physical	26186194
EF1A2_HUMAN	EEF1A2	physical	26186194
EF1A1_HUMAN	EEF1A1	physical	26186194
MKKS_HUMAN	MKKS	physical	26186194
EF1B_HUMAN	EEF1B2	physical	26344197
IPO4_HUMAN	IPO4	physical	26344197
PR38B_HUMAN	PRPF38B	physical	26344197
KLH18_HUMAN	KLHL18	physical	21516116
EF1A2_HUMAN	EEF1A2	physical	28514442
MKKS_HUMAN	MKKS	physical	28514442
SYCC_HUMAN	CARS	physical	28514442
EF1D_HUMAN	EEF1D	physical	28514442
SYVC_HUMAN	VARS	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
EF1A1_HUMAN	EEF1A1	physical	28514442
EF1B_HUMAN	EEF1B2	physical	28514442
KTN1_HUMAN	KTN1	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 EF1G_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-132; LYS-147 AND LYS-434,AND MASS SPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-434.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-434.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"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-46, AND MASSSPECTROMETRY.	18669648 [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-43, AND MASSSPECTROMETRY.	17081983 [Abstract]