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P60228 (EIF3E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit E

Short name=eIF3e
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 6
Viral integration site protein INT-6 homolog
eIF-3 p48
Gene names
Name:EIF3E
Synonyms:EIF3S6, INT6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway. May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins. Ref.18 Ref.19 Ref.22

Subunit structure

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with COPS3, COPS6, COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with IFIT1 and IFIT2. Ref.1 Ref.3 Ref.4 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.25

Subcellular location

Cytoplasm. NucleusPML body Ref.3 Ref.4 Ref.9 Ref.20.

Tissue specificity

Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus. Ref.1 Ref.3

Sequence similarities

Belongs to the eIF-3 subunit E family.

Contains 1 PCI domain.

Mass spectrometry

Molecular mass is 52131.8 Da from positions 1 - 445. Ref.21

Molecular mass is 52133.4±0.2 Da from positions 1 - 445. Determined by MALDI. Ref.25

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

formation of translation preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

gene expression

Traceable author statement. Source: Reactome

negative regulation of translational initiation

Non-traceable author statement Ref.9. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of translational initiation

Non-traceable author statement Ref.18Ref.1. Source: UniProtKB

translation

Traceable author statement. Source: Reactome

translational initiation

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

eukaryotic 43S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic 48S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic translation initiation factor 3 complex

Inferred from direct assay Ref.21Ref.17Ref.25Ref.1. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleoplasm

Non-traceable author statement Ref.18. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18Ref.25. Source: UniProtKB

translation initiation factor activity

Inferred by curator Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EPAS1Q9981410EBI-347740,EBI-447470
ORFQ9Q2G45EBI-347740,EBI-6248094From a different organism.
TRIM27P143737EBI-347740,EBI-719493
ZDHHC17Q8IUH52EBI-347740,EBI-524753

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.21
Chain2 – 445444Eukaryotic translation initiation factor 3 subunit E HAMAP-Rule MF_03004
PRO_0000123515

Regions

Domain290 – 395106PCI
Region4 – 128125Sufficient for interaction with EPAS1 HAMAP-Rule MF_03004
Region9 – 195187Sufficient for interaction with TRIM27 HAMAP-Rule MF_03004
Region351 – 44595Sufficient for interaction with MCM7 HAMAP-Rule MF_03004

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.21 Ref.26 Ref.29 Ref.30
Modified residue3991Phosphoserine Ref.24 Ref.27
Modified residue4391Phosphothreonine By similarity
Modified residue4451Phosphotyrosine By similarity

Natural variations

Natural variant1851A → V. Ref.7
Corresponds to variant rs17856554 [ dbSNP | Ensembl ].
VAR_046480

Experimental info

Mutagenesis3121L → D: Promotes nuclear accumulation. Ref.20

Sequences

Sequence LengthMass (Da)Tools
P60228 [UniParc].

Last modified January 16, 2004. Version 1.
Checksum: A5368651DD0DDD0C

FASTA44552,221
        10         20         30         40         50         60 
MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM VDFAMDVYKN 

        70         80         90        100        110        120 
LYSDDIPHAL REKRTTVVAQ LKQLQAETEP IVKMFEDPET TRQMQSTRDG RMLFDYLADK 

       130        140        150        160        170        180 
HGFRQEYLDT LYRYAKFQYE CGNYSGAAEY LYFFRVLVPA TDRNALSSLW GKLASEILMQ 

       190        200        210        220        230        240 
NWDAAMEDLT RLKETIDNNS VSSPLQSLQQ RTWLIHWSLF VFFNHPKGRD NIIDLFLYQP 

       250        260        270        280        290        300 
QYLNAIQTMC PHILRYLTTA VITNKDVRKR RQVLKDLVKV IQQESYTYKD PITEFVECLY 

       310        320        330        340        350        360 
VNFDFDGAQK KLRECESVLV NDFFLVACLE DFIENARLFI FETFCRIHQC ISINMLADKL 

       370        380        390        400        410        420 
NMTPEEAERW IVNLIRNARL DAKIDSKLGH VVMGNNAVSP YQQVIEKTKS LSFRSQMLAM 

       430        440 
NIEKKLNQNS RSEAPNWATQ DSGFY 

« Hide

References

« Hide 'large scale' references
[1]"The translation initiation factor eIF3-p48 subunit is encoded by int-6, a site of frequent integration by the mouse mammary tumor virus genome."
Asano K., Merrick W.C., Hershey J.W.B.
J. Biol. Chem. 272:23477-23480(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 280-289 AND 427-436, INTERACTION WITH EIF3A, IDENTIFICATION IN THE EIF-3 COMPLEX, TISSUE SPECIFICITY.
Tissue: Liver.
[2]"The chromosome location of the human homolog of the mouse mammary tumor-associated gene INT6 and its status in human breast carcinomas."
Miyazaki S., Imatani A., Ballard L., Marchetti A., Buttitta F., Albertsen H., Nevanlinna H.A., Gallahan D., Callahan R.
Genomics 46:155-158(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Lung.
[3]"Exclusion of Int-6 from PML nuclear bodies by binding to the HTLV-I Tax oncoprotein."
Desbois C., Rousset R., Bantignies F., Jalinot P.
Science 273:951-953(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Divergent subcellular locations of HTLV-I Tax and Int-6: a contrast between in vitro protein-protein binding and intracellular protein colocalization."
Neuvert C., Jin D.-Y., Semmes O.J., Diella F., Callahan R., Jeang K.-T.
J. Biomed. Sci. 4:229-234(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR LOCATION.
[5]"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].
[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 (JUL-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], VARIANT VAL-185.
Tissue: Bone marrow, Brain, Lung and Muscle.
[8]Bienvenut W.V., Heiserich L., Gottlieb E., Matallanas D., Cooper W.N., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9; 60-71; 164-172; 256-265 AND 370-376, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Mammary carcinoma.
[9]"Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies."
Morris-Desbois C., Bochard V., Reynaud C., Jalinot P.
J. Cell Sci. 112:3331-3342(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3C AND TRIM27, SUBCELLULAR LOCATION.
[10]"Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6 interact with the eIF3 core complex by binding to cognate eIF3b subunits."
Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L., Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.
J. Biol. Chem. 276:34948-34957(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3B.
[11]"The human protein HSPC021 interacts with Int-6 and is associated with eukaryotic translation initiation factor 3."
Morris-Desbois C., Rety S., Ferro M., Garin J., Jalinot P.
J. Biol. Chem. 276:45988-45995(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3L.
[12]"Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome."
Hoareau Alves K., Bochard V., Rety S., Jalinot P.
FEBS Lett. 527:15-21(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPS3; COPS6; COPS7 AND PSMC6.
[13]"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[14]"Induction and mode of action of the viral stress-inducible murine proteins, P56 and P54."
Terenzi F., Pal S., Sen G.C.
Virology 340:116-124(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFIT1.
[15]"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4G1, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Distinct induction patterns and functions of two closely related interferon-inducible human genes, ISG54 and ISG56."
Terenzi F., Hui D.J., Merrick W.C., Sen G.C.
J. Biol. Chem. 281:34064-34071(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFIT2.
[17]"Reconstitution reveals the functional core of mammalian eIF3."
Masutani M., Sonenberg N., Yokoyama S., Imataka H.
EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[18]"Human INT6/eIF3e is required for nonsense-mediated mRNA decay."
Morris C., Wittmann J., Jaeck H.-M., Jalinot P.
EMBO Rep. 8:596-602(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF3A; EIF3B; EIF3C; EIF4G1; NCBP1 AND UPF2.
[19]"Mammalian tumor suppressor Int6 specifically targets hypoxia inducible factor 2 alpha for degradation by hypoxia- and pVHL-independent regulation."
Chen L., Uchida K., Endler A., Shibasaki F.
J. Biol. Chem. 282:12707-12716(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EPAS1.
[20]"Isolation of the Schizosaccharomyces pombe proteasome subunit Rpn7 and a structure-function study of the proteasome-COP9-initiation factor domain."
Sha Z., Yen H.-C.S., Scheel H., Suo J., Hofmann K., Chang E.C.
J. Biol. Chem. 282:32414-32423(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-312.
[21]"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[22]"Human INT6 interacts with MCM7 and regulates its stability during S phase of the cell cycle."
Buchsbaum S., Morris C., Bochard V., Jalinot P.
Oncogene 26:5132-5144(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MCM7.
[23]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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 SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B.
[26]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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 SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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].
[29]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Structural roles for human translation factor eIF3 in initiation of protein synthesis."
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U54562 mRNA. Translation: AAC51760.1.
U94174 expand/collapse EMBL AC list , U94162, U94163, U94164, U94165, U94166, U94167, U94168, U94169, U94170, U94171, U94172, U94173 Genomic DNA. Translation: AAC51917.1.
U94175 mRNA. Translation: AAC51919.1.
U62962 mRNA. Translation: AAB58251.1.
U85947 mRNA. Translation: AAB88873.1.
CR542275 mRNA. Translation: CAG47071.1.
CH471060 Genomic DNA. Translation: EAW91918.1.
BC000734 mRNA. Translation: AAH00734.1.
BC008419 mRNA. Translation: AAH08419.1.
BC016706 mRNA. Translation: AAH16706.1.
BC017887 mRNA. Translation: AAH17887.1.
BC021679 mRNA. Translation: AAH21679.1.
CCDSCCDS6308.1.
RefSeqNP_001559.1. NM_001568.2.
UniGeneHs.405590.

3D structure databases

ProteinModelPortalP60228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109857. 83 interactions.
DIPDIP-32691N.
IntActP60228. 37 interactions.
MINTMINT-153842.
STRING9606.ENSP00000220849.

PTM databases

PhosphoSiteP60228.

Polymorphism databases

DMDM41019126.

Proteomic databases

MaxQBP60228.
PaxDbP60228.
PeptideAtlasP60228.
PRIDEP60228.

Protocols and materials databases

DNASU3646.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220849; ENSP00000220849; ENSG00000104408.
GeneID3646.
KEGGhsa:3646.
UCSCuc003ymt.3. human.

Organism-specific databases

CTD3646.
GeneCardsGC08M109284.
HGNCHGNC:3277. EIF3E.
HPAHPA023973.
HPA052182.
MIM602210. gene.
neXtProtNX_P60228.
PharmGKBPA27705.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324642.
HOVERGENHBG001097.
InParanoidP60228.
KOK03250.
OMADILTGKW.
PhylomeDBP60228.
TreeFamTF101518.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP60228.
BgeeP60228.
CleanExHS_EIF3E.
GenevestigatorP60228.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
HAMAPMF_03004. eIF3e.
InterProIPR016650. eIF3e.
IPR019010. eIF3e_N.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR10317. PTHR10317. 1 hit.
PfamPF09440. eIF3_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view]
PIRSFPIRSF016255. eIF3e_su6. 1 hit.
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3E. human.
GeneWikiEIF3S6.
GenomeRNAi3646.
NextBio14271.
PROP60228.
SOURCESearch...

Entry information

Entry nameEIF3E_HUMAN
AccessionPrimary (citable) accession number: P60228
Secondary accession number(s): O43902 expand/collapse secondary AC list , Q64058, Q64059, Q64252, Q6FG33, Q8WVK4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: July 9, 2014
This is version 123 of the entry and version 1 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

MIM cross-references

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

Translation initiation factors

List of translation initiation factor entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

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