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P78344 (IF4G2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4 gamma 2

Short name=eIF-4-gamma 2
Short name=eIF-4G 2
Short name=eIF4G 2
Alternative name(s):
Death-associated protein 5
Short name=DAP-5
p97
Gene names
Name:EIF4G2
Synonyms:DAP5
ORF Names:OK/SW-cl.75
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length907 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases. Ref.1 Ref.3 Ref.10 Ref.11

Subunit structure

Interacts with the serine/threonine protein kinases MKNK1 and MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD. Ref.1 Ref.2 Ref.9 Ref.14

Tissue specificity

Ubiquitously expressed in all adult tissues examined, with high levels in skeletal muscle and heart. Also expressed in fetal brain, lung, liver and kidney. Ref.1 Ref.2 Ref.3

Post-translational modification

Phosphorylation; hyperphosphorylated during mitosis. Ref.10

Miscellaneous

This gene has been shown to be extensively edited in the liver of APOBEC1 transgenic animal model. Its aberrant editing could contribute to the potent oncogenesis induced by overexpression of APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a fundamental translational repressor.

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 1 MI domain.

Contains 1 MIF4G domain.

Contains 1 W2 domain.

Caution

According to Ref.1, this sequence initiates exclusively at a GTG codon.

Sequence caution

The sequence BAB93515.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAD97268.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.

The sequence CAA61857.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P299914EBI-296519,EBI-8826747From a different organism.
EIF2S2P200424EBI-296519,EBI-711977
EIF4A1P608423EBI-296519,EBI-73449

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P78344-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P78344-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-471: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 907907Eukaryotic translation initiation factor 4 gamma 2
PRO_0000213325

Regions

Domain78 – 308231MIF4G
Domain543 – 666124MI
Domain720 – 904185W2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.16 Ref.21 Ref.22
Modified residue3951Phosphoserine Ref.18
Modified residue5081Phosphothreonine Ref.10 Ref.17
Modified residue5141Phosphothreonine Ref.15
Modified residue9021Phosphoserine Ref.18 Ref.20

Natural variations

Alternative sequence434 – 47138Missing in isoform 2.
VSP_038726
Natural variant2361L → M.
Corresponds to variant rs34885591 [ dbSNP | Ensembl ].
VAR_048923

Experimental info

Sequence conflict1691S → P in AAC51166. Ref.2
Sequence conflict2331K → Q in AAC51166. Ref.2
Sequence conflict2451K → Q in AAC51166. Ref.2
Sequence conflict3511F → L in AAC51166. Ref.2
Sequence conflict4411N → S in AAH18746. Ref.6
Sequence conflict5311A → G in AAC51166. Ref.2
Sequence conflict5341S → N in AAH43149. Ref.6
Sequence conflict6131A → G in AAC51166. Ref.2
Sequence conflict8611I → S in AAC51166. Ref.2
Sequence conflict8991E → G in AAC51166. Ref.2

Secondary structure

............................................................................... 907
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4EF050B5EEA4DF91

FASTA907102,362
        10         20         30         40         50         60 
MESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW IPARSTRRDD 

        70         80         90        100        110        120 
NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL LNVGVESKLI LKGVILLIVD 

       130        140        150        160        170        180 
KALEEPKYSS LYAQLCLRLA EDAPNFDGPA AEGQPGQKQS TTFRRLLISK LQDEFENRTR 

       190        200        210        220        230        240 
NVDVYDKREN PLLPEEEEQR AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK 

       250        260        270        280        290        300 
RVQLKDMGED LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD 

       310        320        330        340        350        360 
TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGMRSDF FLEGPFMPPR 

       370        380        390        400        410        420 
MKMDRDPLGG LADMFGQMPG SGIGTGPGVI QDRFSPTMGR HRSNQLFNGH GGHIMPPTQS 

       430        440        450        460        470        480 
QFGEMGGKFM KSQGLSQLYH NQSQGLLSQL QGQSKDMPPR FSKKGQLNAD EISLRPAQSF 

       490        500        510        520        530        540 
LMNKNQVPKL QPQITMIPPS AQPPRTQTPP LGQTPQLGLK TNPPLIQEKP AKTSKKPPPS 

       550        560        570        580        590        600 
KEELLKLTET VVTEYLNSGN ANEAVNGVRE MRAPKHFLPE MLSKVIILSL DRSDEDKEKA 

       610        620        630        640        650        660 
SSLISLLKQE GIATSDNFMQ AFLNVLDQCP KLEVDIPLVK SYLAQFAARA IISELVSISE 

       670        680        690        700        710        720 
LAQPLESGTH FPLFLLCLQQ LAKLQDREWL TELFQQSKVN MQKMLPEIDQ NKDRMLEILE 

       730        740        750        760        770        780 
GKGLSFLFPL LKLEKELLKQ IKLDPSPQTI YKWIKDNISP KLHVDKGFVN ILMTSFLQYI 

       790        800        810        820        830        840 
SSEVNPPSDE TDSSSAPSKE QLEQEKQLLL SFKPVMQKFL HDHVDLQVSA LYALQVHCYN 

       850        860        870        880        890        900 
SNFPKGMLLR FFVHFYDMEI IEEEAFLAWK EDITQEFPGK GKALFQVNQW LTWLETAEEE 


ESEEEAD 

« Hide

Isoform 2 [UniParc].

Checksum: F400E1E28654A2E4
Show »

FASTA86998,150

References

« Hide 'large scale' references
[1]"A new translational regulator with homology to eukaryotic translation initiation factor 4G."
Imataka H., Olsen H.S., Sonenberg N.
EMBO J. 16:817-825(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION OF A NON-AUG INITIATOR START CODON, INTERACTION WITH EIF4A AND EIF3.
Tissue: Placenta.
[2]"A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme."
Yamanaka S., Poksay K.S., Arnold K.S., Innerarity T.L.
Genes Dev. 11:321-333(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH EIF4A.
Tissue: Liver.
[3]"DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death."
Levy-Strumpf N., Deiss L.P., Berissi H., Kimchi A.
Mol. Cell. Biol. 17:1615-1625(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Kidney.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Retinal pigment epithelium, Skin and Testis.
[7]"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 1-12, ACETYLATION AT MET-1.
Tissue: Platelet.
[8]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-907.
Tissue: Colon adenocarcinoma.
[9]"Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKNK1.
[10]"Suppression of cap-dependent translation in mitosis."
Pyronnet S., Dostie J., Sonenberg N.
Genes Dev. 15:2083-2093(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[11]"The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins."
Henis-Korenblit S., Shani G., Sines T., Marash L., Shohat G., Kimchi A.
Proc. Natl. Acad. Sci. U.S.A. 99:5400-5405(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[14]"SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIF4GD.
[15]"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-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-395 AND SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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 SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73824 mRNA. Translation: AAB49973.1.
U76111 mRNA. Translation: AAC51166.1.
X89713 mRNA. Translation: CAA61857.1. Sequence problems.
AK223548 mRNA. Translation: BAD97268.1. Sequence problems.
AC116535 Genomic DNA. No translation available.
BC014930 mRNA. Translation: AAH14930.2.
BC018746 mRNA. Translation: AAH18746.1.
BC018975 mRNA. Translation: AAH18975.1.
BC039851 mRNA. Translation: AAH39851.1.
BC043149 mRNA. Translation: AAH43149.2.
BC111415 mRNA. Translation: AAI11416.1.
BC111548 mRNA. Translation: AAI11549.2.
AB063323 mRNA. Translation: BAB93515.1. Different initiation.
RefSeqNP_001036024.3. NM_001042559.2.
NP_001166176.1. NM_001172705.1.
NP_001409.3. NM_001418.3.
UniGeneHs.183684.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D3MX-ray1.90A/B730-897[»]
3L6AX-ray2.00A540-897[»]
4IULX-ray2.30A/B61-323[»]
ProteinModelPortalP78344.
SMRP78344. Positions 78-311, 540-897.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108297. 21 interactions.
DIPDIP-31366N.
IntActP78344. 17 interactions.
MINTMINT-1182471.
STRING9606.ENSP00000340281.

PTM databases

PhosphoSiteP78344.

Polymorphism databases

DMDM30315906.

Proteomic databases

PaxDbP78344.
PRIDEP78344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339995; ENSP00000340281; ENSG00000110321.
GeneID1982.
KEGGhsa:1982.
UCSCuc001mjb.3. human. [P78344-1]
uc001mjd.3. human. [P78344-2]

Organism-specific databases

CTD1982.
GeneCardsGC11M010775.
HGNCHGNC:3297. EIF4G2.
HPACAB005163.
HPA006773.
HPA016965.
MIM602325. gene.
neXtProtNX_P78344.
PharmGKBPA27723.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301289.
HOVERGENHBG052084.
InParanoidP78344.
KOK03260.
OrthoDBEOG73FQMQ.
PhylomeDBP78344.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP78344.
BgeeP78344.
CleanExHS_EIF4G2.
GenevestigatorP78344.

Family and domain databases

Gene3D1.25.40.180. 3 hits.
InterProIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
IPR003307. W2_domain.
[Graphical view]
PfamPF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTSM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
PROSITEPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4G2. human.
EvolutionaryTraceP78344.
GeneWikiEIF4G2.
GenomeRNAi1982.
NextBio8025.
PMAP-CutDBP78344.
PROP78344.
SOURCESearch...

Entry information

Entry nameIF4G2_HUMAN
AccessionPrimary (citable) accession number: P78344
Secondary accession number(s): O60877 expand/collapse secondary AC list , P78404, Q0VH00, Q0VH01, Q2NKW9, Q49A79, Q53EU1, Q58EZ2, Q8NI71, Q96C16
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 133 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

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 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 11

Human chromosome 11: entries, gene names and cross-references to MIM