IF2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF2A_MOUSE
• UniProt AC: Q6ZWX6
• Protein Name: Eukaryotic translation initiation factor 2 subunit 1
• Gene Name: Eif2s1
• Organism: Mus musculus (Mouse).
• 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 (By similarity)..
• 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
35	Phosphorylation	AEMGAYVSLLEYNNI HHHCCEEEEEHCCCC	17.98	27600695
49	Phosphorylation	IEGMILLSELSRRRI CCHHHHHHHHHHHHH	32.80	-
52	Phosphorylation	MILLSELSRRRIRSI HHHHHHHHHHHHHHH	21.49	19081072
54	Methylation	LLSELSRRRIRSINK HHHHHHHHHHHHHHH	34.69	-
55	Methylation	LSELSRRRIRSINKL HHHHHHHHHHHHHHH	27.80	-
61	Ubiquitination	RRIRSINKLIRIGRN HHHHHHHHHHHCCCC	43.55	27667366
61	Malonylation	RRIRSINKLIRIGRN HHHHHHHHHHHCCCC	43.55	26320211
70	S-nitrosocysteine	IRIGRNECVVVIRVD HHCCCCCEEEEEEEE	3.00	-
70	S-nitrosylation	IRIGRNECVVVIRVD HHCCCCCEEEEEEEE	3.00	20925432
80	Ubiquitination	VIRVDKEKGYIDLSK EEEEECCCCEEECCC	63.86	27667366
82	Phosphorylation	RVDKEKGYIDLSKRR EEECCCCEEECCCCC	11.43	25367039
91	Phosphorylation	DLSKRRVSPEEAIKC ECCCCCCCHHHHHCC	25.45	26824392
101	Ubiquitination	EAIKCEDKFTKSKTV HHHCCCHHCCCHHHH	32.41	22790023
104	Ubiquitination	KCEDKFTKSKTVYSI CCCHHCCCHHHHHHH	53.76	-
106	Acetylation	EDKFTKSKTVYSILR CHHCCCHHHHHHHHH	43.49	22826441
106	Ubiquitination	EDKFTKSKTVYSILR CHHCCCHHHHHHHHH	43.49	22790023
110	Phosphorylation	TKSKTVYSILRHVAE CCHHHHHHHHHHHHH	15.71	26643407
123	Acetylation	AEVLEYTKDEQLESL HHHHHHCCHHHHHHH	59.37	23954790
141	Ubiquitination	TAWVFDDKYKRPGYG HHHHCCCCCCCCCCC	55.29	22790023
141	Acetylation	TAWVFDDKYKRPGYG HHHHCCCCCCCCCCC	55.29	22826441
142	Phosphorylation	AWVFDDKYKRPGYGA HHHCCCCCCCCCCCH	21.15	25367039
143	Ubiquitination	WVFDDKYKRPGYGAY HHCCCCCCCCCCCHH	58.83	27667366
147	Phosphorylation	DKYKRPGYGAYDAFK CCCCCCCCCHHHHHH	10.98	25367039
150	Phosphorylation	KRPGYGAYDAFKHAV CCCCCCHHHHHHHHC	11.93	25367039
158	Phosphorylation	DAFKHAVSDPSILDS HHHHHHCCCHHHHHC	44.58	26239621
161	Phosphorylation	KHAVSDPSILDSLDL HHHCCCHHHHHCCCC	40.55	21149613
165	Phosphorylation	SDPSILDSLDLNEDE CCHHHHHCCCCCHHH	21.97	26370283
185	Phosphorylation	NNINRRLTPQAVKIR HHHHCCCCCCCEEEC	16.14	27149854
218	Glutathionylation	ALRAGLNCSTETMPI HHHCCCCCCCCCCCE	6.82	24333276
218	S-nitrosylation	ALRAGLNCSTETMPI HHHCCCCCCCCCCCE	6.82	20925432
218	S-nitrosocysteine	ALRAGLNCSTETMPI HHHCCCCCCCCCCCE	6.82	-
259	Acetylation	NQAMAVIKEKIEEKR HHHHHHHHHHHHHHC	46.48	22826441
259	Ubiquitination	NQAMAVIKEKIEEKR HHHHHHHHHHHHHHC	46.48	22790023
279	Phosphorylation	QMEPKVVTDTDETEL EECCEEECCCCHHHH	35.85	30352176
281	Phosphorylation	EPKVVTDTDETELAR CCEEECCCCHHHHHH	26.77	28066266

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	Q9Z2R9	Uniprot
52	S	Phosphorylation	Kinase	EIF2AK2	Q03963	GPS
52	S	Phosphorylation	Kinase	EIF2AK3	Q9Z2B5	GPS
52	S	Phosphorylation	Kinase	EIF2AK4	Q9QZ05	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.	10504407
52	S	Phosphorylation	Phosphorylated; phosphorylation on Ser-52 by the EIF2AK4/GCN2 protein kinase occurs in response to amino acid starvation and UV irradiation.	10504407
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.	10504407

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of IF2A_MOUSE !!

Drug and Disease Associations

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