Q60876 (4EBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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.1
Subunit structure	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. Interacts with RPTOR. Ref.1
Tissue specificity	Highest expression in fat cells. Ref.1
Post-translational modification	Phosphorylation at Thr-36, Thr-45, Ser-64 and Thr-69 is regulated by mTORC1. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Ref.1
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 Reference proteome
Gene Ontology (GO)
Biological process	insulin receptor signaling pathway Inferred from direct assay Ref.1. Source: MGI negative regulation of translational initiation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred by curator. Source: MGI
Molecular function	eukaryotic initiation factor 4E binding Inferred from physical interaction. Source: MGI translation repressor activity Traceable author statement Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 117	116	Eukaryotic translation initiation factor 4E-binding protein 1		PRO_0000190514
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity UniProtKB Q62622
	Modified residue	10	1	Phosphothreonine By similarity
	Modified residue	33	1	Phosphotyrosine By similarity
	Modified residue	34	1	Phosphoserine By similarity
	Modified residue	35	1	Phosphothreonine By similarity
	Modified residue	36	1	Phosphothreonine; by MTOR By similarity
	Modified residue	40	1	Phosphothreonine By similarity
	Modified residue	43	1	Phosphoserine By similarity
	Modified residue	44	1	Phosphothreonine By similarity
	Modified residue	45	1	Phosphothreonine By similarity
	Modified residue	45	1	Phosphothreonine; by MTOR By similarity
	Modified residue	49	1	Phosphothreonine By similarity
	Modified residue	53	1	Phosphotyrosine By similarity
	Modified residue	64	1	Phosphoserine; by MAPK1, MAPK3 and MTOR By similarity UniProtKB Q62622
	Modified residue	69	1	Phosphothreonine; by MTOR By similarity
	Modified residue	81	1	Phosphothreonine By similarity
	Modified residue	82	1	Phosphoserine By similarity
	Modified residue	93	1	Phosphoserine By similarity
	Modified residue	100	1	Phosphoserine By similarity
	Modified residue	111	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	93	1	S → N in BAB28612. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q60876 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3458D5687468A7EA	FASTA	117	12,325
	10 20 30 40 50 60 MSAGSSCSQT PSRAIPTRRV ALGDGVQLPP GDYSTTPGGT LFSTTPGGTR IIYDRKFLME 70 80 90 100 110 CRNSPVAKTP PKDLPAIPGV TSPTSDEPPM QASQSQLPSS PEDKRAGGEE SQFEMDI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Control of PHAS-I by insulin in 3T3-L1 adipocytes. Synthesis, degradation, and phosphorylation by a rapamycin-sensitive and mitogen-activated protein kinase-independent pathway." Lin T.-A., Kong X., Saltiel A.R., Blackshear P.J., Lawrence J.C. Jr. J. Biol. Chem. 270:18531-18538(1995) [PubMed: 7629182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH EIF4E.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Embryo.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U28656 mRNA. Translation: AAA88818.1. AK013033 mRNA. Translation: BAB28612.1. AK169979 mRNA. Translation: BAE41494.1. AK170031 mRNA. Translation: BAE41521.1. BC002045 mRNA. Translation: AAH02045.1.
IPI	IPI00318938.
PIR	A57396.
RefSeq	NP_031944.3. NM_007918.3.
UniGene	Mm.6700.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32577N.
IntAct	Q60876. 1 interaction.
MINT	MINT-203831.
STRING	Q60876.
PTM databases
PhosphoSite	Q60876.
Proteomic databases
PRIDE	Q60876.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033880; ENSMUSP00000033880; ENSMUSG00000031490.
GeneID	13685.
KEGG	mmu:13685.
UCSC	uc009lih.1. mouse.
Organism-specific databases
CTD	1978.
MGI	MGI:103267. Eif4ebp1.
Phylogenomic databases
eggNOG	roNOG17464.
GeneTree	ENSGT00390000013843.
HOGENOM	HBG714775.
HOVERGEN	HBG050425.
InParanoid	Q60876.
OMA	DKPAGGE.
OrthoDB	EOG40P486.
PhylomeDB	Q60876.
Gene expression databases
ArrayExpress	Q60876.
Bgee	Q60876.
Genevestigator	Q60876.
GermOnline	ENSMUSG00000031490. Mus musculus.
Family and domain databases
InterPro	IPR008606. EIF4EBP. [Graphical view]
KO	K07205.
PANTHER	PTHR12669. EIF4EBP. 1 hit.
Pfam	PF05456. eIF_4EBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284450.
SOURCE	Search...

Entry information

Entry name

4EBP1_MOUSE

Accession

Primary (citable) accession number: Q60876
Secondary accession number(s): Q3TDS8, Q9CZ40

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program