EF1A2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EF1A2_RAT
• UniProt AC: P62632
• Protein Name: Elongation factor 1-alpha 2
• Gene Name: Eef1a2
• Organism: Rattus norvegicus (Rat).
• 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

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MGKEKTHIN ------CCCCCCEEE	46.99	-
23	Phosphorylation	VDSGKSTTTGHLIYK CCCCCCCCCCEEEEE	37.56	-
24	Phosphorylation	DSGKSTTTGHLIYKC CCCCCCCCCEEEEEC	23.77	-
29	Phosphorylation	TTTGHLIYKCGGIDK CCCCEEEEECCCCCH	13.44	25532521
36	Methylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
41	Acetylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	149079
44	Acetylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	149225
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	-
53	Phosphorylation	AAEMGKGSFKYAWVL HHHCCCCCEEHHHHH	23.27	28432305
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	-
141	Phosphorylation	REHALLAYTLGVKQL HHHHHHHHHHCCCEE	11.49	29779826
142	Phosphorylation	EHALLAYTLGVKQLI HHHHHHHHHCCCEEE	16.07	27097102
146	Acetylation	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	149081
165	"N6,N6,N6-trimethyllysine"	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	-
165	Methylation	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	-
165	Acetylation	TEPAYSEKRYDEIVK CCCCCCHHHHHHHHH	50.77	22902405
172	Acetylation	KRYDEIVKEVSAYIK HHHHHHHHHHHHHHH	59.04	22902405
177	Phosphorylation	IVKEVSAYIKKIGYN HHHHHHHHHHHHCCC	13.03	-
179	Acetylation	KEVSAYIKKIGYNPA HHHHHHHHHHCCCCC	26.18	22902405
180	Acetylation	EVSAYIKKIGYNPAT HHHHHHHHHCCCCCC	31.63	26302492
215	Acetylation	MPWFKGWKVERKEGN CCCCCCEEEEEECCC	42.77	22902405
224	Phosphorylation	ERKEGNASGVSLLEA EEECCCCCCHHHHHH	43.67	22673903
244	Ubiquitination	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	-
254	Phosphorylation	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	27097102
255	Ubiquitination	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
255	Acetylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	22643113
301	Formation of an isopeptide bond	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
301	5-glutamyl glycerylphosphorylethanolamine	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
374	5-glutamyl glycerylphosphorylethanolamine	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
374	Formation of an isopeptide bond	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
382	Methylation	LKEKIDRRSGKKLED HHHHHHHHCCCCCCC	46.11	-
392	Ubiquitination	KKLEDNPKSLKSGDA CCCCCCCCCCCCCCE	74.75	-
439	Acetylation	TVAVGVIKNVEKKSG HEEEEEEECCEECCC	53.16	22902405
450	Ubiquitination	KKSGGAGKVTKSAQK ECCCCCCCCCHHHHH	46.31	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EF1A2_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	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.

Oops, there are no SNP-PTM records of EF1A2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EF1A2_RAT !!

Drug and Disease Associations

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