4EBP3_HUMAN - dbPTM
4EBP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 4EBP3_HUMAN
UniProt AC O60516
Protein Name Eukaryotic translation initiation factor 4E-binding protein 3
Gene Name EIF4EBP3
Organism Homo sapiens (Human).
Sequence Length 100
Subcellular Localization
Protein Description Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation..
Protein Sequence MSTSTSCPIPGGRDQLPDCYSTTPGGTLYATTPGGTRIIYDRKFLLECKNSPIARTPPCCLPQIPGVTTPPTAPLSKLEELKEQETEEEIPDDAQFEMDI
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 Orthologous
Protein Cluster
2Phosphorylation------MSTSTSCPI
------CCCCCCCCC
30.9429083192
3Phosphorylation-----MSTSTSCPIP
-----CCCCCCCCCC
34.4229083192
4Phosphorylation----MSTSTSCPIPG
----CCCCCCCCCCC
15.8329083192
5Phosphorylation---MSTSTSCPIPGG
---CCCCCCCCCCCC
34.1429083192
6Phosphorylation--MSTSTSCPIPGGR
--CCCCCCCCCCCCC
20.0529083192
20PhosphorylationRDQLPDCYSTTPGGT
CCCCCCCEECCCCCE
19.2128796482
21PhosphorylationDQLPDCYSTTPGGTL
CCCCCCEECCCCCEE
31.9430576142
22PhosphorylationQLPDCYSTTPGGTLY
CCCCCEECCCCCEEE
15.5530576142
23PhosphorylationLPDCYSTTPGGTLYA
CCCCEECCCCCEEEE
17.6222322096
27PhosphorylationYSTTPGGTLYATTPG
EECCCCCEEEEECCC
23.6322322096
29PhosphorylationTTPGGTLYATTPGGT
CCCCCEEEEECCCCE
11.1825262027
31PhosphorylationPGGTLYATTPGGTRI
CCCEEEEECCCCEEE
21.7022322096
32PhosphorylationGGTLYATTPGGTRII
CCEEEEECCCCEEEE
16.2722322096
36PhosphorylationYATTPGGTRIIYDRK
EEECCCCEEEEECCC
25.3028796482
40PhosphorylationPGGTRIIYDRKFLLE
CCCEEEEECCCEEEE
13.8126074081
51PhosphorylationFLLECKNSPIARTPP
EEEECCCCCCCCCCC
11.8128450419
56PhosphorylationKNSPIARTPPCCLPQ
CCCCCCCCCCCCCCC
23.6628450419
68PhosphorylationLPQIPGVTTPPTAPL
CCCCCCCCCCCCCCH
39.2326552605
69PhosphorylationPQIPGVTTPPTAPLS
CCCCCCCCCCCCCHH
25.5130576142
72PhosphorylationPGVTTPPTAPLSKLE
CCCCCCCCCCHHHHH
41.9526552605
76PhosphorylationTPPTAPLSKLEELKE
CCCCCCHHHHHHHHH
33.8526552605
77UbiquitinationPPTAPLSKLEELKEQ
CCCCCHHHHHHHHHH
68.54-

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

Oops, there are no upstream regulatory protein records of 4EBP3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 4EBP3_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 4EBP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4E2_HUMANEIF4E2physical
16189514
IF4E_HUMANEIF4Ephysical
12482586
IF4E_HUMANEIF4Ephysical
9593750

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 4EBP3_HUMAN

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Related Literatures of Post-Translational Modification

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