dbPTM

EF1A1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1A1_MOUSE
UniProt AC	P10126
Protein Name	Elongation factor 1-alpha 1
Gene Name	Eef1a1
Organism	Mus musculus (Mouse).
Sequence Length	462
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleolus . Cell membrane . Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens. Localization
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	MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGSASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MGKEKTHIN ------CCCCCCEEE	46.99	-
21	Phosphorylation	GHVDSGKSTTTGHLI EECCCCCCCCCCEEE	34.21	22499769
22	Phosphorylation	HVDSGKSTTTGHLIY ECCCCCCCCCCEEEE	31.68	22499769
23	Phosphorylation	VDSGKSTTTGHLIYK CCCCCCCCCCEEEEE	37.56	22499769
24	Phosphorylation	DSGKSTTTGHLIYKC CCCCCCCCCEEEEEC	23.77	22499769
29	Phosphorylation	TTTGHLIYKCGGIDK CCCCEEEEECCCCCH	13.44	25177544
30	Acetylation	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	68967
30	Ubiquitination	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	22790023
36	"N6,N6,N6-trimethyllysine"	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
36	Acetylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	68971
36	Methylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
41	Acetylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	23864654
41	Malonylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	26320211
41	Ubiquitination	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	-
44	Acetylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	23806337
44	Malonylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	26320211
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	-
55	"N6,N6-dimethyllysine"	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
55	Methylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
79	"N6,N6,N6-trimethyllysine"	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	-
79	Acetylation	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	15742316
79	Methylation	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	-
82	Phosphorylation	ISLWKFETSKYYVTI EEEEEEECCCEEEEE	33.38	25367039
83	Phosphorylation	SLWKFETSKYYVTII EEEEEECCCEEEEEE	16.09	25367039
84	Acetylation	LWKFETSKYYVTIID EEEEECCCEEEEEEE	48.28	6569233
85	Phosphorylation	WKFETSKYYVTIIDA EEEECCCEEEEEEEC	11.70	25195567
86	Phosphorylation	KFETSKYYVTIIDAP EEECCCEEEEEEECC	8.54	25367039
128	Phosphorylation	GEFEAGISKNGQTRE CCHHCCCCCCCCCHH	21.10	-
129	Ubiquitination	EFEAGISKNGQTREH CHHCCCCCCCCCHHH	64.28	-
141	Phosphorylation	REHALLAYTLGVKQL HHHHHHHHHHCCCEE	11.49	25521595
142	Phosphorylation	EHALLAYTLGVKQLI HHHHHHHHHCCCEEE	16.07	27742792
146	Acetylation	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	22826441
146	Malonylation	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	26073543
146	Ubiquitination	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	-
154	Acetylation	QLIVGVNKMDSTEPP EEEECCCCCCCCCCC	41.50	22826441
154	Ubiquitination	QLIVGVNKMDSTEPP EEEECCCCCCCCCCC	41.50	22790023
157	Phosphorylation	VGVNKMDSTEPPYSQ ECCCCCCCCCCCCCH	31.04	24899341
163	Phosphorylation	DSTEPPYSQKRYEEI CCCCCCCCHHHHHHH	34.69	25521595
165	"N6,N6-dimethyllysine"	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	-
165	Acetylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	23806337
165	Malonylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	26320211
165	Methylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	28108655
165	Ubiquitination	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	-
166	Dimethylation	EPPYSQKRYEEIVKE CCCCCHHHHHHHHHH	36.14	-
166	Methylation	EPPYSQKRYEEIVKE CCCCCHHHHHHHHHH	36.14	-
172	Acetylation	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	23806337
172	Malonylation	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	26320211
172	Ubiquitination	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	-
175	Phosphorylation	EEIVKEVSTYIKKIG HHHHHHHHHHHHHHC	19.31	25367039
176	Phosphorylation	EIVKEVSTYIKKIGY HHHHHHHHHHHHHCC	34.15	25367039
177	Phosphorylation	IVKEVSTYIKKIGYN HHHHHHHHHHHHCCC	11.84	30352176
179	Acetylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	23864654
179	Malonylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	26320211
179	Succinylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	23806337
180	Ubiquitination	EVSTYIKKIGYNPDT HHHHHHHHHCCCCCC	31.63	22790023
212	Acetylation	SANMPWFKGWKVTRK CCCCCCCCCEEEEEC	61.05	23954790
215	Malonylation	MPWFKGWKVTRKDGS CCCCCCEEEEECCCC	42.25	26073543
219	Malonylation	KGWKVTRKDGSASGT CCEEEEECCCCCCCC	58.01	25418362
219	Ubiquitination	KGWKVTRKDGSASGT CCEEEEECCCCCCCC	58.01	-
222	Phosphorylation	KVTRKDGSASGTTLL EEEECCCCCCCCHHH	29.42	26824392
224	Phosphorylation	TRKDGSASGTTLLEA EECCCCCCCCHHHHH	38.07	26643407
226	Phosphorylation	KDGSASGTTLLEALD CCCCCCCCHHHHHHH	16.27	26643407
227	Phosphorylation	DGSASGTTLLEALDC CCCCCCCHHHHHHHH	32.63	26643407
234	S-nitrosocysteine	TLLEALDCILPPTRP HHHHHHHHHCCCCCC	3.42	-
234	Glutathionylation	TLLEALDCILPPTRP HHHHHHHHHCCCCCC	3.42	24333276
234	S-nitrosylation	TLLEALDCILPPTRP HHHHHHHHHCCCCCC	3.42	24926564
234	S-palmitoylation	TLLEALDCILPPTRP HHHHHHHHHCCCCCC	3.42	28526873
239	Phosphorylation	LDCILPPTRPTDKPL HHHHCCCCCCCCCCC	47.55	23140645
242	Phosphorylation	ILPPTRPTDKPLRLP HCCCCCCCCCCCCCC	54.05	23140645
244	Acetylation	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	23806337
254	Phosphorylation	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	28066266
255	Acetylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	22826441
255	Malonylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	26320211
255	Succinylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
255	Ubiquitination	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
261	Phosphorylation	YKIGGIGTVPVGRVE EEECCCEEEECCEEE	21.51	26643407
269	Phosphorylation	VPVGRVETGVLKPGM EECCEEECCCCCCCE	29.72	22006019
273	Acetylation	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	23806337
273	Malonylation	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	26320211
273	Ubiquitination	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	-
286	Phosphorylation	TFAPVNVTTEVKSVE EEECCCEEEEEEEEE	16.43	-
287	Phosphorylation	FAPVNVTTEVKSVEM EECCCEEEEEEEEEH	34.20	22006019
290	Ubiquitination	VNVTTEVKSVEMHHE CCEEEEEEEEEHHHH	42.42	-
291	Phosphorylation	NVTTEVKSVEMHHEA CEEEEEEEEEHHHHH	28.61	26824392
300	Phosphorylation	EMHHEALSEALPGDN EHHHHHHHHHCCCCC	28.07	26824392
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	-
318	"N6,N6,N6-trimethyllysine"	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	-
318	Methylation	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	-
329	Phosphorylation	RGNVAGDSKNDPPME CCCCCCCCCCCCCHH	32.23	24899341
374	5-glutamyl glycerylphosphorylethanolamine	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
374	Formation of an isopeptide bond	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	2569467
383	Phosphorylation	KEKIDRRSGKKLEDG HHHHHHCCCCCCCCC	56.72	29514104
386	Acetylation	IDRRSGKKLEDGPKF HHHCCCCCCCCCCCH	61.71	22826441
392	Acetylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	23806337
392	Malonylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	26320211
392	Succinylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	-
392	Succinylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	23806337
392	Ubiquitination	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	-
395	Acetylation	EDGPKFLKSGDAAIV CCCCCHHCCCCEEEE	56.37	22826441
395	Malonylation	EDGPKFLKSGDAAIV CCCCCHHCCCCEEEE	56.37	26320211
395	Ubiquitination	EDGPKFLKSGDAAIV CCCCCHHCCCCEEEE	56.37	-
396	Phosphorylation	DGPKFLKSGDAAIVD CCCCHHCCCCEEEEE	44.01	25195567
408	Acetylation	IVDMVPGKPMCVESF EEECCCCCEEEEEEC	24.41	23236377
408	Ubiquitination	IVDMVPGKPMCVESF EEECCCCCEEEEEEC	24.41	22790023
411	S-nitrosocysteine	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	-
411	Glutathionylation	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	24333276
411	S-nitrosylation	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	19101475
411	S-palmitoylation	MVPGKPMCVESFSDY CCCCCEEEEEECCCC	4.10	28526873
414	Phosphorylation	GKPMCVESFSDYPPL CCEEEEEECCCCCCC	15.06	19060867
418	Phosphorylation	CVESFSDYPPLGRFA EEEECCCCCCCCHHH	12.92	19060867
432	Phosphorylation	AVRDMRQTVAVGVIK HHHCHHHHHHHEEEE	10.48	22817900
439	Acetylation	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	23806337
439	Malonylation	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	26320211
439	Ubiquitination	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	-
443	Acetylation	GVIKAVDKKAAGAGK EEEEECCHHHCCCCC	37.40	22826441
452	Phosphorylation	AAGAGKVTKSAQKAQ HCCCCCCCHHHHHHH	23.83	-
454	Phosphorylation	GAGKVTKSAQKAQKA CCCCCCHHHHHHHHC	26.94	22817900

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
300	S	Phosphorylation	Kinase	TGFBR1	Q64729	Uniprot
432	T	Phosphorylation	Kinase	PASK	Q8CEE6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	G	Methylation	28108655
Trimethylated at Gly-2 by EEF1AKNMT.
36	K	Methylation	28108655
Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant.
55	K	Methylation	28108655
Mono- and dimethylated at Lys-55 by EEF1AKNMT; dimethylated form is predominant (By similarity).
79	K	Methylation	28108655
Trimethylated at Lys-79 by EEF1AKMT1 (By similarity).
165	K	Methylation	23806337
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	28108655
Trimethylated at Lys-318 by EEF1AKMT2 (By similarity).

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RGS12_HUMAN	RGS12	physical	17124247
SYCC_HUMAN	CARS	physical	26496610
SYDC_HUMAN	DARS	physical	26496610
EF1B_HUMAN	EEF1B2	physical	26496610
EF1D_HUMAN	EEF1D	physical	26496610
EF1G_HUMAN	EEF1G	physical	26496610
SYEP_HUMAN	EPRS	physical	26496610
GAK_HUMAN	GAK	physical	26496610
TF3B_HUMAN	BRF1	physical	26496610
SYIC_HUMAN	IARS	physical	26496610
KTN1_HUMAN	KTN1	physical	26496610
SYMC_HUMAN	MARS	physical	26496610
PHB_HUMAN	PHB	physical	26496610
SYRC_HUMAN	RARS	physical	26496610
RRBP1_HUMAN	RRBP1	physical	26496610
SOAT1_HUMAN	SOAT1	physical	26496610
SPAG1_HUMAN	SPAG1	physical	26496610
SVIL_HUMAN	SVIL	physical	26496610
TOP2B_HUMAN	TOP2B	physical	26496610
TTC1_HUMAN	TTC1	physical	26496610
SYVC_HUMAN	VARS	physical	26496610
S39A7_HUMAN	SLC39A7	physical	26496610
HERC2_HUMAN	HERC2	physical	26496610
AIMP1_HUMAN	AIMP1	physical	26496610
CP135_HUMAN	CEP135	physical	26496610
ERLN2_HUMAN	ERLIN2	physical	26496610
PHB2_HUMAN	PHB2	physical	26496610
PTHB1_HUMAN	BBS9	physical	26496610
EGFL7_HUMAN	EGFL7	physical	26496610
SYLC_HUMAN	LARS	physical	26496610
VPS29_HUMAN	VPS29	physical	26496610
TRPM7_HUMAN	TRPM7	physical	26496610
ENOX1_HUMAN	ENOX1	physical	26496610

Drug and Disease Associations

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

Regulatory Network of EF1A1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationallymodified by novel amide-linked ethanolamine-phosphoglycerol moieties.Addition of ethanolamine-phosphoglycerol to specific glutamic acidresidues on EF-1 alpha."; Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.; J. Biol. Chem. 264:14334-14341(1989). Cited for: PROTEIN SEQUENCE OF 291-313 AND 372-376, AND ETHANOLAMINYLATION ATGLU-301 AND GLU-374.	2569467 [Abstract]

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