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P60228

- EIF3E_HUMAN

UniProt

P60228 - EIF3E_HUMAN

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Protein

Eukaryotic translation initiation factor 3 subunit E

Gene

EIF3E

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

Functioni

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.3 PublicationsUniRule annotation

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein N-terminus binding Source: UniProtKB
  3. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
  3. gene expression Source: Reactome
  4. negative regulation of translational initiation Source: UniProtKB
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  6. regulation of translational initiation Source: UniProtKB
  7. translation Source: Reactome
  8. translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit EUniRule annotation
Short name:
eIF3eUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 6UniRule annotation
Viral integration site protein INT-6 homolog
eIF-3 p48UniRule annotation
Gene namesi
Name:EIF3EUniRule annotation
Synonyms:EIF3S6UniRule annotation, INT6UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3277. EIF3E.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  4. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  5. eukaryotic translation initiation factor 3 complex Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
  7. membrane Source: UniProtKB
  8. nucleoplasm Source: UniProtKB
  9. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi312 – 3121L → D: Promotes nuclear accumulation. 1 Publication

Organism-specific databases

PharmGKBiPA27705.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 PublicationsUniRule annotation
Chaini2 – 445444Eukaryotic translation initiation factor 3 subunit EPRO_0000123515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 PublicationsUniRule annotation
Modified residuei399 – 3991Phosphoserine2 Publications
Modified residuei439 – 4391PhosphothreonineBy similarity
Modified residuei445 – 4451PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP60228.
PaxDbiP60228.
PeptideAtlasiP60228.
PRIDEiP60228.

PTM databases

PhosphoSiteiP60228.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus.2 Publications

Gene expression databases

BgeeiP60228.
CleanExiHS_EIF3E.
ExpressionAtlasiP60228. baseline and differential.
GenevestigatoriP60228.

Organism-specific databases

HPAiHPA023973.
HPA052182.

Interactioni

Subunit structurei

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 IFIT2.15 PublicationsUniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109857. 87 interactions.
DIPiDIP-32691N.
IntActiP60228. 37 interactions.
MINTiMINT-153842.
STRINGi9606.ENSP00000220849.

Structurei

3D structure databases

ProteinModelPortaliP60228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini290 – 395106PCIUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 128125Sufficient for interaction with EPAS1Add
BLAST
Regioni9 – 195187Sufficient for interaction with TRIM27Add
BLAST
Regioni351 – 44595Sufficient for interaction with MCM7Add
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit E family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Phylogenomic databases

eggNOGiNOG324642.
GeneTreeiENSGT00390000002661.
HOVERGENiHBG001097.
InParanoidiP60228.
KOiK03250.
OMAiDILTGKW.
PhylomeDBiP60228.
TreeFamiTF101518.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03004. eIF3e.
InterProiIPR016650. eIF3e.
IPR019010. eIF3e_N.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10317. PTHR10317. 1 hit.
PfamiPF09440. eIF3_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view]
PIRSFiPIRSF016255. eIF3e_su6. 1 hit.
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P60228 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM
60 70 80 90 100
VDFAMDVYKN LYSDDIPHAL REKRTTVVAQ LKQLQAETEP IVKMFEDPET
110 120 130 140 150
TRQMQSTRDG RMLFDYLADK HGFRQEYLDT LYRYAKFQYE CGNYSGAAEY
160 170 180 190 200
LYFFRVLVPA TDRNALSSLW GKLASEILMQ NWDAAMEDLT RLKETIDNNS
210 220 230 240 250
VSSPLQSLQQ RTWLIHWSLF VFFNHPKGRD NIIDLFLYQP QYLNAIQTMC
260 270 280 290 300
PHILRYLTTA VITNKDVRKR RQVLKDLVKV IQQESYTYKD PITEFVECLY
310 320 330 340 350
VNFDFDGAQK KLRECESVLV NDFFLVACLE DFIENARLFI FETFCRIHQC
360 370 380 390 400
ISINMLADKL NMTPEEAERW IVNLIRNARL DAKIDSKLGH VVMGNNAVSP
410 420 430 440
YQQVIEKTKS LSFRSQMLAM NIEKKLNQNS RSEAPNWATQ DSGFY
Length:445
Mass (Da):52,221
Last modified:January 16, 2004 - v1
Checksum:iA5368651DD0DDD0C
GO

Mass spectrometryi

Molecular mass is 52131.8 Da from positions 1 - 445. 1 Publication
Molecular mass is 52133.4±0.2 Da from positions 1 - 445. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti185 – 1851A → V.1 Publication
Corresponds to variant rs17856554 [ dbSNP | Ensembl ].
VAR_046480

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U54562 mRNA. Translation: AAC51760.1.
U94174
, 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.
CCDSiCCDS6308.1.
RefSeqiNP_001559.1. NM_001568.2.
UniGeneiHs.405590.

Genome annotation databases

EnsembliENST00000220849; ENSP00000220849; ENSG00000104408.
GeneIDi3646.
KEGGihsa:3646.
UCSCiuc003ymt.3. human.

Polymorphism databases

DMDMi41019126.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U54562 mRNA. Translation: AAC51760.1 .
U94174
, 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 .
CCDSi CCDS6308.1.
RefSeqi NP_001559.1. NM_001568.2.
UniGenei Hs.405590.

3D structure databases

ProteinModelPortali P60228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109857. 87 interactions.
DIPi DIP-32691N.
IntActi P60228. 37 interactions.
MINTi MINT-153842.
STRINGi 9606.ENSP00000220849.

PTM databases

PhosphoSitei P60228.

Polymorphism databases

DMDMi 41019126.

Proteomic databases

MaxQBi P60228.
PaxDbi P60228.
PeptideAtlasi P60228.
PRIDEi P60228.

Protocols and materials databases

DNASUi 3646.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220849 ; ENSP00000220849 ; ENSG00000104408 .
GeneIDi 3646.
KEGGi hsa:3646.
UCSCi uc003ymt.3. human.

Organism-specific databases

CTDi 3646.
GeneCardsi GC08M109215.
HGNCi HGNC:3277. EIF3E.
HPAi HPA023973.
HPA052182.
MIMi 602210. gene.
neXtProti NX_P60228.
PharmGKBi PA27705.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324642.
GeneTreei ENSGT00390000002661.
HOVERGENi HBG001097.
InParanoidi P60228.
KOi K03250.
OMAi DILTGKW.
PhylomeDBi P60228.
TreeFami TF101518.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF3E. human.
GeneWikii EIF3S6.
GenomeRNAii 3646.
NextBioi 14271.
PROi P60228.
SOURCEi Search...

Gene expression databases

Bgeei P60228.
CleanExi HS_EIF3E.
ExpressionAtlasi P60228. baseline and differential.
Genevestigatori P60228.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
HAMAPi MF_03004. eIF3e.
InterProi IPR016650. eIF3e.
IPR019010. eIF3e_N.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR10317. PTHR10317. 1 hit.
Pfami PF09440. eIF3_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view ]
PIRSFi PIRSF016255. eIF3e_su6. 1 hit.
SMARTi SM00088. PINT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiEIF3E_HUMAN
AccessioniPrimary (citable) accession number: P60228
Secondary accession number(s): O43902
, Q64058, Q64059, Q64252, Q6FG33, Q8WVK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: October 29, 2014
This is version 126 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3