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O43432 (IF4G3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4 gamma 3

Short name=eIF-4-gamma 3
Short name=eIF-4G 3
Short name=eIF4G 3
Alternative name(s):
eIF-4-gamma II
Short name=eIF4GII
Gene names
Name:EIF4G3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1585 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1. Ref.1

Subunit structure

Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a complex with EIF4E. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA By similarity. Ref.1 Ref.6

Post-translational modification

Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription. Ref.8 Ref.9

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 5 HEAT repeats.

Contains 1 MI domain.

Contains 1 MIF4G domain.

Contains 1 W2 domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein biosynthesis
Translation regulation
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

positive regulation of meiosis I

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of translation

Inferred from electronic annotation. Source: Ensembl

regulation of translational initiation

Traceable author statement Ref.1. Source: ProtInc

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionRNA cap binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

translation factor activity, nucleic acid binding

Traceable author statement Ref.1. Source: ProtInc

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43432-1)

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: O43432-2)

The sequence of this isoform differs from the canonical sequence as follows:
     11-11: F → FAAGPRPPHHQF
     499-504: AQIAIT → ETSNEC
     505-1585: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O43432-3)

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: P → PGGFRPIQ
     182-182: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: O43432-4)

The sequence of this isoform differs from the canonical sequence as follows:
     219-498: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15851585Eukaryotic translation initiation factor 4 gamma 3
PRO_0000213329

Regions

Repeat745 – 78339HEAT 1
Domain755 – 983229MIF4G
Repeat784 – 83148HEAT 2
Repeat832 – 90574HEAT 3
Repeat906 – 94439HEAT 4
Repeat945 – 98440HEAT 5
Domain1221 – 1343123MI
Domain1416 – 1585170W2
Region134 – 16229PABPC1-binding
Region619 – 63012EIF4E-binding By similarity
Region699 – 1019321eIF3/EIF4A-binding By similarity
Region1433 – 1585153EIF4A-binding By similarity
Region1571 – 158515Necessary but not sufficient for MKNK1-binding By similarity
Coiled coil447 – 47529 Potential
Coiled coil994 – 102330 Potential

Sites

Site699 – 7002Cleavage; by enterovirus/rhinovirus protease 2A
Site700 – 7012Cleavage; by foot-and-mouth disease virus leader protease

Amino acid modifications

Modified residue1681Phosphothreonine By similarity
Modified residue2301Phosphoserine Ref.17 Ref.19
Modified residue2321Phosphoserine Ref.17 Ref.19
Modified residue2671Phosphoserine By similarity
Modified residue4951Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
Modified residue11561Phosphoserine; by CaMK1 Ref.7

Natural variations

Alternative sequence101P → PGGFRPIQ in isoform 3.
VSP_043447
Alternative sequence111F → FAAGPRPPHHQF in isoform 2.
VSP_010487
Alternative sequence1821Missing in isoform 3.
VSP_043448
Alternative sequence219 – 498280Missing in isoform 4.
VSP_054502
Alternative sequence499 – 5046AQIAIT → ETSNEC in isoform 2.
VSP_010488
Alternative sequence505 – 15851081Missing in isoform 2.
VSP_010489
Natural variant3781Q → R.
Corresponds to variant rs35731992 [ dbSNP | Ensembl ].
VAR_048924
Natural variant4961P → A.
Corresponds to variant rs35176330 [ dbSNP | Ensembl ].
VAR_034009
Natural variant11851D → E.
Corresponds to variant rs2230572 [ dbSNP | Ensembl ].
VAR_048925

Experimental info

Mutagenesis7561R → D: Reduces binding to EIF4A; when associated with D-759 and D-764. Ref.21
Mutagenesis7591R → D: Reduces binding to EIF4A; when associated with D-756 and D-764. Ref.21
Mutagenesis7641K → D: Reduces binding to EIF4A; when associated with D-756 and D-759. Ref.21
Mutagenesis8141R → D: Reduces binding to EIF4A; when associated with D-820. Ref.21
Mutagenesis8201K → D: Reduces binding to EIF4A; when associated with D-814. Ref.21
Mutagenesis834 – 8352RK → DD: Reduces binding to IRES.
Sequence conflict1591M → I in AAH30578. Ref.4
Sequence conflict3331D → G in AAH30578. Ref.4

Secondary structure

......................... 1585
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 2.
Checksum: EA483139373DCA5C

FASTA1,585176,652
        10         20         30         40         50         60 
MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM VNHLPMPYPV 

        70         80         90        100        110        120 
PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFPNAYGT PFYPSQPVYQ 

       130        140        150        160        170        180 
SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPTSTPTP 

       190        200        210        220        230        240 
PQQLPSQVPE HSPVVYGTVE SAHLAASTPV TAASDQKQEE KPKPDPVLKS PSPVLRLVLS 

       250        260        270        280        290        300 
GEKKEQEGQT SETTAIVSIA ELPLPPSPTT VSSVARSTIA APTSSALSSQ PIFTTAIDDR 

       310        320        330        340        350        360 
CELSSPREDT IPIPSLTSCT ETSDPLPTNE NDDDICKKPC SVAPNDIPLV SSTNLINEIN 

       370        380        390        400        410        420 
GVSEKLSATE SIVEIVKQEV LPLTLELEIL ENPPEEMKLE CIPAPITPST VPSFPPTPPT 

       430        440        450        460        470        480 
PPASPPHTPV IVPAAATTVS SPSAAITVQR VLEEDESIRT CLSEDAKEIQ NKIEVEADGQ 

       490        500        510        520        530        540 
TEEILDSQNL NSRRSPVPAQ IAITVPKTWK KPKDRTRTTE EMLEAELELK AEEELSIDKV 

       550        560        570        580        590        600 
LESEQDKMSQ GFHPERDPSD LKKVKAVEEN GEEAEPVRNG AESVSEGEGI DANSGSTDSS 

       610        620        630        640        650        660 
GDGVTFPFKP ESWKPTDTEG KKQYDREFLL DFQFMPACIQ KPEGLPPISD VVLDKINQPK 

       670        680        690        700        710        720 
LPMRTLDPRI LPRGPDFTPA FADFGRQTPG GRGVPLLNVG SRRSQPGQRR EPRKIITVSV 

       730        740        750        760        770        780 
KEDVHLKKAE NAWKPSQKRD SQADDPENIK TQELFRKVRS ILNKLTPQMF NQLMKQVSGL 

       790        800        810        820        830        840 
TVDTEERLKG VIDLVFEKAI DEPSFSVAYA NMCRCLVTLK VPMADKPGNT VNFRKLLLNR 

       850        860        870        880        890        900 
CQKEFEKDKA DDDVFEKKQK ELEAASAPEE RTRLHDELEE AKDKARRRSI GNIKFIGELF 

       910        920        930        940        950        960 
KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD QYFNQMEKIV 

       970        980        990       1000       1010       1020 
KERKTSSRIR FMLQDVIDLR LCNWVSRRAD QGPKTIEQIH KEAKIEEQEE QRKVQQLMTK 

      1030       1040       1050       1060       1070       1080 
EKRRPGVQRV DEGGWNTVQG AKNSRVLDPS KFLKITKPTI DEKIQLVPKA QLGSWGKGSS 

      1090       1100       1110       1120       1130       1140 
GGAKASETDA LRSSASSLNR FSALQPPAPS GSTPSTPVEF DSRRTLTSRG SMGREKNDKP 

      1150       1160       1170       1180       1190       1200 
LPSATARPNT FMRGGSSKDL LDNQSQEEQR REMLETVKQL TGGVDVERNS TEAERNKTRE 

      1210       1220       1230       1240       1250       1260 
SAKPEISAMS AHDKAALSEE ELERKSKSII DEFLHINDFK EAMQCVEELN AQGLLHVFVR 

      1270       1280       1290       1300       1310       1320 
VGVESTLERS QITRDHMGQL LYQLVQSEKL SKQDFFKGFS ETLELADDMA IDIPHIWLYL 

      1330       1340       1350       1360       1370       1380 
AELVTPMLKE GGISMRELTI EFSKPLLPVG RAGVLLSEIL HLLCKQMSHK KVGALWREAD 

      1390       1400       1410       1420       1430       1440 
LSWKDFLPEG EDVHNFLLEQ KLDFIESDSP CSSEALSKKE LSAEELYKRL EKLIIEDKAN 

      1450       1460       1470       1480       1490       1500 
DEQIFDWVEA NLDEIQMSSP TFLRALMTAV CKAAIIADSS TFRVDTAVIK QRVPILLKYL 

      1510       1520       1530       1540       1550       1560 
DSDTEKELQA LYALQASIVK LDQPANLLRM FFDCLYDEEV ISEDAFYKWE SSKDPAEQNG 

      1570       1580 
KGVALKSVTA FFTWLREAEE ESEDN 

« Hide

Isoform 2 [UniParc].

Checksum: 0B4E961F10F62EA0
Show »

FASTA51555,227
Isoform 3 [UniParc].

Checksum: A6A4BEC78E05CC92
Show »

FASTA1,591177,280
Isoform 4 [UniParc].

Checksum: EDF74715CD55642D
Show »

FASTA1,305146,871

References

« Hide 'large scale' references
[1]"A novel functional human eukaryotic translation initiation factor 4G."
Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N.
Mol. Cell. Biol. 18:334-342(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EIF4A; EIF4E AND EIF3.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"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 2; 3 AND 4).
Tissue: PNS and Testis.
[5]"Characterization of secretory proteins of human ovarian follicle cells by cDNA cloning."
Klaudiny J.J., von der Kammer H.H., Scheit K.K.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 887-1585 (ISOFORM 1).
Tissue: Ovary.
[6]"A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation."
Imataka H., Gradi A., Sonenberg N.
EMBO J. 17:7480-7489(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1.
[7]"Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I."
Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.
J. Biol. Chem. 278:48570-48579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1156 BY CAMK1.
[8]"Human rhin4ovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different."
Gradi A., Svitkin Y.V., Sommergruber W., Imataka H., Morino S., Skern T., Sonenberg N.
J. Virol. 77:5026-5029(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY RHINOVIRUS PROTEASE.
[9]"Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro."
Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T., Belsham G.J.
J. Virol. 78:3271-3278(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS PROTEASE.
[10]"eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation."
Gingras A.-C., Raught B., Sonenberg N.
Annu. Rev. Biochem. 68:913-963(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[14]"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-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"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 SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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-230; SER-232 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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-230; SER-232 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII."
Miura T., Shiratori Y., Shimma N.
J. Biomol. NMR 27:279-280(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 621-637 IN COMPLEX WITH EIF4E.
[21]"A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery."
Marcotrigiano J., Lomakin I.B., Sonenberg N., Pestova T.V., Hellen C.U.T., Burley S.K.
Mol. Cell 7:193-203(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 745-986, MUTAGENESIS OF ARG-756; ARG-759; LYS-764; ARG-814; LYS-820 AND 834-ARG-LYS-835.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012072 mRNA. Translation: AAC02903.2.
AL031005 Genomic DNA. No translation available.
AL358392, AL606477, AL627311 Genomic DNA. Translation: CAI12155.1.
AL606477, AL358392, AL627311 Genomic DNA. Translation: CAI12534.1.
AL627311, AL358392, AL606477 Genomic DNA. Translation: CAI14553.1.
AL672037 Genomic DNA. No translation available.
CH471134 Genomic DNA. Translation: EAW94956.1.
BC030578 mRNA. Translation: AAH30578.1.
BC094683 mRNA. Translation: AAH94683.1.
BC136643 mRNA. Translation: AAI36644.1.
Z34918 mRNA. Translation: CAA84397.1.
CCDSCCDS214.1. [O43432-1]
CCDS55580.1. [O43432-3]
CCDS59192.1. [O43432-2]
PIRS49172.
RefSeqNP_001185730.1. NM_001198801.1.
NP_001185731.1. NM_001198802.1. [O43432-3]
NP_001185732.1. NM_001198803.1. [O43432-2]
NP_003751.2. NM_003760.4. [O43432-1]
UniGeneHs.467084.
Hs.732241.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU3X-ray2.37A745-1003[»]
ProteinModelPortalO43432.
SMRO43432. Positions 136-161, 745-986, 1214-1551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114220. 15 interactions.
DIPDIP-33245N.
IntActO43432. 11 interactions.
MINTMINT-85560.
STRING9606.ENSP00000264211.

PTM databases

PhosphoSiteO43432.

Proteomic databases

MaxQBO43432.
PaxDbO43432.
PRIDEO43432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264211; ENSP00000264211; ENSG00000075151. [O43432-1]
ENST00000356916; ENSP00000349386; ENSG00000075151. [O43432-2]
ENST00000374935; ENSP00000364071; ENSG00000075151.
ENST00000374937; ENSP00000364073; ENSG00000075151. [O43432-3]
ENST00000400422; ENSP00000383274; ENSG00000075151. [O43432-1]
ENST00000602326; ENSP00000473510; ENSG00000075151. [O43432-3]
GeneID8672.
KEGGhsa:8672.
UCSCuc001bec.3. human. [O43432-1]
uc001bee.3. human. [O43432-3]
uc001beh.3. human. [O43432-2]

Organism-specific databases

CTD8672.
GeneCardsGC01M021132.
HGNCHGNC:3298. EIF4G3.
HPAHPA025031.
HPA025039.
HPA025041.
MIM603929. gene.
neXtProtNX_O43432.
PharmGKBPA27724.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301289.
HOVERGENHBG052083.
InParanoidO43432.
KOK03260.
OMAICKKSCS.
OrthoDBEOG7D59N2.
PhylomeDBO43432.
TreeFamTF101527.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO43432.
BgeeO43432.
CleanExHS_EIF4G3.
GenevestigatorO43432.

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

ChiTaRSEIF4G3. human.
EvolutionaryTraceO43432.
GeneWikiEIF4G3.
GenomeRNAi8672.
NextBio32529.
PMAP-CutDBO43432.
PROO43432.
SOURCESearch...

Entry information

Entry nameIF4G3_HUMAN
AccessionPrimary (citable) accession number: O43432
Secondary accession number(s): B9EGQ7 expand/collapse secondary AC list , Q15597, Q504Z1, Q5SWC3, Q8NEN1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 134 of the entry and version 2 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 1

Human chromosome 1: entries, gene names and cross-references to MIM