dbPTM

IF4E2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF4E2_HUMAN
UniProt AC	O60573
Protein Name	Eukaryotic translation initiation factor 4E type 2
Gene Name	EIF4E2
Organism	Homo sapiens (Human).
Sequence Length	245
Subcellular Localization
Protein Description	Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. [PubMed: 9582349]
Protein Sequence	MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	DALKDDDSGDHDQNE CCCCCCCCCCCCCCC	53.79	23401153
23	Phosphorylation	HDQNEENSTQKDGEK CCCCCCCCCCCCCHH	35.18	22167270
24	Phosphorylation	DQNEENSTQKDGEKE CCCCCCCCCCCCHHH	51.74	22167270
30	Acetylation	STQKDGEKEKTERDK CCCCCCHHHHHHHHC	70.78	26051181
68	Phosphorylation	TFWYSRRTPGRPTSS EEEEECCCCCCCCCC	29.05	25159151
73	Phosphorylation	RRTPGRPTSSQSYEQ CCCCCCCCCCHHHHH	39.38	21406692
74	Phosphorylation	RTPGRPTSSQSYEQN CCCCCCCCCHHHHHH	29.12	21406692
75	Phosphorylation	TPGRPTSSQSYEQNI CCCCCCCCHHHHHHH	26.14	21406692
77	Phosphorylation	GRPTSSQSYEQNIKQ CCCCCCHHHHHHHHH	32.36	21406692
78	Phosphorylation	RPTSSQSYEQNIKQI CCCCCHHHHHHHHHH	17.56	21406692
121	Ubiquitination	HLFKEGIKPMWEDDA HHHHCCCCCCCCCCC	39.41	PubMed
130	Ubiquitination	MWEDDANKNGGKWII CCCCCCCCCCCEEEE	59.70	PubMed
134	Acetylation	DANKNGGKWIIRLRK CCCCCCCEEEEHHCH	36.30	19608861
134	Malonylation	DANKNGGKWIIRLRK CCCCCCCEEEEHHCH	36.30	26320211
172	Phosphorylation	EICGAVVSVRFQEDI CCCCCEEEEEEHHHH	10.85	24719451
199	Phosphorylation	TTARIRDTLRRVLNL HHHHHHHHHHHHHCC	16.59	25954137
222	Ubiquitination	KTHTDSIKMPGRLGP ECCCCCCCCCCCCCH	42.89	PubMed
222	Ubiquitination	KTHTDSIKMPGRLGP ECCCCCCCCCCCCCH	42.89	-
225 (in isoform 2)	Phosphorylation	-	33.67	26434776
226 (in isoform 2)	Phosphorylation	-	30.51	26434776
239	Ubiquitination	LLFQNLWKPRLNVP- HHHCCCCCCCCCCC-	24.35	21890473
239	Acetylation	LLFQNLWKPRLNVP- HHHCCCCCCCCCCC-	24.35	25953088
241	Methylation	FQNLWKPRLNVP--- HCCCCCCCCCCC---	34.86	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	ARIH1	Q9Y4X5	PMID:14623119

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF4E2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of IF4E2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
4ET_HUMAN	EIF4ENIF1	physical	16189514
K1C20_HUMAN	KRT20	physical	16189514
KR412_HUMAN	KRTAP4-12	physical	16189514
ARI1_HUMAN	ARIH1	physical	14623119
UB2L3_HUMAN	UBE2L3	physical	14623119
A4_HUMAN	APP	physical	21832049
GGYF2_HUMAN	GIGYF2	physical	22751931
4ET_HUMAN	EIF4ENIF1	physical	22751931
GGYF1_HUMAN	GIGYF1	physical	22751931
ZN598_HUMAN	ZNF598	physical	22751931
4ET_HUMAN	EIF4ENIF1	physical	19060904
MDFI_HUMAN	MDFI	physical	19060904
MAGD1_HUMAN	MAGED1	physical	25416956
TMCC2_HUMAN	TMCC2	physical	25416956
SPY2_HUMAN	SPRY2	physical	25416956
SPAG5_HUMAN	SPAG5	physical	25416956
MARE3_HUMAN	MAPRE3	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
ATL4_HUMAN	ADAMTSL4	physical	25416956
NECA2_HUMAN	NECAB2	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
PRD14_HUMAN	PRDM14	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
UBX11_HUMAN	UBXN11	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
MIPO1_HUMAN	MIPOL1	physical	25416956
UBP54_HUMAN	USP54	physical	25416956
SPERT_HUMAN	SPERT	physical	25416956
ZBTB9_HUMAN	ZBTB9	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR108_HUMAN	KRTAP10-8	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
GGYF1_HUMAN	GIGYF1	physical	28514442
GGYF2_HUMAN	GIGYF2	physical	28514442
4ET_HUMAN	EIF4ENIF1	physical	28514442
4EBP2_HUMAN	EIF4EBP2	physical	28514442
EIF3F_HUMAN	EIF3F	physical	28514442
SYTC_HUMAN	TARS	physical	28514442
SYTC2_HUMAN	TARSL2	physical	28514442
KCTD3_HUMAN	KCTD3	physical	27173435
KI13B_HUMAN	KIF13B	physical	27173435
ZBT21_HUMAN	ZBTB21	physical	27173435
GGYF1_HUMAN	GIGYF1	physical	27173435
LRFN1_HUMAN	LRFN1	physical	27173435
DEN1A_HUMAN	DENND1A	physical	27173435
SPD2A_HUMAN	SH3PXD2A	physical	27173435
SRGP2_HUMAN	SRGAP2	physical	27173435
SI1L1_HUMAN	SIPA1L1	physical	27173435
LIMA1_HUMAN	LIMA1	physical	27173435
MAGI1_HUMAN	MAGI1	physical	27173435
TESK2_HUMAN	TESK2	physical	27173435
DCLK1_HUMAN	DCLK1	physical	27173435
RTKN_HUMAN	RTKN	physical	27173435
MAST3_HUMAN	MAST3	physical	27173435
DEN4C_HUMAN	DENND4C	physical	27173435
ZN638_HUMAN	ZNF638	physical	27173435
PPM1H_HUMAN	PPM1H	physical	27173435
CING_HUMAN	CGN	physical	27173435
SRS12_HUMAN	SRSF12	physical	27173435
SYDE1_HUMAN	SYDE1	physical	27173435
AGAP1_HUMAN	AGAP1	physical	27173435
MPIP2_HUMAN	CDC25B	physical	27173435
CDK16_HUMAN	CDK16	physical	27173435
SIN1_HUMAN	MAPKAP1	physical	27173435
F110B_HUMAN	FAM110B	physical	27173435
UBP21_HUMAN	USP21	physical	27173435
HDAC4_HUMAN	HDAC4	physical	27173435
AN34A_HUMAN	ANKRD34A	physical	27173435
FA53C_HUMAN	FAM53C	physical	27173435
F110A_HUMAN	FAM110A	physical	27173435
NF1_HUMAN	NF1	physical	27173435
CBY1_HUMAN	CBY1	physical	27173435
NADK_HUMAN	NADK	physical	27173435
LPIN3_HUMAN	LPIN3	physical	27173435
TIAM1_HUMAN	TIAM1	physical	27173435
M3K21_HUMAN	KIAA1804	physical	27173435
PHLB2_HUMAN	PHLDB2	physical	27173435
NGAP_HUMAN	RASAL2	physical	27173435
MPIP3_HUMAN	CDC25C	physical	27173435
CAMP2_HUMAN	CAMSAP2	physical	27173435
TBC25_HUMAN	TBC1D25	physical	27173435
GGYF2_HUMAN	GIGYF2	physical	27173435
PKHA7_HUMAN	PLEKHA7	physical	27173435
MELK_HUMAN	MELK	physical	27173435
GAB2_HUMAN	GAB2	physical	27173435
KIF1C_HUMAN	KIF1C	physical	27173435
SH3R3_HUMAN	SH3RF3	physical	27173435
NAV1_HUMAN	NAV1	physical	27173435
RPTOR_HUMAN	RPTOR	physical	27173435
DEP1B_HUMAN	DEPDC1B	physical	27173435
PTN14_HUMAN	PTPN14	physical	27173435
STA13_HUMAN	STARD13	physical	27173435
TANC2_HUMAN	TANC2	physical	27173435
PTN13_HUMAN	PTPN13	physical	27173435
AFAD_HUMAN	MLLT4	physical	27173435
RGPS2_HUMAN	RALGPS2	physical	27173435
OSBL6_HUMAN	OSBPL6	physical	27173435
HDAC7_HUMAN	HDAC7	physical	27173435
PKHA5_HUMAN	PLEKHA5	physical	27173435
LARP1_HUMAN	LARP1	physical	27173435
SH3B4_HUMAN	SH3BP4	physical	27173435
KIF1B_HUMAN	KIF1B	physical	27173435
CHK1_HUMAN	CHEK1	physical	27173435
INP5E_HUMAN	INPP5E	physical	27173435
RAB3I_HUMAN	RAB3IP	physical	27173435

Drug and Disease Associations

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

Regulatory Network of IF4E2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND MASS SPECTROMETRY.	19608861 [Abstract]