4EBP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: 4EBP2_MOUSE
• UniProt AC: P70445
• Protein Name: Eukaryotic translation initiation factor 4E-binding protein 2 {ECO:0000250|UniProtKB:Q13542}
• Gene Name: Eif4ebp2 {ECO:0000312|MGI:MGI:109198}
• Organism: Mus musculus (Mouse).
• Sequence Length: 120
• Protein Description: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation. [PubMed: 16237163]
• Protein Sequence: MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI

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	Phosphorylation	------MSASAGGSH ------CCCCCCCCC	30.82	26824392
4	Phosphorylation	----MSASAGGSHQP ----CCCCCCCCCCC	21.82	23072113
8	Phosphorylation	MSASAGGSHQPSQSR CCCCCCCCCCCCCCC	20.31	22345495
12	Phosphorylation	AGGSHQPSQSRAIPT CCCCCCCCCCCCCCC	33.93	28059163
19	Phosphorylation	SQSRAIPTRTVAISD CCCCCCCCCEEEEHH	32.62	28059163
21	Phosphorylation	SRAIPTRTVAISDAA CCCCCCCEEEEHHHH	19.43	27087446
25	Phosphorylation	PTRTVAISDAAQLPQ CCCEEEEHHHHHCCC	16.09	23737553
34	Phosphorylation	AAQLPQDYCTTPGGT HHHCCCCCCCCCCCC	6.10	27087446
36	Phosphorylation	QLPQDYCTTPGGTLF HCCCCCCCCCCCCEE	29.78	27087446
37	Phosphorylation	LPQDYCTTPGGTLFS CCCCCCCCCCCCEEE	19.17	25521595
41	Phosphorylation	YCTTPGGTLFSTTPG CCCCCCCCEEECCCC	30.46	27087446
44	Phosphorylation	TPGGTLFSTTPGGTR CCCCCEEECCCCCCE	34.19	25521595
45	Phosphorylation	PGGTLFSTTPGGTRI CCCCEEECCCCCCEE	29.67	27087446
46	Phosphorylation	GGTLFSTTPGGTRII CCCEEECCCCCCEEE	20.81	25521595
50	Phosphorylation	FSTTPGGTRIIYDRK EECCCCCCEEEEECC	25.30	27087446
54	Phosphorylation	PGGTRIIYDRKFLLD CCCCEEEEECCHHHH	13.81	27087446
65	Phosphorylation	FLLDRRNSPMAQTPP HHHHCCCCCCCCCCC	17.78	25521595
70	Phosphorylation	RNSPMAQTPPCHLPN CCCCCCCCCCCCCCC	21.47	25521595
82	Phosphorylation	LPNIPGVTSPGALIE CCCCCCCCCCCCEEC	34.81	25619855
83	Phosphorylation	PNIPGVTSPGALIED CCCCCCCCCCCEECC	20.94	25619855
91	Phosphorylation	PGALIEDSKVEVNNL CCCEECCCCEECCCC	26.30	25619855
99	Deamidated asparagine	KVEVNNLNNLNNHDR CEECCCCCCCCCCCC	53.73	-
99	Deamidation	KVEVNNLNNLNNHDR CEECCCCCCCCCCCC	53.73	20347422
102	Deamidation	VNNLNNLNNHDRKHA CCCCCCCCCCCCHHC	46.01	20347422
102	Deamidated asparagine	VNNLNNLNNHDRKHA CCCCCCCCCCCCHHC	46.01	-

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
37	T	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot
41	T	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP
46	T	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot
65	S	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot
70	T	Phosphorylation	Kinase	MTOR	Q9JLN9	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
18	P	Phosphorylation	First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E.	24139800
37	T	Phosphorylation	First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E.	21183079
37	T	Phosphorylation	Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions.	21183079
37	T	Phosphorylation	Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000.	21183079
46	T	Phosphorylation	First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E.	21183079
46	T	Phosphorylation	Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions.	21183079
46	T	Phosphorylation	Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000.	21183079
62	R	Phosphorylation	First phosphorylated at Thr-37 and Thr-46 by MTOR, inducing folding of region encompassing residues from Pro-18 to Arg-62 of into a four-stranded beta-domain that sequesters the helical YXXXXLPhi motif into a partly buried beta-strand, blocking accessibility to EIF4E.	24139800
65	S	Phosphorylation	Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions.	21183079
65	S	Phosphorylation	Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000.	21183079
70	T	Phosphorylation	Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions.	21183079
70	T	Phosphorylation	Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000.	21183079
83	S	Phosphorylation	Phosphorylation at Thr-37, Thr-46, Ser-65, Thr-70 and Ser-83 is mediated by MTOR and corresponds to the hyperphosphorylated form: it abolishes binding to EIF4E by inducing folding of intrinsically disordered regions.	24139800
83	S	Phosphorylation	Protein phosphorylated at Thr-37 and Thr-46 is however unstable and subsequent phosphorylation at Ser-65, Thr-70 and Ser-83 is required to stabilize the fold, decreasing affinity for EIF4E by a factor of 4000.	24139800
99	N	Amidation	Deamidated at Asn-99 and Asn-102 to aspartate (Asp) in brain.	20424163
102	N	Amidation	Deamidated at Asn-99 and Asn-102 to aspartate (Asp) in brain.	20424163

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of 4EBP2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of 4EBP2_MOUSE !!

Drug and Disease Associations

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