EF1A1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EF1A1_RAT
• UniProt AC: P62630
• Protein Name: Elongation factor 1-alpha 1
• Gene Name: Eef1a1
• Organism: Rattus norvegicus (Rat).
• 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

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	"N6,N6,N6-trimethyllysine"	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
36	Methylation	YKCGGIDKRTIEKFE EECCCCCHHHHHHHH	49.90	-
41	Acetylation	IDKRTIEKFEKEAAE CCHHHHHHHHHHHHH	55.78	22902405
44	Acetylation	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	149239
44	Ubiquitination	RTIEKFEKEAAEMGK HHHHHHHHHHHHCCC	56.64	-
53	Phosphorylation	AAEMGKGSFKYAWVL HHHCCCCCEEHHHHH	23.27	28432305
55	"N6,N6-dimethyllysine"	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
55	Methylation	EMGKGSFKYAWVLDK HCCCCCEEHHHHHHH	35.44	-
79	"N6,N6,N6-trimethyllysine"	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	-
79	Methylation	TIDISLWKFETSKYY EEEEEEEEEECCCEE	38.32	-
141	Phosphorylation	REHALLAYTLGVKQL HHHHHHHHHHCCCEE	11.49	29779826
142	Phosphorylation	EHALLAYTLGVKQLI HHHHHHHHHCCCEEE	16.07	27097102
146	Acetylation	LAYTLGVKQLIVGVN HHHHHCCCEEEECCC	37.27	22902405
154	Acetylation	QLIVGVNKMDSTEPP EEEECCCCCCCCCCC	41.50	22902405
163	Phosphorylation	DSTEPPYSQKRYEEI CCCCCCCCHHHHHHH	34.69	30181290
165	Methylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	-
165	"N6,N6-dimethyllysine"	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	-
165	Acetylation	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	22902405
165	Ubiquitination	TEPPYSQKRYEEIVK CCCCCCHHHHHHHHH	51.51	-
172	Acetylation	KRYEEIVKEVSTYIK HHHHHHHHHHHHHHH	59.04	149153
175	Phosphorylation	EEIVKEVSTYIKKIG HHHHHHHHHHHHHHC	19.31	28689409
176	Phosphorylation	EIVKEVSTYIKKIGY HHHHHHHHHHHHHCC	34.15	25575281
177	Phosphorylation	IVKEVSTYIKKIGYN HHHHHHHHHHHHCCC	11.84	28689409
179	Acetylation	KEVSTYIKKIGYNPD HHHHHHHHHHCCCCC	28.11	25786129
194	Phosphorylation	TVAFVPISGWNGDNM CEEEEECCCCCCCCC	31.52	22673903
205	Phosphorylation	GDNMLEPSANMPWFK CCCCCCCCCCCCCCC	23.93	22673903
215	Acetylation	MPWFKGWKVTRKDGS CCCCCCEEEEECCCC	42.25	72609859
219	Succinylation	KGWKVTRKDGSASGT CCEEEEECCCCCCCC	58.01	26843850
222	Phosphorylation	KVTRKDGSASGTTLL EEEECCCCCCCCHHH	29.42	23984901
224	Phosphorylation	TRKDGSASGTTLLEA EECCCCCCCCHHHHH	38.07	23984901
226	Phosphorylation	KDGSASGTTLLEALD CCCCCCCCHHHHHHH	16.27	23984901
227	Phosphorylation	DGSASGTTLLEALDC CCCCCCCHHHHHHHH	32.63	23984901
239	Phosphorylation	LDCILPPTRPTDKPL HHHHCCCCCCCCCCC	47.55	30181290
242	Phosphorylation	ILPPTRPTDKPLRLP HCCCCCCCCCCCCCC	54.05	30181290
244	Ubiquitination	PPTRPTDKPLRLPLQ CCCCCCCCCCCCCHH	48.72	-
254	Phosphorylation	RLPLQDVYKIGGIGT CCCHHHEEEECCCEE	12.74	27097102
255	Acetylation	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	22902405
255	Ubiquitination	LPLQDVYKIGGIGTV CCHHHEEEECCCEEE	34.42	-
273	Succinylation	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	26843850
273	Ubiquitination	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	-
273	Acetylation	RVETGVLKPGMVVTF EEECCCCCCCEEEEE	36.80	22902405
300	Phosphorylation	EMHHEALSEALPGDN EHHHHHHHHHCCCCC	28.07	-
301	Formation of an isopeptide bond	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
301	5-glutamyl glycerylphosphorylethanolamine	MHHEALSEALPGDNV HHHHHHHHHCCCCCC	55.89	-
318	"N6,N6,N6-trimethyllysine"	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	-
318	Methylation	NVKNVSVKDVRRGNV EEEECCHHHHHCCCC	42.89	-
374	Formation of an isopeptide bond	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
374	5-glutamyl glycerylphosphorylethanolamine	HIACKFAELKEKIDR HHHHHHHHHHHHHHH	64.60	-
386	Succinylation	IDRRSGKKLEDGPKF HHHCCCCCCCCCCCH	61.71	26843850
386	Acetylation	IDRRSGKKLEDGPKF HHHCCCCCCCCCCCH	61.71	72605859
392	Succinylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	-
392	Succinylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	-
392	Acetylation	KKLEDGPKFLKSGDA CCCCCCCCHHCCCCE	69.71	22902405
408	Ubiquitination	IVDMVPGKPMCVESF EEECCCCCEEEEEEC	24.41	-
432	Phosphorylation	AVRDMRQTVAVGVIK HHHCHHHHHHHEEEE	10.48	-
439	Ubiquitination	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	-
439	Acetylation	TVAVGVIKAVDKKAA HHHHEEEEECCHHHC	39.69	25786129
450	Ubiquitination	KKAAGAGKVTKSAQK HHHCCCCCCCHHHHH	46.31	-

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	P80204	Uniprot
432	T	Phosphorylation	Kinase	PASK	O88506	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	G	Methylation	Trimethylated at Gly-2 by EEF1AKNMT.	-
36	K	Methylation	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	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	Trimethylated at Lys-318 by EEF1AKMT2.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EF1A1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EF1A1_RAT !!

Drug and Disease Associations

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