dbPTM

EF1A2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1A2_MOUSE
UniProt AC	P62631
Protein Name	Elongation factor 1-alpha 2
Gene Name	Eef1a2
Organism	Mus musculus (Mouse).
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	MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKKIGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDIRRGNVCGDSKADPPQEAAQFTSQVIILNHPGQISAGYSPVIDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPPLGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK

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	69031
30	Ubiquitination	TTGHLIYKCGGIDKR CCCEEEEECCCCCHH	21.29	-
36	Methylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
36	Acetylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	69035
41	Acetylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	69039
41	Ubiquitination	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	27667366
44	Acetylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	90425
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	27667366
55	"N6,N6,N6-trimethyllysine"	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
55	Methylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
79	Methylation	TIDISLWKFETTKYY EEEEEEEEEECCEEE	38.32	-
79	"N6,N6,N6-trimethyllysine"	TIDISLWKFETTKYY EEEEEEEEEECCEEE	38.32	-
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	Ubiquitination	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	-
154	Ubiquitination	QLIVGVNKMDSTEPA EEEECCCCCCCCCCC	41.50	22790023
163	Phosphorylation	DSTEPAYSEKRYDEI CCCCCCCCHHHHHHH	38.45	28464351
165	Ubiquitination	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	22790023
165	"N6,N6,N6-trimethyllysine"	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	-
165	Methylation	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	-
172	Ubiquitination	KRYDEIVKEVSAYIK HHHHHHHHHHHHHHH	59.04	22790023
177	Phosphorylation	IVKEVSAYIKKIGYN HHHHHHHHHHHHCCC	13.03	28464351
179	Acetylation	KEVSAYIKKIGYNPA HHHHHHHHHHCCCCC	26.18	-
179	Ubiquitination	KEVSAYIKKIGYNPA HHHHHHHHHHCCCCC	26.18	27667366
219	Ubiquitination	KGWKVERKEGNASGV CCEEEEEECCCCCCH	57.37	22790023
224	Phosphorylation	ERKEGNASGVSLLEA EEECCCCCCHHHHHH	43.67	22210690
227	Phosphorylation	EGNASGVSLLEALDT CCCCCCHHHHHHHHH	30.66	22210690
254	Phosphorylation	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	28066266
255	Ubiquitination	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	27667366
255	Acetylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	22643115
261	Phosphorylation	YKIGGIGTVPVGRVE EEECCCEEEECCEEE	21.51	26643407
286	Phosphorylation	TFAPVNITTEVKSVE EEECCCEEEEEEEEE	16.23	19854140
291	Phosphorylation	NITTEVKSVEMHHEA CEEEEEEEEEHHHHH	28.61	30387612
300	Phosphorylation	EMHHEALSEALPGDN EHHHHHHHHHCCCCC	28.07	25890499
301	Formation of an isopeptide bond	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
301	5-glutamyl glycerylphosphorylethanolamine	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
374	Formation of an isopeptide bond	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
374	5-glutamyl glycerylphosphorylethanolamine	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
386	Ubiquitination	IDRRSGKKLEDNPKS HHHHCCCCCCCCCCC	61.71	22790023
392	Ubiquitination	KKLEDNPKSLKSGDA CCCCCCCCCCCCCCE	74.75	22790023
411	S-palmitoylation	MVPGKPMCVESFSQY ECCCCCEEECCHHHC	4.10	28680068
411	S-nitrosylation	MVPGKPMCVESFSQY ECCCCCEEECCHHHC	4.10	21278135
411	S-nitrosocysteine	MVPGKPMCVESFSQY ECCCCCEEECCHHHC	4.10	-
416	Phosphorylation	PMCVESFSQYPPLGR CEEECCHHHCCCCCC	37.78	-
418	Phosphorylation	CVESFSQYPPLGRFA EECCHHHCCCCCCHH	12.96	-
432	Phosphorylation	AVRDMRQTVAVGVIK HHCCHHHHEEEEEEE	10.48	21183079
439	Ubiquitination	TVAVGVIKNVEKKSG HEEEEEEECCEECCC	53.16	22790023
439	Acetylation	TVAVGVIKNVEKKSG HEEEEEEECCEECCC	53.16	-
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
Oops, there are no upstream regulatory protein records of EF1A2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
36	K	Methylation	-
Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant.
55	K	Methylation	-
Trimethylated at the N-terminus and dimethylated at Lys-55 by EEF1AKNMT.
165	K	Methylation	-
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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLCB1_RAT	Plcb1	physical	23665500
SRSF3_MOUSE	Srsf3	physical	23665500
PHB2_MOUSE	Phb2	physical	23665500

Drug and Disease Associations

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

Regulatory Network of EF1A2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-141, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND MASSSPECTROMETRY.	17947660 [Abstract]

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