Eukaryotic translation initiation factor 4E-binding protein 1

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Q62622 (4EBP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 4E-binding protein 1
Short name=4E-BP1
Short name=eIF4E-binding protein 1

Alternative name(s):
Phosphorylated heat- and acid-stable protein regulated by insulin 1
Short name=PHAS-I

Gene names

Name:

Eif4ebp1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates eIF4E activity by preventing its assembly into the eIF4F complex. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Ref.2
Subunit structure	Interacts with RPTOR By similarity. Nonphosphorylated 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. Ref.2
Tissue specificity	Expressed in all tissues examined; highest levels in fat and skeletal tissue, lowest levels in kidney. Ref.1 Ref.2
Post-translational modification	Phosphorylation at Thr-36, Thr-45, Ser-64 and Thr-69 is regulated by mTORC1. Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Ref.1 Ref.2
Sequence similarities	Belongs to the eIF4E-binding protein family.

Ontologies

Keywords
Biological process	Translation regulation
Molecular function	Protein synthesis inhibitor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara TOR signaling cascade Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara lung development Inferred from expression pattern PubMed 18952566. Source: RGD negative regulation of protein complex assembly Inferred from mutant phenotype PubMed 11865047. Source: RGD negative regulation of translational initiation Inferred from mutant phenotype PubMed 11865047. Source: RGD positive regulation of mitotic cell cycle Inferred from electronic annotation. Source: Compara response to ethanol Inferred from expression pattern PubMed 15388509. Source: RGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 18952566. Source: RGD nucleus Inferred from direct assay PubMed 18952566. Source: RGD protein complex Inferred from direct assay PubMed 18952566. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 117

116

Eukaryotic translation initiation factor 4E-binding protein 1

PRO_0000190515

Amino acid modifications

Modified residue

N-acetylserine By similarity Ref.1

Modified residue

Phosphothreonine; by MTOR By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphothreonine; by MTOR By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR Ref.2

Modified residue

Phosphothreonine; by MTOR By similarity

Modified residue

Phosphoserine By similarity

Modified residue

100

Phosphoserine; by DYRK2 By similarity

Modified residue

111

Phosphoserine By similarity

Experimental info

Mutagenesis

S → A: Decreases phosphorylation by MAPK1 and MAPK3. Ref.2

Sequence conflict

R → N AA sequence Ref.1

Sequence conflict

T → P AA sequence Ref.1

Sequence conflict

P → L AA sequence Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q62622 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3449D57B09FA101A
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FASTA

117

12,404

        10         20         30         40         50         60 
MSAGSSCSQT PSRAIPTRRV ALGDGVQLPP GDYSTTPGGT LFSTTPGGTR IIYDRKFLME 

        70         80         90        100        110 
CRNSPVAKTP PKDLPTIPGV TSPTSDEPPM QASQSHLHSS PEDKRAGGEE SQFEMDI

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References

[1]	"Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin and growth factors." Hu C., Pang S., Kong X., Velleca M., Lawrence J.C. Jr. Proc. Natl. Acad. Sci. U.S.A. 91:3730-3734(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-33; 43-53; 62-80 AND 98-117, PHOSPHORYLATION, TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Adipocyte and Skeletal muscle.
[2]	"PHAS-I as a link between mitogen-activated protein kinase and translation initiation." Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J., Sonenberg N., Lawrence J.C. Jr. Science 266:653-656(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF4E, PHOSPHORYLATION AT SER-64 BY MAPK1 AND MAPK3, MUTAGENESIS OF SER-64.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U05014 mRNA. Translation: AAA86938.1.
IPI	IPI00207037.
PIR	A55258.
RefSeq	NP_446309.1. NM_053857.2.
UniGene	Rn.11161.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-267N.
MINT	MINT-94776.
STRING	10116.ENSRNOP00000016885.
PTM databases
PhosphoSite	Q62622.
Proteomic databases
PRIDE	Q62622.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000016885; ENSRNOP00000016885; ENSRNOG00000012582.
GeneID	116636.
KEGG	rno:116636.
UCSC	RGD:620259. rat.
Organism-specific databases
CTD	1978.
RGD	620259. Eif4ebp1.
Phylogenomic databases
eggNOG	NOG78084.
GeneTree	ENSGT00390000013843.
HOGENOM	HOG000231190.
HOVERGEN	HBG050425.
InParanoid	Q62622.
KO	K07205.
OMA	DKPAGGE.
OrthoDB	EOG40P486.
Gene expression databases
Genevestigator	Q62622.
GermOnline	ENSRNOG00000012582. Rattus norvegicus.
Family and domain databases
InterPro	IPR008606. EIF4EBP. [Graphical view]
PANTHER	PTHR12669. PTHR12669. 1 hit.
Pfam	PF05456. eIF_4EBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	619343.
PMAP-CutDB	Q62622.

Entry information

Entry name

4EBP1_RAT

Accession

Primary (citable) accession number: Q62622

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents