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4E-BP1 (mouse)

Overview 4E-BP1 binds to eIF4E, preventing its assembly into the EIF4F complex and inhibiting cap-dependent translation. Phosphorylation of 4E-BP1 disrupts this binding, activating cap-dependent translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the PI3 kinase pathway. Note: This description may include information from UniProtKB. Protein type: Translation initiation; Translation Cellular Component: protein complex; cytoplasm; nucleus Molecular Function: protein binding; translation repressor activity; translation initiation factor binding; eukaryotic initiation factor 4E binding Biological Process: regulation of translation; negative regulation of translational initiation; TOR signaling pathway; negative regulation of translation; insulin receptor signaling pathway; positive regulation of mitotic cell cycle; negative regulation of protein complex assembly; regulation of translational initiation; G1/S transition of mitotic cell cycle Reference #:  Q60876 (UniProtKB) Alt. Names/Synonyms: 4E-BP1; 4EBP1; AA959816; eIF4E-binding protein 1; Eif4ebp1; eukaryotic translation initiation factor 4E binding protein 1; Eukaryotic translation initiation factor 4E-binding protein 1; PHAS-I; Phosphorylated heat- and acid-stable protein regulated by insulin 1 Gene Symbols: Eif4ebp1 Molecular weight: 12,325 Da Basal Isoelectric point: 5.01  Predict pI for various phosphorylation states CST Pathways:  AMPK Signaling  |  Angiogenesis  |  Insulin Receptor Signaling  |  mTOR Signaling  |  PI3K/Akt Signaling  |  Translation: eIF4E and p70S6K Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below 4E-BP1 1WKW - B=47-66 (human) 2JGB - B=51-67 (human) 2JGC - B=51-67 (human) 2V8W - B/F=51-64 (human) 2V8X - B/F=51-64 (human) 2V8Y - B/F=51-64 (human) 3HXG - C=51-67 (human) 3HXI - C=51-67 (human) 3M93 - C=51-67 (human) 3M94 - C=51-67 (human) 3SMU - D/C=47-66 (human) 3U7X - D/C=47-66 (human)

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	Sites Implicated In
molecular association, regulation: T36‑p, T45‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			mouse
0	1		S2	______MSAGSSCSQ
0	1		S5	___MSAGSSCSQTPS
0	1		S8	MSAGSSCSQTPSRAI
0	1		D24	TRRVALGDGVQLPPG
0	56		Y33-p	VQLPPGDysttPGGt
0	34		S34-p	QLPPGDysttPGGtL
1	28		T35-p	LPPGDysttPGGtLF
83	106		T36-p	PPGDysttPGGtLFs
0	62		T40-p	ysttPGGtLFsttPG
0	53		S43-p	tPGGtLFsttPGGtR
1	64		T44-p	PGGtLFsttPGGtRI
84	105		T45-p	GGtLFsttPGGtRII
0	48		T49-p	FsttPGGtRIIyDRk
0	27		Y53-p	PGGtRIIyDRkFLME
0	1		K56-u	tRIIyDRkFLMECRN
57	25		S64-p	FLMECRNsPVAKtPP
0	3		A67	ECRNsPVAKtPPKDL
0	1		K68	CRNsPVAKtPPKDLP
35	25		T69-p	RNsPVAKtPPKDLPA
0	2		T81-p	LPAIPGVtsPtsDEP
4	5		S82-p	PAIPGVtsPtsDEPP
0	2		T84-p	IPGVtsPtsDEPPMQ
0	2		S85-p	PGVtsPtsDEPPMQA
1	7		S93-p	DEPPMQAsQsQLPss
0	2		S95-p	PPMQAsQsQLPssPE
1	3		S99-p	AsQsQLPssPEDKRA
2	7		S100-p	sQsQLPssPEDKRAG
5	18		S111-p	KRAGGEEsQFEMDI_

	human
S2-p	______MsGGsSCsQ
S5-p	___MsGGsSCsQTPS
S8-p	MsGGsSCsQTPSRAI
D25-ca	TRRVVLGdGVQLPPG
Y34-p	VQLPPGDysttPGGt
S35-p	QLPPGDysttPGGtL
T36-p	LPPGDysttPGGtLF
T37-p	PPGDysttPGGtLFs
T41-p	ysttPGGtLFsttPG
S44-p	tPGGtLFsttPGGtR
T45-p	PGGtLFsttPGGtRI
T46-p	GGtLFsttPGGtRII
T50-p	FsttPGGtRIIyDRK
Y54-p	PGGtRIIyDRKFLME
K57	tRIIyDRKFLMECRN
S65-p	FLMECRNsPVtktPP
T68-p	ECRNsPVtktPPRDL
K69-u	CRNsPVtktPPRDLP
T70-p	RNsPVtktPPRDLPT
T82-p	LPTIPGVtsPsSDEP
S83-p	PTIPGVtsPsSDEPP
S85-p	IPGVtsPsSDEPPME
S86	PGVtsPsSDEPPMEA
S94-p	DEPPMEAsQSHLRNs
S96	PPMEAsQSHLRNsPE
N100	AsQSHLRNsPEDKRA
S101-p	sQSHLRNsPEDKRAG
S112-p	KRAGGEEsQFEMDI_

	rat
S2	______MSAGSSCSQ
S5	___MSAGSSCSQTPS
S8	MSAGSSCSQTPSRAI
D24	TRRVALGDGVQLPPG
Y33	VQLPPGDYSttPGGT
S34	QLPPGDYSttPGGTL
T35-p	LPPGDYSttPGGTLF
T36-p	PPGDYSttPGGTLFS
T40	YSttPGGTLFSttPG
S43	tPGGTLFSttPGGTR
T44-p	PGGTLFSttPGGTRI
T45-p	GGTLFSttPGGTRII
T49	FSttPGGTRIIYDRK
Y53	PGGTRIIYDRKFLME
K56	TRIIYDRKFLMECRN
S64-p	FLMECRNsPVAKtPP
A67	ECRNsPVAKtPPKDL
K68	CRNsPVAKtPPKDLP
T69-p	RNsPVAKtPPKDLPT
T81	LPTIPGVTsPTSDEP
S82-p	PTIPGVTsPTSDEPP
T84	IPGVTsPTSDEPPMQ
S85	PGVTsPTSDEPPMQA
S93	DEPPMQASQSHLHsS
S95	PPMQASQSHLHsSPE
S99-p	ASQSHLHsSPEDKRA
S100	SQSHLHsSPEDKRAG
S111-p	KRAGGEEsQFEMDI_

	fruit fly
S2	______MSASPTARQ
P5	___MSASPTARQAIT
R8	MSASPTARQAITQAL
D26	TRKVVISDPIQMPEV
Y34	PIQMPEVYSSTPGGT
S35	IQMPEVYSSTPGGTL
S36	QMPEVYSSTPGGTLY
T37	MPEVYSSTPGGTLYS
T41	YSSTPGGTLYSTTPG
S44	TPGGTLYSTTPGGTK
T45	PGGTLYSTTPGGTKL
T46	GGTLYSTTPGGTKLI
T50	YSTTPGGTKLIYERA
Y54	PGGTKLIYERAFMKN
A57	TKLIYERAFMKNLRG
S65	FMKNLRGSPLSQTPP
S68	NLRGSPLSQTPPSNV
Q69	LRGSPLSQTPPSNVP
T70	RGSPLSQTPPSNVPS
G82	VPSCLLRGTPRTPFR
T83	PSCLLRGTPRTPFRK
R85	CLLRGTPRTPFRKCV
T86	LLRGTPRTPFRKCVP
-	gap
-	gap
-	gap
-	gap
-	gap

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