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Q13541 (4EBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Ref.1 Ref.24

Subunit structure

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 with RPTOR. Ref.1 Ref.9 Ref.11 Ref.12 Ref.24

Post-translational modification

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. Ref.1 Ref.10 Ref.12 Ref.13 Ref.24

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. Ref.1 Ref.10 Ref.12 Ref.13 Ref.24

Sequence similarities

Belongs to the eIF4E-binding protein family.

Ontologies

Keywords
   Biological processTranslation regulation
   Molecular functionProtein synthesis inhibitor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 14673156. Source: UniProtKB

TOR signaling

Inferred from direct assay Ref.11Ref.24. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of translational initiation

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 14673156. Source: UniProtKB

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to ischemia

Inferred from electronic annotation. Source: Ensembl

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12150925Ref.27Ref.28. Source: UniProtKB

translation repressor activity

Inferred from direct assay Ref.24. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 118117Eukaryotic translation initiation factor 4E-binding protein 1
PRO_0000190513

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.25 UniProtKB Q62622
Modified residue371Phosphothreonine; by MTOR Ref.12 Ref.18 Ref.20 Ref.21 Ref.24
Modified residue411Phosphothreonine Ref.18
Modified residue461Phosphothreonine; by MTOR Ref.12 Ref.18 Ref.20 Ref.24
Modified residue501Phosphothreonine Ref.17 Ref.18
Modified residue541Phosphotyrosine Ref.18
Modified residue651Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR Ref.12 Ref.13 Ref.14 Ref.18 Ref.24 UniProtKB Q62622
Modified residue701Phosphothreonine; by MTOR Ref.12 Ref.17 Ref.18 Ref.21 Ref.23 Ref.24
Modified residue831Phosphoserine Ref.18
Modified residue1011Phosphoserine; by DYRK2 Ref.13 Ref.17
Modified residue1121Phosphoserine Ref.13 Ref.16 Ref.23
Cross-link57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Experimental info

Mutagenesis371T → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-46; A-65 and A-70. Ref.24
Mutagenesis461T → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-65 and A-70. Ref.24
Mutagenesis571K → R: Impaired ubiquitination by the BCR(KLHL25) complex. Ref.24
Mutagenesis59 – 602LM → AA: Abolishes eIF4E-binding. Increased ubiquitination by the BCR(KLHL25) complex.
Mutagenesis651S → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-70. Ref.24
Mutagenesis691K → R: Does not affect ubiquitination by the BCR(KLHL25) complex. Ref.24
Mutagenesis701T → A: Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-65. Ref.24
Mutagenesis1051K → R: Does not affect ubiquitination by the BCR(KLHL25) complex. Ref.24

Secondary structure

.... 118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13541 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1682A6BA74132966

FASTA11812,580
        10         20         30         40         50         60 
MSGGSSCSQT PSRAIPATRR VVLGDGVQLP PGDYSTTPGG TLFSTTPGGT RIIYDRKFLM 

        70         80         90        100        110 
ECRNSPVTKT PPRDLPTIPG VTSPSSDEPP MEASQSHLRN SPEDKRAGGE ESQFEMDI 

« Hide

References

« Hide 'large scale' references
[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(1994) [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 (JUN-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 (MAY-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 (JUN-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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Lung.
[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(2003) [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(1995) [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(1998) [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(2002) [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(2003) [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(2003) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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(2008) [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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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(2009) [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(2009) [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(2010) [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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND SER-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Translational homeostasis via the mRNA cap-binding protein, eIF4E."
Yanagiya A., Suyama E., Adachi H., Svitkin Y.V., Aza-Blanc P., Imataka H., Mikami S., Martineau Y., Ronai Z.A., Sonenberg N.
Mol. Cell 46:847-858(2012) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 4-118.
[27]"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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-70 IN COMPLEX WITH EIF4E AND MRNA CAP ANALOG.
[28]"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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-67 IN COMPLEX WITH EIF4E2 AND MRNA CAP ANALOG.
[29]"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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 51-64 IN COMPLEX WITH EIF4E AND MRNA CAP ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6100.1.
PIRS50866.
RefSeqNP_004086.1. NM_004095.3.
UniGeneHs.411641.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00028.
ProteinModelPortalQ13541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108293. 25 interactions.
DIPDIP-30944N.
IntActQ13541. 14 interactions.
MINTMINT-210160.
STRING9606.ENSP00000340691.

PTM databases

PhosphoSiteQ13541.

Polymorphism databases

DMDM34921508.

Proteomic databases

MaxQBQ13541.
PaxDbQ13541.
PeptideAtlasQ13541.
PRIDEQ13541.

Protocols and materials databases

DNASU1978.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338825; ENSP00000340691; ENSG00000187840.
GeneID1978.
KEGGhsa:1978.
UCSCuc003xks.3. human.

Organism-specific databases

CTD1978.
GeneCardsGC08P037888.
HGNCHGNC:3288. EIF4EBP1.
HPACAB005032.
CAB005039.
HPA023501.
MIM602223. gene.
neXtProtNX_Q13541.
PharmGKBPA27715.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78084.
HOGENOMHOG000231190.
HOVERGENHBG050425.
InParanoidQ13541.
KOK07205.
OMANHLRNSP.
OrthoDBEOG7B31Q1.
PhylomeDBQ13541.
TreeFamTF101530.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.
SignaLinkQ13541.

Gene expression databases

BgeeQ13541.
CleanExHS_EIF4EBP1.
GenevestigatorQ13541.

Family and domain databases

InterProIPR008606. EIF4EBP.
[Graphical view]
PfamPF05456. eIF_4EBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13541.
GeneWikiEIF4EBP1.
GenomeRNAi1978.
NextBio8003.
PMAP-CutDBQ13541.
PROQ13541.
SOURCESearch...

Entry information

Entry name4EBP1_HUMAN
AccessionPrimary (citable) accession number: Q13541
Secondary accession number(s): B2R502, D3DSW8, Q6IBN3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM