Q62622 · 4EBP1_RAT
- ProteinEukaryotic translation initiation factor 4E-binding protein 1
- GeneEif4ebp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids117 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (By similarity).
Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7939721).
Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways (PubMed:7939721).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 4E-binding protein 1
- Short names4E-BP1; eIF4E-binding protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ62622
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 64 | Decreases phosphorylation by MAPK1 and MAPK3. | ||||
Sequence: S → A |
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000190515 | 2-117 | Eukaryotic translation initiation factor 4E-binding protein 1 | |||
Sequence: SAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVAKTPPKDLPTIPGVTSPTSDEPPMQASQSHLHSSPEDKRAGGEESQFEMDI | ||||||
Modified residue | 36 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 40 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 43 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 45 | Phosphothreonine; by MTOR | ||||
Sequence: T | ||||||
Modified residue | 49 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 53 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Cross-link | 56 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 64 | Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR | ||||
Sequence: S | ||||||
Modified residue | 69 | Phosphothreonine; by MTOR | ||||
Sequence: T | ||||||
Modified residue | 76 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 95 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 99 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 100 | Phosphoserine; by DYRK2 | ||||
Sequence: S | ||||||
Modified residue | 111 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Phosphorylation at Thr-36, Thr-45, Ser-64 and Thr-69, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E.
Ubiquitinated: when eIF4E levels are low, hypophosphorylated form is ubiquitinated by the BCR(KLHL25) complex, leading to its degradation and serving as a homeostatic mechanism to maintain translation and prevent eIF4E inhibition when eIF4E levels are low. Not ubiquitinated when hyperphosphorylated (at Thr-36, Thr-45, Ser-64 and Thr-69) or associated with eIF4E.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all tissues examined; highest levels in fat and skeletal tissue, lowest levels in kidney.
Gene expression databases
Interaction
Subunit
Hypophosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) or mTORC1 phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation (PubMed:7939721).
Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (By similarity).
Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MSAGSSCSQTPSRAI | ||||||
Region | 1-47 | Disordered | ||||
Sequence: MSAGSSCSQTPSRAIPTRRVALGDGVQLPPGDYSTTPGGTLFSTTPG | ||||||
Compositional bias | 33-47 | Polar residues | ||||
Sequence: YSTTPGGTLFSTTPG | ||||||
Motif | 53-59 | YXXXXLphi motif | ||||
Sequence: YDRKFLM | ||||||
Region | 64-117 | Disordered | ||||
Sequence: SPVAKTPPKDLPTIPGVTSPTSDEPPMQASQSHLHSSPEDKRAGGEESQFEMDI | ||||||
Compositional bias | 78-97 | Polar residues | ||||
Sequence: PGVTSPTSDEPPMQASQSHL | ||||||
Compositional bias | 98-117 | Basic and acidic residues | ||||
Sequence: HSSPEDKRAGGEESQFEMDI | ||||||
Motif | 113-117 | TOS motif | ||||
Sequence: FEMDI |
Domain
The TOS motif mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex.
Sequence similarities
Belongs to the eIF4E-binding protein family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length117
- Mass (Da)12,404
- Last updated2007-01-23 v3
- Checksum3449D57B09FA101A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2Q998 | A0A8L2Q998_RAT | Eif4ebp1 | 119 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MSAGSSCSQTPSRAI | ||||||
Sequence conflict | 19 | in Ref. 1; AA sequence | ||||
Sequence: R → N | ||||||
Compositional bias | 33-47 | Polar residues | ||||
Sequence: YSTTPGGTLFSTTPG | ||||||
Sequence conflict | 69 | in Ref. 1; AA sequence | ||||
Sequence: T → P | ||||||
Sequence conflict | 75 | in Ref. 1; AA sequence | ||||
Sequence: P → L | ||||||
Compositional bias | 78-97 | Polar residues | ||||
Sequence: PGVTSPTSDEPPMQASQSHL | ||||||
Compositional bias | 98-117 | Basic and acidic residues | ||||
Sequence: HSSPEDKRAGGEESQFEMDI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U05014 EMBL· GenBank· DDBJ | AAA86938.1 EMBL· GenBank· DDBJ | mRNA |