Descriptions

EIF4G is a 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. The eIF4E-binding site in eukaryotic initiation factor 4G (eIF4G) functions as an autoinhibitory domain to modulate its ability to stimulate eIF4A helicase activity. Binding of eIF4E counteracts this autoinhibition, enabling eIF4G to stimulate eIF4A helicase activity.

Autoinhibitory domains (AIDs)

Target domain

686-1089 (eIF4A-binding domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6NZJ6

Entry ID Method Resolution Chain Position Source
AF-Q6NZJ6-F1 Predicted AlphaFoldDB

78 variants for Q6NZJ6

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3406788083 26 G>V No EVA
rs3406150448 28 T>S No EVA
rs237672896 35 T>S No EVA
rs3389387217 85 P>A No EVA
rs3389322949 87 V>D No EVA
rs3389413304 87 V>L No EVA
rs3389414686 88 Y>F No EVA
rs3389387166 104 S>P No EVA
rs3389401280 149 A>V No EVA
rs3389414727 164 S>G No EVA
rs3389403663 213 P>S No EVA
rs3508089888 247 A>G No EVA
rs3508087019 247 A>T No EVA
rs3508090742 248 I>T No EVA
rs3389407474 250 G>V No EVA
rs1134739190 251 R>Q No EVA
rs3508086942 252 P>S No EVA
rs1133198718 310 S>L No EVA
rs3389401023 313 I>N No EVA
rs3389417900 324 S>F No EVA
rs3406403081 331 E>* No EVA
rs3389355967 336 V>I No EVA
rs242328290 359 A>S No EVA
rs3389409820 362 P>S No EVA
rs247354483 364 K>R No EVA
rs3389423100 370 P>S No EVA
rs3389368006 432 P>A No EVA
rs215266436 447 I>V No EVA
rs251283225 451 A>S No EVA
rs251283225 451 A>T No EVA
rs3389377142 451 A>V No EVA
rs221592403 459 T>N No EVA
rs3389423143 479 A>T No EVA
rs3413048523 520 R>Q No EVA
rs3389404725 536 D>N No EVA
rs3389367954 544 A>T No EVA
rs3389407510 544 A>V No EVA
rs3405074848 547 E>Q No EVA
rs233857892 564 G>A No EVA
rs31416468 566 M>T No EVA
rs3389407528 631 M>V No EVA
rs3389324485 632 Q>K No EVA
rs3389355958 658 P>H No EVA
rs3389377132 668 P>S No EVA
rs45770361 673 S>P No EVA
rs3389423089 712 P>L No EVA
rs3389409874 754 E>* No EVA
rs3389367992 779 M>I No EVA
rs3389409815 816 S>F No EVA
rs3389398198 839 V>E No EVA
rs3389414724 861 D>N No EVA
rs3389409871 864 V>A No EVA
rs3389409806 868 K>R No EVA
rs3389409888 870 K>I No EVA
rs3389398247 875 A>T No EVA
rs47774653 892 R>W No EVA
rs3389367976 958 R>P No EVA
rs3406150445 966 M>L No EVA
rs13473261 994 W>* No EVA
rs3389414712 1015 M>K No EVA
rs3389404756 1118 R>C No EVA
rs3389387225 1121 T>I No EVA
rs242629180 1191 E>D No EVA
rs3389423075 1255 H>P No EVA
rs3389414732 1255 H>Y No EVA
rs3389408236 1268 E>V No EVA
rs3389417831 1269 L>V No EVA
rs3389409822 1285 S>A No EVA
rs3389423112 1289 R>L No EVA
rs3389356004 1306 C>Y No EVA
rs3389367927 1342 E>D No EVA
rs3406810084 1350 E>V No EVA
rs251863834 1357 E>D No EVA
rs214445582 1394 M>T No EVA
rs3552086809 1397 R>Q No EVA
rs3406403084 1438 L>I No EVA
rs226732776 1461 F>S No EVA
rs3389356008 1570 A>T No EVA

No associated diseases with Q6NZJ6

3 regional properties for Q6NZJ6

Type Name Position InterPro Accession
domain W2 domain 1429 - 1599 IPR003307
domain MIF4G-like, type 3 765 - 993 IPR003890
domain Initiation factor eIF-4 gamma, MA3 1241 - 1363 IPR003891

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Cytoplasm, Stress granule
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
eukaryotic translation initiation factor 4F complex The eukaryotic translation initiation factor 4F complex is composed of eIF4E, eIF4A and eIF4G; it is involved in the recognition of the mRNA cap, ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of the mRNA to the ribosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
postsynapse The part of a synapse that is part of the post-synaptic cell.
ribosome An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
eukaryotic initiation factor 4E binding Binding to eukaryotic initiation factor 4E, a polypeptide factor involved in the initiation of ribosome-mediated translation.
identical protein binding Binding to an identical protein or proteins.
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

19 GO annotations of biological process

Name Definition
behavioral fear response An acute behavioral change resulting from a perceived external threat.
cellular response to nutrient levels Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients.
energy homeostasis Any process involved in the balance between food intake (energy input) and energy expenditure.
lung development The process whose specific outcome is the progression of the lung over time, from its formation to the mature structure. In all air-breathing vertebrates the lungs are developed from the ventral wall of the oesophagus as a pouch which divides into two sacs. In amphibians and many reptiles the lungs retain very nearly this primitive sac-like character, but in the higher forms the connection with the esophagus becomes elongated into the windpipe and the inner walls of the sacs become more and more divided, until, in the mammals, the air spaces become minutely divided into tubes ending in small air cells, in the walls of which the blood circulates in a fine network of capillaries. In mammals the lungs are more or less divided into lobes, and each lung occupies a separate cavity in the thorax.
miRNA-mediated gene silencing by inhibition of translation An RNA interference pathway in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs.
negative regulation of autophagy Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
negative regulation of peptidyl-threonine phosphorylation Any process that decreases the frequency, rate or extent of peptidyl-threonine phosphorylation. Peptidyl-threonine phosphorylation is the phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
neuron differentiation The process in which a relatively unspecialized cell acquires specialized features of a neuron.
positive regulation of cell growth Any process that activates or increases the frequency, rate, extent or direction of cell growth.
positive regulation of eukaryotic translation initiation factor 4F complex assembly Any process that activates or increases the frequency, rate or extent of eukaryotic translation initiation factor 4F complex assembly.
positive regulation of G1/S transition of mitotic cell cycle Any signalling pathway that increases or activates a cell cycle cyclin-dependent protein kinase to modulate the switch from G1 phase to S phase of the mitotic cell cycle.
positive regulation of neuron differentiation Any process that activates or increases the frequency, rate or extent of neuron differentiation.
positive regulation of peptidyl-serine phosphorylation Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-serine.
positive regulation of protein localization to cell periphery Any process that activates or increases the frequency, rate or extent of protein localization to cell periphery.
positive regulation of translation in response to endoplasmic reticulum stress Any process that activates, or increases the frequency, rate or extent of translation as a result of endoplasmic reticulum stress.
regulation of presynapse assembly Any process that modulates the frequency, rate or extent of presynapse assembly.
regulation of translational initiation Any process that modulates the frequency, rate or extent of translational initiation.
response to ethanol Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus.
translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q41583 Eukaryotic translation initiation factor isoform 4G-2 Triticum aestivum (Wheat) PR
Q95L46 EIF4G2 Eukaryotic translation initiation factor 4 gamma 2 Bos taurus (Bovine) PR
Q9H074 PAIP1 Polyadenylate-binding protein-interacting protein 1 Homo sapiens (Human) PR
P78344 EIF4G2 Eukaryotic translation initiation factor 4 gamma 2 Homo sapiens (Human) PR
O43432 EIF4G3 Eukaryotic translation initiation factor 4 gamma 3 Homo sapiens (Human) EV
Q04637 EIF4G1 Eukaryotic translation initiation factor 4 gamma 1 Homo sapiens (Human) EV
Q8VE62 Paip1 Polyadenylate-binding protein-interacting protein 1 Mus musculus (Mouse) PR
Q62448 Eif4g2 Eukaryotic translation initiation factor 4 gamma 2 Mus musculus (Mouse) PR
Q80XI3 Eif4g3 Eukaryotic translation initiation factor 4 gamma 3 Mus musculus (Mouse) SS
10 20 30 40 50 60
MNKAPQPTGP PPARSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQG GFRSLQHFYP
70 80 90 100 110 120
SRAQPPSSAA SRVQSAAPAR PGPAPHVYPA GSQVMMIPSQ ISYSASQGAY YIPGQGRSTY
130 140 150 160 170 180
VVPTQQYPVQ PGAPGFYPGA SPTEFGTYAG AYYPAQGVQQ FPASVAPAPV LMNQPPQIAP
190 200 210 220 230 240
KRERKTIRIR DPNQGGKDIT EEIMSGARTA STPTPPQTGG SLEPQPNGES PQVAVIIRPD
250 260 270 280 290 300
DRSQGAAIGG RPGLPGPEHS PGTESQPSSP SPTPSPPPIL EPGSESNLGV LSIPGDTMTT
310 320 330 340 350 360
GMIPMSVEES TPISCETGEP YCLSPEPTLA EPILEVEVTL SKPIPESEFS SSPLQVSTAL
370 380 390 400 410 420
VPHKVETHEP NGVIPSEDLE PEVESSTEPA PPPLSPCASE SLVPIAPTAQ PEELLNGAPS
430 440 450 460 470 480
PPAVDLSPVS EPEEQAKKVS SAALASILSP APPVAPSDTS PAQEEEMEED DDDEEGGEAE
490 500 510 520 530 540
SEKGGEDVPL DSTPVPAQLS QNLEVAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE
550 560 570 580 590 600
VDPAVPEVEN QPPTGSNPSP ESEGSMVPTQ PEETEETWDS KEDKIHNAEN IQPGEQKYEY
610 620 630 640 650 660
KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI TDVVLDKANK TPLRQLDPSR
670 680 690 700 710 720
LPGINCGPDF TPSFANLGRP ALSNRGPPRG GPGGELPRGP AGLGPRRSQQ GPRKETRKII
730 740 750 760 770 780
SSVIMTEDIK LNKAEKAWKP SSKRTAADKD RGEEDADGSK TQDLFRRVRS ILNKLTPQMF
790 800 810 820 830 840
QQLMKQVTQL AIDTEERLKG VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT
850 860 870 880 890 900
VNFRKLLLNR CQKEFEKDKD DDEVFEKKQK EMDEAATAEE RGRLKEELEE ARDIARRRSL
910 920 930 940 950 960
GNIKFIGELF KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFAKAKPRMD
970 980 990 1000 1010 1020
QYFNQMEKII KEKKTSSRIR FMLQDVLDLR QSNWVPRRGD QGPKTIDQIH KEAEMEEHRE
1030 1040 1050 1060 1070 1080
HIKVQQLMAK GSDKRRGGPP GPPINRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG
1090 1100 1110 1120 1130 1140
SIDSNNQLFA PGGRLSWGKG SSGGSGAKPS DTASEATRPA TLNRFSALQQ TLPAENTDNR
1150 1160 1170 1180 1190 1200
RVVQRSSLSR ERGEKAGDRG DRLERSERGG DRGDRLDRAR TPATKRSFSK EVEERSRERP
1210 1220 1230 1240 1250 1260
SQPEGLRKAA SLTEDRGRDP VKREATLPPV SPPKAALSVD EVEKKSKAII EEYLHLNDMK
1270 1280 1290 1300 1310 1320
EAVQCVQELA SPSLLFIFVR LGIESTLERS TIAREHMGRL LHQLLCAGHL STAQYYQGLY
1330 1340 1350 1360 1370 1380
ETLELAEDME IDIPHVWLYL AELITPILQE DGVPMGELFR EITKPLRPMG KATSLLLEIL
1390 1400 1410 1420 1430 1440
GLLCKSMGPK KVGMLWREAG LSWREFLAEG QDVGSFVAEK KVEYTLGEES EAPGQRTLAF
1450 1460 1470 1480 1490 1500
EELRRQLEKL LKDGGSNQRV FDWIDANLNE QQIASNTLVR ALMTTVCYSA IIFETPLRVD
1510 1520 1530 1540 1550 1560
VQVLKVRARL LQKYLCDEQK ELQALYALQA LVVTLEQPAN LLRMFFDALY DEDVVKEDAF
1570 1580 1590
YSWESSKDPA EQQGKGVALK SVTAFFNWLR EAEDEESDHN