Eukaryotic translation initiation factor 3 subunit E

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P60228 (EIF3E_HUMAN)

Last modified July 7, 2009. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Eukaryotic translation initiation factor 3 subunit E
      Short name=eIF3e
Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 6
    eIF-3 p48
    Viral integration site protein INT-6 homolog

Gene names

Name:	EIF3E
Synonyms:	EIF3S6, INT6

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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 posttermination 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.15 Ref.16 Ref.19
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 FRAP1 and RAPTOR, 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. Ref.15 Ref.16 Ref.19 Ref.1 Ref.3 Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.22
Subcellular location	Cytoplasm. Nucleus. Note: Localizes to PML bodies. Ref.3 Ref.4 Ref.7 Ref.17
Tissue specificity	Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus. Ref.1 Ref.3
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.
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.18 Molecular mass is 52133.4±0.2 Da from positions 1 - 445. Determined by MALDI. Ref.22

Hide | Top

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of translational initiation Non-traceable author statement. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype. Source: UniProtKB translational initiation Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation initiation factor 3 complex Ref.1 Inferred from direct assay. Source: UniProtKB nucleoplasm Ref.15 Non-traceable author statement. Source: UniProtKB
Molecular function	protein N-terminus binding Inferred from physical interaction. Source: UniProtKB translation initiation factor activity Ref.1 Inferred by curator. Source: UniProtKB
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
BAT2	P48634	1	EBI-347740,EBI-347545
CNTF	P26441	1	EBI-347740,EBI-1050897
EIF1B	O60739	1	EBI-347740,EBI-1043343
EIF3A	Q14152	1	EBI-347740,EBI-366617
EIF3C	Q99613	2	EBI-347740,EBI-353741
EPAS1	Q99814	7	EBI-347740,EBI-447470
MAGED1	Q9Y5V3	1	EBI-347740,EBI-716006
NDRG1	Q92597	1	EBI-347740,EBI-716486
RGS2	P41220	1	EBI-347740,EBI-712388
SAP18	O00422	1	EBI-347740,EBI-1044156
TRIM27	P14373	4	EBI-347740,EBI-719493

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6 Ref.18

Chain

2 – 445

444

Eukaryotic translation initiation factor 3 subunit E

PRO_0000123515

Regions

Domain

290 – 395

106

PCI

Region

4 – 128

125

Sufficient for interaction with EPAS1

Region

9 – 195

187

Sufficient for interaction with TRIM27

Region

351 – 445

Sufficient for interaction with MCM7

Amino acid modifications

Modified residue

N-acetylalanine Ref.6 Ref.18

Modified residue

399

Phosphoserine Ref.20 Ref.21

Modified residue

439

Phosphothreonine By similarity

Modified residue

445

Phosphotyrosine Ref.11

Natural variations

Natural variant

185

A → V: dbSNP rs17856554. Ref.5

VAR_046480

Experimental info

Mutagenesis

312

L → D: Promotes nuclear accumulation. Ref.17

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P60228-1 [UniParc].

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

FASTA

445

52,221

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 9295280] [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: 9403073] [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: 8688078] [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: 12386384] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TAX-1, SUBCELLULAR LOCATION.
[5]	"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], VARIANT VAL-185. Tissue: Bone marrow, Brain, Lung and Muscle.
[6]	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, MASS SPECTROMETRY. Tissue: Colon carcinoma and Mammary carcinoma.
[7]	"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: 10504338] [Abstract] Cited for: INTERACTION WITH EIF3C AND TRIM27, SUBCELLULAR LOCATION.
[8]	"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: 11457827] [Abstract] Cited for: INTERACTION WITH EIF3B.
[9]	"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: 11590142] [Abstract] Cited for: INTERACTION WITH EIF3L.
[10]	"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: 12220626] [Abstract] Cited for: INTERACTION WITH COPS3; COPS6; COPS7 AND PSMC6.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-445, MASS SPECTROMETRY.
[12]	"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: 15703437] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[13]	"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: 16766523] [Abstract] Cited for: INTERACTION WITH EIF4G1, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[14]	"Reconstitution reveals the functional core of mammalian eIF3." Masutani M., Sonenberg N., Yokoyama S., Imataka H. EMBO J. 26:3373-3383(2007) [PubMed: 17581632] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[15]	"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: 17468741] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF3A; EIF3B; EIF3C; EIF4G1; NCBP1 AND UPF2.
[16]	"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: 17324924] [Abstract] Cited for: FUNCTION, INTERACTION WITH EPAS1.
[17]	"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: 17761670] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-312.
[18]	"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: 17322308] [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.
[19]	"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: 17310990] [Abstract] Cited for: FUNCTION, INTERACTION WITH MCM7.
[20]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, MASS SPECTROMETRY.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, MASS SPECTROMETRY.
[22]	"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: 18599441] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"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: 16322461] [Abstract] Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
	U54562 mRNA. Translation: AAC51760.1. U94174 U94173 Genomic DNA. Translation: AAC51917.1. U94175 mRNA. Translation: AAC51919.1. U62962 mRNA. Translation: AAB58251.1. U85947 mRNA. Translation: AAB88873.1. 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.
IPI	IPI00013068.
RefSeq	NP_001559.1.
UniGene	Hs.405590
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P60228. 28 interactions.
PTM databases
PhosphoSite	P60228.
Proteomic databases
PeptideAtlas	P60228.
PRIDE	P60228.
Genome annotation databases
Ensembl	ENSG00000104408. Homo sapiens. [Contig view]
GeneID	3646.
KEGG	hsa:3646.
UCSC	uc003ymu.1. human.
Organism-specific databases
GeneCards	GC08M109284.
H-InvDB	HIX0007722.
HGNC	HGNC:3277. EIF3E.
MIM	602210. gene.
PharmGKB	PA27705.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P60228.
HOVERGEN	P60228.
OMA	P60228. NARLMIF.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P60228.
Bgee	P60228.
CleanEx	HS_EIF3E.
GermOnline	ENSG00000104408. Homo sapiens.
Family and domain databases
InterPro	IPR019010. eIF3_su6_N. IPR000717. PCI. IPR016650. Transl_init_fac_3_su6_euk. [Graphical view]
Pfam	PF09440. eIF3_N. 1 hit. PF01399. PCI. 1 hit. [Graphical view]
PIRSF	PIRSF016255. eIF3e_su6. 1 hit.
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	14271.
SOURCE	Search...

Hide | Top

Entry information

Entry name

EIF3E_HUMAN

Accession

Primary (citable) accession number: P60228
Secondary accession number(s): O43902

Q8WVK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	July 7, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 8

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Translation initiation factors

List of translation initiation factor entries

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents