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Protein

Eukaryotic translation initiation factor 4E-binding protein 1

Gene

EIF4EBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways.2 Publications

GO - Molecular functioni

  1. translation repressor activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: UniProtKB
  3. gene expression Source: Reactome
  4. insulin receptor signaling pathway Source: Reactome
  5. IRES-dependent translational initiation Source: Ensembl
  6. lung development Source: Ensembl
  7. negative regulation of protein complex assembly Source: Ensembl
  8. negative regulation of translational initiation Source: UniProtKB
  9. positive regulation of mitotic cell cycle Source: UniProtKB
  10. response to ethanol Source: Ensembl
  11. response to ischemia Source: Ensembl
  12. TOR signaling Source: UniProtKB
  13. translation Source: Reactome
  14. translational initiation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Protein synthesis inhibitor

Keywords - Biological processi

Translation regulation

Enzyme and pathway databases

ReactomeiREACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_6836. Release of eIF4E.
SignaLinkiQ13541.

Names & Taxonomyi

Protein namesi
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 namesi
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:3288. EIF4EBP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: HPA
  4. protein complex Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371T → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-46; A-65 and A-70. 1 Publication
Mutagenesisi46 – 461T → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-65 and A-70. 1 Publication
Mutagenesisi57 – 571K → R: Impaired ubiquitination by the BCR(KLHL25) complex. 1 Publication
Mutagenesisi59 – 602LM → AA: Abolishes eIF4E-binding. Increased ubiquitination by the BCR(KLHL25) complex. 1 Publication
Mutagenesisi65 – 651S → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-70. 1 Publication
Mutagenesisi69 – 691K → R: Does not affect ubiquitination by the BCR(KLHL25) complex. 1 Publication
Mutagenesisi70 – 701T → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-65. 1 Publication
Mutagenesisi105 – 1051K → R: Does not affect ubiquitination by the BCR(KLHL25) complex. 1 Publication

Organism-specific databases

PharmGKBiPA27715.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 118117Eukaryotic translation initiation factor 4E-binding protein 1PRO_0000190513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei37 – 371Phosphothreonine; by MTOR5 Publications
Modified residuei41 – 411Phosphothreonine1 Publication
Modified residuei46 – 461Phosphothreonine; by MTOR4 Publications
Modified residuei50 – 501Phosphothreonine2 Publications
Modified residuei54 – 541Phosphotyrosine1 Publication
Cross-linki57 – 57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei65 – 651Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR6 Publications
Modified residuei70 – 701Phosphothreonine; by MTOR7 Publications
Modified residuei77 – 771Phosphothreonine1 Publication
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei101 – 1011Phosphoserine; by DYRK22 Publications
Modified residuei112 – 1121Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Phosphorylation at Thr-37, Thr-46, Ser-65 and Thr-70, corresponding to the hyperphosphorylated form, is regulated by mTORC1 and abolishes binding to EIF4E.12 Publications
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-37, Thr-46, Ser-65 and Thr-70) or associated with eIF4E.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13541.
PaxDbiQ13541.
PeptideAtlasiQ13541.
PRIDEiQ13541.

PTM databases

PhosphoSiteiQ13541.

Miscellaneous databases

PMAP-CutDBQ13541.

Expressioni

Gene expression databases

BgeeiQ13541.
CleanExiHS_EIF4EBP1.
GenevestigatoriQ13541.

Organism-specific databases

HPAiCAB005032.
CAB005039.
HPA023501.

Interactioni

Subunit structurei

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. Interacts (via TOS motif) with RPTOR; promoting phosphorylation by mTORC1 (PubMed:12747827).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO2Q9UKV82EBI-74090,EBI-528269
EIF4EP067308EBI-74090,EBI-73440
MTORP423452EBI-74090,EBI-359260
MtorQ9JLN92EBI-74090,EBI-1571628From a different organism.
RPTORQ8N1225EBI-74090,EBI-1567928

Protein-protein interaction databases

BioGridi108293. 30 interactions.
DIPiDIP-30944N.
IntActiQ13541. 17 interactions.
MINTiMINT-210160.
STRINGi9606.ENSP00000340691.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 616Combined sources
Helixi62 – 643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ4X-ray2.25B51-64[»]
1WKWX-ray2.10B47-66[»]
2JGBX-ray1.70B51-67[»]
2JGCX-ray2.40B51-67[»]
2V8WX-ray2.30B/F51-64[»]
2V8XX-ray2.30B/F51-64[»]
2V8YX-ray2.10B/F51-64[»]
3HXGX-ray2.10C51-67[»]
3HXIX-ray1.80C51-67[»]
3M93X-ray2.90C51-67[»]
3M94X-ray2.05C51-67[»]
3U7XX-ray2.10C/D47-66[»]
DisProtiDP00028.
ProteinModelPortaliQ13541.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13541.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi54 – 607YXXXXLphi motifBy similarity
Motifi114 – 1185TOS motif1 Publication

Domaini

The TOS motif mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex.1 Publication

Sequence similaritiesi

Belongs to the eIF4E-binding protein family.Curated

Phylogenomic databases

eggNOGiNOG78084.
GeneTreeiENSGT00390000013843.
HOGENOMiHOG000231190.
HOVERGENiHBG050425.
InParanoidiQ13541.
KOiK07205.
OMAiNHLRNSP.
OrthoDBiEOG7B31Q1.
PhylomeDBiQ13541.
TreeFamiTF101530.

Family and domain databases

InterProiIPR008606. EIF4EBP.
[Graphical view]
PfamiPF05456. eIF_4EBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGSSCSQT PSRAIPATRR VVLGDGVQLP PGDYSTTPGG TLFSTTPGGT
60 70 80 90 100
RIIYDRKFLM ECRNSPVTKT PPRDLPTIPG VTSPSSDEPP MEASQSHLRN
110
SPEDKRAGGE ESQFEMDI
Length:118
Mass (Da):12,580
Last modified:January 22, 2007 - v3
Checksum:i1682A6BA74132966
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36055 mRNA. Translation: AAA62269.1.
AB044548 mRNA. Translation: BAB18650.1.
BT007162 mRNA. Translation: AAP35826.1.
CR456769 mRNA. Translation: CAG33050.1.
AK312011 mRNA. Translation: BAG34949.1.
CH471080 Genomic DNA. Translation: EAW63341.1.
CH471080 Genomic DNA. Translation: EAW63342.1.
BC004459 mRNA. Translation: AAH04459.1.
BC058073 mRNA. Translation: AAH58073.1.
CCDSiCCDS6100.1.
PIRiS50866.
RefSeqiNP_004086.1. NM_004095.3.
UniGeneiHs.411641.

Genome annotation databases

GeneIDi1978.
KEGGihsa:1978.
UCSCiuc003xks.3. human.

Polymorphism databases

DMDMi34921508.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36055 mRNA. Translation: AAA62269.1.
AB044548 mRNA. Translation: BAB18650.1.
BT007162 mRNA. Translation: AAP35826.1.
CR456769 mRNA. Translation: CAG33050.1.
AK312011 mRNA. Translation: BAG34949.1.
CH471080 Genomic DNA. Translation: EAW63341.1.
CH471080 Genomic DNA. Translation: EAW63342.1.
BC004459 mRNA. Translation: AAH04459.1.
BC058073 mRNA. Translation: AAH58073.1.
CCDSiCCDS6100.1.
PIRiS50866.
RefSeqiNP_004086.1. NM_004095.3.
UniGeneiHs.411641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ4X-ray2.25B51-64[»]
1WKWX-ray2.10B47-66[»]
2JGBX-ray1.70B51-67[»]
2JGCX-ray2.40B51-67[»]
2V8WX-ray2.30B/F51-64[»]
2V8XX-ray2.30B/F51-64[»]
2V8YX-ray2.10B/F51-64[»]
3HXGX-ray2.10C51-67[»]
3HXIX-ray1.80C51-67[»]
3M93X-ray2.90C51-67[»]
3M94X-ray2.05C51-67[»]
3U7XX-ray2.10C/D47-66[»]
DisProtiDP00028.
ProteinModelPortaliQ13541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108293. 30 interactions.
DIPiDIP-30944N.
IntActiQ13541. 17 interactions.
MINTiMINT-210160.
STRINGi9606.ENSP00000340691.

PTM databases

PhosphoSiteiQ13541.

Polymorphism databases

DMDMi34921508.

Proteomic databases

MaxQBiQ13541.
PaxDbiQ13541.
PeptideAtlasiQ13541.
PRIDEiQ13541.

Protocols and materials databases

DNASUi1978.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1978.
KEGGihsa:1978.
UCSCiuc003xks.3. human.

Organism-specific databases

CTDi1978.
GeneCardsiGC08P037888.
HGNCiHGNC:3288. EIF4EBP1.
HPAiCAB005032.
CAB005039.
HPA023501.
MIMi602223. gene.
neXtProtiNX_Q13541.
PharmGKBiPA27715.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG78084.
GeneTreeiENSGT00390000013843.
HOGENOMiHOG000231190.
HOVERGENiHBG050425.
InParanoidiQ13541.
KOiK07205.
OMAiNHLRNSP.
OrthoDBiEOG7B31Q1.
PhylomeDBiQ13541.
TreeFamiTF101530.

Enzyme and pathway databases

ReactomeiREACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_6836. Release of eIF4E.
SignaLinkiQ13541.

Miscellaneous databases

EvolutionaryTraceiQ13541.
GeneWikiiEIF4EBP1.
GenomeRNAii1978.
NextBioi8003.
PMAP-CutDBQ13541.
PROiQ13541.
SOURCEiSearch...

Gene expression databases

BgeeiQ13541.
CleanExiHS_EIF4EBP1.
GenevestigatoriQ13541.

Family and domain databases

InterProiIPR008606. EIF4EBP.
[Graphical view]
PfamiPF05456. eIF_4EBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function."
    Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., Lawrence J.C. Jr., Sonenberg N.
    Nature 371:762-767(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF4E, PHOSPHORYLATION.
    Tissue: Placenta.
  2. "Identification of multiple genes and immunogenic epitopes of pancreatic cancer cells."
    Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon and Lung1 Publication.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT SER-2.
    Tissue: Platelet.
  9. "Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
    Haghighat A., Mader S., Pause A., Sonenberg N.
    EMBO J. 14:5701-5709(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF4E AND EIF4G.
  10. "RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1."
    Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MTOR.
  11. "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action."
    Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K.
    Cell 110:177-189(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPTOR.
  12. "TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function."
    Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.
    Curr. Biol. 13:797-806(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPTOR, PHOSPHORYLATION AT THR-37; THR-46; SER-65 AND THR-70 BY MTOR.
  13. "The C terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation."
    Wang X., Li W., Parra J.L., Beugnet A., Proud C.G.
    Mol. Cell. Biol. 23:1546-1557(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-65; SER-101 AND SER-112, PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  17. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50; THR-70 AND SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; THR-41; THR-46; THR-50; TYR-54; SER-65; THR-70 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND THR-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. Cited for: FUNCTION, INTERACTION WITH EIF4E, UBIQUITINATION AT LYS-57, PHOSPHORYLATION AT THR-37; THR-46; SER-65 AND THR-70, MUTAGENESIS OF THR-37; THR-46; LYS-57; 59-LEU-MET-60; SER-65; LYS-69; THR-70 AND LYS-105.
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; THR-70 AND THR-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  27. "The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein."
    Fletcher C.M., Wagner G.
    Protein Sci. 7:1639-1642(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 4-118.
  28. "Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods."
    Tomoo K., Matsushita Y., Fujisaki H., Abiko F., Shen X., Taniguchi T., Miyagawa H., Kitamura K., Miura K., Ishida T.
    Biochim. Biophys. Acta 1753:191-208(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-70 IN COMPLEX WITH EIF4E AND MRNA CAP ANALOG.
  29. "Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms."
    Rosettani P., Knapp S., Vismara M.-G., Rusconi L., Cameron A.D.
    J. Mol. Biol. 368:691-705(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-67 IN COMPLEX WITH EIF4E2 AND MRNA CAP ANALOG.
  30. "Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives."
    Brown C.J., McNae I., Fischer P.M., Walkinshaw M.D.
    J. Mol. Biol. 372:7-15(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 51-64 IN COMPLEX WITH EIF4E AND MRNA CAP ANALOG.

Entry informationi

Entry namei4EBP1_HUMAN
AccessioniPrimary (citable) accession number: Q13541
Secondary accession number(s): B2R502, D3DSW8, Q6IBN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2003
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.