IF2A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF2A_RAT
• UniProt AC: P68101
• Protein Name: Eukaryotic translation initiation factor 2 subunit 1
• Gene Name: Eif2s1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 315
• Subcellular Localization: Cytoplasm, Stress granule . Colocalizes with NANOS3 in the stress granules.
• Protein Description: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B..
• Protein Sequence: MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTETMPIKINLIAPPRYVMTTTTLERTEGLSVLNQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQLERLERENAEVDGDDDAEEMEAKAED

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
49	Phosphorylation	IEGMILLSELSRRRI CCHHHHHHHHHHHHH	32.80	-
52	Phosphorylation	MILLSELSRRRIRSI HHHHHHHHHHHHHHH	21.49	19004820
107	Phosphorylation	DKFTKSKTVYSILRH HHCCCHHHHHHHHHH	31.59	30181290
109	Phosphorylation	FTKSKTVYSILRHVA CCCHHHHHHHHHHHH	8.67	30181290
110	Phosphorylation	TKSKTVYSILRHVAE CCHHHHHHHHHHHHH	15.71	23984901
141	Acetylation	TAWVFDDKYKRPGYG HHHHCCCCCCCCCCC	55.29	22902405
158	Phosphorylation	DAFKHAVSDPSILDS HHHHHHCCCHHHHHC	44.58	27097102
161	Phosphorylation	KHAVSDPSILDSLDL HHHCCCHHHHHCCCC	40.55	27097102
165	Phosphorylation	SDPSILDSLDLNEDE CCHHHHHCCCCCHHH	21.97	27097102
279	Phosphorylation	QMEPKVVTDTDETEL EECCEEECCCCHHHH	35.85	-
281	Phosphorylation	EPKVVTDTDETELAR CCEEECCCCHHHHHH	26.77	-

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
49	S	Phosphorylation	Kinase	HRI	Q63185	Uniprot
52	S	Phosphorylation	Kinase	EIF2AK1	Q9BQI3	GPS
52	S	Phosphorylation	Kinase	EIF2AK2	P19525	GPS
52	S	Phosphorylation	Kinase	EIF2AK3	Q9Z1Z1	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
49	S	Phosphorylation	Phosphorylation at Ser-49 and Ser-52 stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation, while concomitantly initiating the preferential translation of integrated stress response (ISR)-specific mRNAs (By similarity).	-
52	S	Phosphorylation	Phosphorylated; phosphorylation on Ser-52 by the EIF2AK4/GCN2 protein kinase occurs in response to amino acid starvation and UV irradiation (By similarity).	-
52	S	Phosphorylation	Phosphorylation at Ser-49 and Ser-52 stabilizes the eIF-2/GDP/eIF-2B complex and prevents GDP/GTP exchange reaction, thus impairing the recycling of eIF-2 between successive rounds of initiation and leading to global inhibition of translation, while concomitantly initiating the preferential translation of integrated stress response (ISR)-specific mRNAs (By similarity).	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IF2A_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of IF2A_RAT !!

Drug and Disease Associations

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