Reviewed, UniProtKB/Swiss-Prot O43432 (IF4G3_HUMAN)

Names and origin

Protein names

Recommended 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

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

Protein attributes

Sequence length	1585 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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 eIF4G family. Contains 5 HEAT repeats. Contains 1 MI domain. Contains 1 MIF4G domain. Contains 1 W2 domain.

Ontologies

Keywords
Biological process	Host-virus interaction Protein biosynthesis Translation regulation
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	RNA metabolic process Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of translational initiation Ref.1 Traceable author statement. Source: ProtInc translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	eukaryotic translation initiation factor 4F complex Ref.1 Traceable author statement. Source: ProtInc
Molecular function	RNA cap binding Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4A1	P60842	1	EBI-464766,EBI-73449
EIF4A2	Q14240	1	EBI-464766,EBI-73473
NCBP1	Q09161	1	EBI-464766,EBI-464743

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1585

1585

Eukaryotic translation initiation factor 4 gamma 3

PRO_0000213329

Regions

Repeat

745 – 783

39

HEAT 1

Domain

755 – 983

229

MIF4G

Repeat

784 – 831

48

HEAT 2

Repeat

832 – 905

74

HEAT 3

Repeat

906 – 944

39

HEAT 4

Repeat

945 – 984

40

HEAT 5

Domain

1221 – 1343

123

MI

Domain

1416 – 1585

170

W2

Region

134 – 162

29

PABPC1-binding

Region

619 – 630

12

EIF4E-binding By similarity

Region

699 – 1019

321

eIF3/EIF4A-binding By similarity

Region

1433 – 1585

153

EIF4A-binding By similarity

Region

1571 – 1585

15

Necessary but not sufficient for MKNK1-binding By similarity

Coiled coil

447 – 475

29

Potential

Coiled coil

994 – 1023

30

Potential

Sites

Site

699 – 700

2

Cleavage; by enterovirus/rhinovirus protease 2A

Site

700 – 701

2

Cleavage; by foot-and-mouth disease virus leader protease

Amino acid modifications

Modified residue

230

1

Phosphoserine Ref.11

Modified residue

232

1

Phosphoserine Ref.11 Ref.15

Modified residue

240

1

Phosphoserine By similarity

Modified residue

267

1

Phosphoserine By similarity

Modified residue

495

1

Phosphoserine Ref.11 Ref.15 Ref.12 Ref.13 Ref.14 Ref.16

Modified residue

944

1

N6-acetyllysine Ref.18

Modified residue

1156

1

Phosphoserine; by CaMK1 Ref.7

Natural variations

Alternative sequence

11

1

F → FAAGPRPPHHQF in isoform 2.

VSP_010487

Alternative sequence

499 – 504

6

AQIAIT → ETSNEC in isoform 2.

VSP_010488

Alternative sequence

505 – 1585

1081

Missing in isoform 2.

VSP_010489

Natural variant

378

1

Q → R: dbSNP rs35731992.

VAR_048924

Natural variant

496

1

P → A: dbSNP rs35176330.

VAR_034009

Natural variant

1185

1

D → E: dbSNP rs2230572.

VAR_048925

Experimental info

Mutagenesis

756

1

R → D: Reduces binding to EIF4A; when associated with D-759 and D-764. Ref.20

Mutagenesis

759

1

R → D: Reduces binding to EIF4A; when associated with D-756 and D-764. Ref.20

Mutagenesis

764

1

K → D: Reduces binding to EIF4A; when associated with D-756 and D-759. Ref.20

Mutagenesis

814

1

R → D: Reduces binding to EIF4A; when associated with D-820. Ref.20

Mutagenesis

820

1

K → D: Reduces binding to EIF4A; when associated with D-814. Ref.20

Mutagenesis

834 – 835

2

RK → DD: Reduces binding to IRES.

Sequence conflict

159

1

M → I in AAH30578. Ref.4

Sequence conflict

333

1

D → G in AAH30578. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1585

Helix Strand Turn

Details...

Helix

746 – 762

17

Helix

770 – 777

8

Helix

785 – 801

17

Helix

803 – 805

3

Helix

806 – 816

11

Helix

833 – 848

16

Helix

885 – 900

16

Turn

901 – 903

3

Helix

907 – 919

13

Helix

923 – 940

18

Turn

943 – 945

3

Helix

946 – 961

16

Helix

967 – 981

15

Turn

982 – 984

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: EA483139373DCA5C	FASTA	1,585	176,652
	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
	Isoform 2. Checksum: 0B4E961F10F62EA0	FASTA	515	55,227
	10 20 30 40 50 60 MNSQPQTRSP FAAGPRPPHH QFFQRPQIQP PRATIPNSSP SIRPGAQTPT AVYQANQHIM 70 80 90 100 110 120 MVNHLPMPYP VPQGPQYCIP QYRHSGPPYV GPPQQYPVQP PGPGPFYPGP GPGDFPNAYG 130 140 150 160 170 180 TPFYPSQPVY QSAPIIVPTQ QQPPPAKREK KTIRIRDPNQ GGKDITEEIM SGGGSRNPTP 190 200 210 220 230 240 PIGRPTSTPT PPQQLPSQVP EHSPVVYGTV ESAHLAASTP VTAASDQKQE EKPKPDPVLK 250 260 270 280 290 300 SPSPVLRLVL SGEKKEQEGQ TSETTAIVSI AELPLPPSPT TVSSVARSTI AAPTSSALSS 310 320 330 340 350 360 QPIFTTAIDD RCELSSPRED TIPIPSLTSC TETSDPLPTN ENDDDICKKP CSVAPNDIPL 370 380 390 400 410 420 VSSTNLINEI NGVSEKLSAT ESIVEIVKQE VLPLTLELEI LENPPEEMKL ECIPAPITPS 430 440 450 460 470 480 TVPSFPPTPP TPPASPPHTP VIVPAAATTV SSPSAAITVQ RVLEEDESIR TCLSEDAKEI 490 500 510 QNKIEVEADG QTEEILDSQN LNSRRSPVPE TSNEC

References

	« Hide 'large scale' referencesShow '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: 9418880] [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. , 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: 16710414] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: 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: 9857202] [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: 14507913] [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: 12663812] [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: 15016848] [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: 10872469] [Abstract] Cited for: REVIEW.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND SER-495, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"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: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, MASS SPECTROMETRY.
[14]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, MASS SPECTROMETRY.
[15]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-495, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"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-495, MASS SPECTROMETRY.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-944, MASS SPECTROMETRY.
[19]	"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: 12975586] [Abstract] Cited for: STRUCTURE BY NMR OF 621-637 IN COMPLEX WITH EIF4E.
[20]	"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: 11172724] [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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF012072 mRNA. Translation: AAC02903.2.
AL358392, AL606477, AL627311 Genomic DNA. Translation: CAI12155.1.
AL606477, AL358392, AL627311 Genomic DNA. Translation: CAI12534.1.
AL627311, AL358392, AL606477 Genomic DNA. Translation: CAI14553.1.
CH471134 Genomic DNA. Translation: EAW94956.1.
BC030578 mRNA. Translation: AAH30578.1.
Z34918 mRNA. Translation: CAA84397.1.

IPI

IPI00411710.
IPI00646377.

PIR

S49172.

RefSeq

NP_003751.2.

UniGene

Hs.467084

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HU3	X-ray	2.37	A	745-1003	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O43432. 4 interactions.

STRING

O43432.

PTM databases

PhosphoSite

O43432.

Proteomic databases

PRIDE

O43432.

Genome annotation databases

Ensembl

ENST00000264211; ENSP00000264211; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000356916; ENSP00000349386; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000374927; ENSP00000364062; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000374933; ENSP00000364069; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000374935; ENSP00000364071; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000374937; ENSP00000364073; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000400409; ENSP00000383260; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000400415; ENSP00000383266; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000400422; ENSP00000383274; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000411888; ENSP00000396083; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000435383; ENSP00000415717; ENSG00000075151; Homo sapiens. [Genome view]
ENST00000438975; ENSP00000395381; ENSG00000075151; Homo sapiens. [Genome view]

GeneID

8672.

KEGG

hsa:8672.

UCSC

uc001bec.1. human.
uc001bef.1. human.
uc001beh.2. human.

Organism-specific databases

CTD

8672.

GeneCards

GC01M021005.

H-InvDB

HIX0023524.

HGNC

HGNC:3298. EIF4G3.

HPA

HPA025031.
HPA025039.
HPA025041.

MIM

603929. gene.

PharmGKB

PA27724.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O43432.

OMA

ISMRELI.

Gene expression databases

ArrayExpress

O43432.

Bgee

O43432.

CleanEx

HS_EIF4G3.

Genevestigator

O43432.

GermOnline

ENSG00000075151. Homo sapiens.

Family and domain databases

InterPro

IPR003307. eIF5C.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]

Gene3D

G3DSA:1.25.40.230. eIF5C. 1 hit.
G3DSA:1.25.40.180. MIF4-like_typ_1/2/3. 1 hit.

Pfam

PF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]

SMART

SM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]

PROSITE

PS50077. HEAT_REPEAT. False negative.
PS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32529.

PMAP-CutDB

O43432.

SOURCE

Search...

Entry information

Entry name

IF4G3_HUMAN

Accession

Primary (citable) accession number: O43432
Secondary accession number(s): Q15597, Q5SWC3, Q8NEN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.