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Q04637

- IF4G1_HUMAN

UniProt

Q04637 - IF4G1_HUMAN

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Protein
Eukaryotic translation initiation factor 4 gamma 1
Gene
EIF4G1, EIF4F, EIF4G, EIF4GI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei674 – 6752Cleavage; by foot-and-mouth disease virus leader protease
Sitei681 – 6822Cleavage; by enterovirus/rhinovirus protease 2A

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. translation factor activity, nucleic acid binding Source: ProtInc
  4. translation initiation factor activity Source: UniProtKB

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. cell death Source: UniProtKB-KW
  3. cellular protein metabolic process Source: Reactome
  4. cytokine-mediated signaling pathway Source: Reactome
  5. gene expression Source: Reactome
  6. insulin receptor signaling pathway Source: Reactome
  7. mRNA metabolic process Source: Reactome
  8. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  9. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  10. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  11. regulation of translational initiation Source: UniProtKB
  12. translation Source: Reactome
  13. translational initiation Source: Reactome
  14. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_6772. S6K1 signalling.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
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 4 gamma 1
Short name:
eIF-4-gamma 1
Short name:
eIF-4G 1
Short name:
eIF-4G1
Alternative name(s):
p220
Gene namesi
Name:EIF4G1
Synonyms:EIF4F, EIF4G, EIF4GI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:3296. EIF4G1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. eukaryotic translation initiation factor 4F complex Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti502 – 5021A → V in PARK18. 1 Publication
Corresponds to variant rs111290936 [ dbSNP | Ensembl ].
VAR_066573
Natural varianti1205 – 12051R → H in PARK18. 1 Publication
Corresponds to variant rs112176450 [ dbSNP | Ensembl ].
VAR_066579

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi174 – 1785KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. 1 Publication
Mutagenesisi180 – 1801I → A: Loss of PABPC1 binding. 1 Publication
Mutagenesisi182 – 1821I → A: Loss of PABPC1 binding. 1 Publication
Mutagenesisi184 – 1874DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178.
Mutagenesisi192 – 1921I → A: Loss of PABPC1 binding. 1 Publication
Mutagenesisi196 – 1961I → A: Loss of PABPC1 binding. 1 Publication
Mutagenesisi612 – 6121Y → A or F: Abolishes binding to EIF4E. 1 Publication
Mutagenesisi617 – 6182LL → AA: Abolishes binding to EIF4E.
Mutagenesisi682 – 6821G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. 1 Publication
Mutagenesisi768 – 7681L → A: Abolishes binding to EIF4A; when associated with A-770 and A-775. 1 Publication
Mutagenesisi771 – 7711L → A: Abolishes binding to EIF4A; when associated with A-767 and A-775. 1 Publication
Mutagenesisi776 – 7761F → A: Abolishes binding to EIF4A; when associated with A-767 and A-770. 1 Publication
Mutagenesisi842 – 8432LL → AA: Abolishes binding to EIF4A; when associated with A-850 and K-851.
Mutagenesisi851 – 8522FE → AK: Abolishes binding to EIF4A; when associated with A-841 and A-842.
Mutagenesisi896 – 8961L → A: Abolishes binding to EIF4A; when associated with A-92 and A-95. 1 Publication
Mutagenesisi902 – 9021I → A: Abolishes binding to EIF4A; when associated with A-895 and A-95. 1 Publication
Mutagenesisi905 – 9051L → A: Abolishes binding to EIF4A; when associated with A-895 and A-92. 1 Publication
Mutagenesisi974 – 9741R → A: Abolishes binding to EIF4A; when associated with A-976. 1 Publication
Mutagenesisi977 – 9771F → A: Abolishes binding to EIF4A; when associated with A-973. 1 Publication
Mutagenesisi985 – 9851L → A: Slightly reduced binding to EIF4A; when associated with A-989. 1 Publication
Mutagenesisi990 – 9901W → A: Slightly reduced binding to EIF4A; when associated with A-984. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

MIMi614251. phenotype.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA27722.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15991599Eukaryotic translation initiation factor 4 gamma 1
PRO_0000007786Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei207 – 2071Phosphothreonine1 Publication
Modified residuei223 – 2231Phosphothreonine1 Publication
Modified residuei602 – 6021N6-acetyllysine By similarity
Modified residuei647 – 6471Phosphothreonine1 Publication
Modified residuei1028 – 10281Phosphoserine2 Publications
Modified residuei1092 – 10921Phosphoserine4 Publications
Modified residuei1095 – 10951N6-acetyllysine1 Publication
Modified residuei1145 – 11451Phosphoserine1 Publication
Modified residuei1147 – 11471Phosphoserine1 Publication
Modified residuei1185 – 11851Phosphoserine; by PKC/PRKCA3 Publications
Modified residuei1187 – 11871Phosphoserine2 Publications
Modified residuei1209 – 12091Phosphoserine3 Publications
Modified residuei1211 – 12111Phosphothreonine2 Publications
Modified residuei1231 – 12311Phosphoserine4 Publications
Modified residuei1596 – 15961Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1.1 Publication
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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ04637.
PaxDbiQ04637.
PRIDEiQ04637.

PTM databases

PhosphoSiteiQ04637.

Miscellaneous databases

PMAP-CutDBQ04637.

Expressioni

Gene expression databases

ArrayExpressiQ04637.
BgeeiQ04637.
CleanExiHS_EIF4G1.
GenevestigatoriQ04637.

Organism-specific databases

HPAiCAB014774.
HPA028487.
HPA043866.

Interactioni

Subunit structurei

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. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. 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/EIF4G3 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. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with CIRBP and MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis. Interacts with RBM4. Interacts with HNRNPD/AUF1; the interaction requires RNA.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX3XO005713EBI-73711,EBI-353779
EIF3JO758222EBI-73711,EBI-366647
EIF4A1P608427EBI-73711,EBI-73449
EIF4EP067302EBI-73711,EBI-73440
HNRNPDQ14103-43EBI-73711,EBI-432545
PABPC1P119402EBI-73711,EBI-81531

Protein-protein interaction databases

BioGridi108296. 60 interactions.
DIPiDIP-1161N.
IntActiQ04637. 35 interactions.
MINTiMINT-135718.
STRINGi9606.ENSP00000316879.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi181 – 1833
Helixi185 – 1873
Helixi193 – 1975
Helixi614 – 6196
Helixi1234 – 125623
Helixi1259 – 12679
Helixi1272 – 12743
Helixi1275 – 128612
Turni1287 – 12893
Helixi1291 – 130616
Helixi1312 – 132918
Turni1330 – 13323
Helixi1336 – 13449
Helixi1345 – 13484
Helixi1355 – 13628
Turni1363 – 13653
Helixi1366 – 13694
Helixi1372 – 138716
Helixi1389 – 139810
Helixi1403 – 14053
Helixi1413 – 14197
Helixi1423 – 14253
Helixi1439 – 145214
Helixi1457 – 146711
Helixi1470 – 14734
Helixi1476 – 148914
Beta strandi1494 – 14963
Helixi1501 – 151414
Helixi1518 – 153417
Helixi1541 – 155111
Helixi1557 – 15637

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LJ2X-ray2.38C/D172-199[»]
1UG3X-ray2.24A/B1233-1571[»]
2W97X-ray2.29E/F609-622[»]
4F02X-ray2.00C/F178-203[»]
DisProtiDP00406.
ProteinModelPortaliQ04637.
SMRiQ04637. Positions 173-199, 751-991, 1234-1592.

Miscellaneous databases

EvolutionaryTraceiQ04637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini565 – 792228MIF4G
Add
BLAST
Domaini1241 – 1363123MI
Add
BLAST
Domaini1433 – 1599167W2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 20029PABPC1-binding
Add
BLAST
Regioni607 – 61812EIF4E-binding
Add
BLAST
Regioni682 – 1085404eIF3/EIF4A-binding
Add
BLAST
Regioni1450 – 1599150EIF4A-binding
Add
BLAST
Regioni1585 – 159915Necessary but not sufficient for MKNK1-binding
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi454 – 46714Poly-Glu
Add
BLAST
Compositional biasi501 – 5044Poly-Ala

Sequence similaritiesi

Contains 1 MI domain.
Contains 1 MIF4G domain.
Contains 1 W2 domain.

Phylogenomic databases

eggNOGiNOG301289.
HOVERGENiHBG052083.
KOiK03260.
OMAiGSNWVPR.
OrthoDBiEOG7D59N2.
PhylomeDBiQ04637.
TreeFamiTF101527.

Family and domain databases

Gene3Di1.25.40.180. 3 hits.
InterProiIPR016024. 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]
PfamiPF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTiSM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform A (identifier: Q04637-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH     50
FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ 100
GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG 150
VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA 200
RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI IADRPGLPGP 250
EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES 300
TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP 350
LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP 400
EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS 450
PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE 500
AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA VPEVENQPPA 550
GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ 600
WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR 650
PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG 700
PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR TAADKDRGEE 750
DADGSKTQDL FRRVRSILNK LTPQMFQQLM KQVTQLAIDT EERLKGVIDL 800
IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR KLLLNRCQKE 850
FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK 900
FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK 950
AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK 1000
TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG 1050
GWNTVPISKG SRPIDTSRLT KITKPGSIDS NNQLFAPGGR LSWGKGSSGG 1100
SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV VQRSSLSRER 1150
GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ 1200
PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII 1250
EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL 1300
LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL AELVTPILQE 1350
GGVPMGELFR EITKPLRPLG KAASLLLEIL GLLCKSMGPK KVGTLWREAG 1400
LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS EELNRQLEKL 1450
LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD 1500
VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY 1550
DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN 1599
Length:1,599
Mass (Da):175,491
Last modified:April 20, 2010 - v4
Checksum:i324088B60863DA34
GO
Isoform B (identifier: Q04637-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: Missing.

Note: Produced by alternative initiation at Met-41 of isoform A.

Show »
Length:1,559
Mass (Da):171,514
Checksum:i22F62E219E629C0E
GO
Isoform C (identifier: Q04637-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.

Note: Produced by alternative initiation at Met-88 of isoform A.

Show »
Length:1,512
Mass (Da):166,619
Checksum:i09DD6DC263462CB6
GO
Isoform D (identifier: Q04637-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-164: Missing.

Note: Produced by alternative initiation at Met-165 of isoform A.

Show »
Length:1,435
Mass (Da):158,517
Checksum:i6F7E9DE4106E73B9
GO
Isoform E (identifier: Q04637-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.

Note: Produced by alternative initiation at Met-197 of isoform A.

Show »
Length:1,403
Mass (Da):154,805
Checksum:i3E93A66EE3DFDDA9
GO
Isoform 7 (identifier: Q04637-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.
     696-696: P → PQ

Note: Produced by alternative splicing.

Show »
Length:1,404
Mass (Da):154,933
Checksum:iE2CE3C54B5BB0A50
GO
Isoform 8 (identifier: Q04637-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     696-696: P → PQ

Note: Produced by alternative splicing.

Show »
Length:1,600
Mass (Da):175,619
Checksum:i2B32EF7A6D50B657
GO
Isoform 9 (identifier: Q04637-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-48: R → RQGGFRSL

Note: Produced by alternative splicing. Gene prediction based on EST data.

Show »
Length:1,606
Mass (Da):176,237
Checksum:iE4464821E0BA5FF6
GO

Sequence cautioni

The sequence BAD18554.1 differs from that shown. Reason: Aberrant splicing.
The sequence BAA02185.1 differs from that shown. Reason: Frameshift at several positions.
The sequence AAC78444.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAC82471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711P → S.1 Publication
Corresponds to variant rs113810947 [ dbSNP | Ensembl ].
VAR_066571
Natural varianti161 – 1611T → A.5 Publications
Corresponds to variant rs13319149 [ dbSNP | Ensembl ].
VAR_061147
Natural varianti311 – 3111Y → C.1 Publication
Corresponds to variant rs16858632 [ dbSNP | Ensembl ].
VAR_055704
Natural varianti432 – 4321M → V.4 Publications
Corresponds to variant rs2178403 [ dbSNP | Ensembl ].
VAR_063040
Natural varianti466 – 4683Missing.
VAR_066572
Natural varianti502 – 5021A → V in PARK18. 1 Publication
Corresponds to variant rs111290936 [ dbSNP | Ensembl ].
VAR_066573
Natural varianti686 – 6861G → C Found in patients with Parkinson disease; unknown pathological significance. 1 Publication
Corresponds to variant rs112019125 [ dbSNP | Ensembl ].
VAR_066574
Natural varianti696 – 6961P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036117
Natural varianti806 – 8061I → V.1 Publication
Corresponds to variant rs62287499 [ dbSNP | Ensembl ].
VAR_066575
Natural varianti829 – 8291T → S.1 Publication
Corresponds to variant rs111500185 [ dbSNP | Ensembl ].
VAR_066576
Natural varianti1164 – 11641S → R Found in a patient with Parkinson disease; unknown pathological significance. 1 Publication
Corresponds to variant rs113169049 [ dbSNP | Ensembl ].
VAR_066577
Natural varianti1197 – 11971R → W Found in a patient with Parkinson disease; unknown pathological significance. 1 Publication
Corresponds to variant rs113388242 [ dbSNP | Ensembl ].
VAR_066578
Natural varianti1205 – 12051R → H in PARK18. 1 Publication
Corresponds to variant rs112176450 [ dbSNP | Ensembl ].
VAR_066579
Natural varianti1229 – 12291P → A.1 Publication
Corresponds to variant rs35629949 [ dbSNP | Ensembl ].
VAR_061148
Natural varianti1233 – 12331L → P.1 Publication
Corresponds to variant rs2230570 [ dbSNP | Ensembl ].
VAR_055705
Natural varianti1257 – 12571N → S.1 Publication
Corresponds to variant rs73053766 [ dbSNP | Ensembl ].
VAR_066580

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 196196Missing in isoform E and isoform 7.
VSP_018723Add
BLAST
Alternative sequencei1 – 164164Missing in isoform D.
VSP_018722Add
BLAST
Alternative sequencei1 – 8787Missing in isoform C.
VSP_018721Add
BLAST
Alternative sequencei1 – 4040Missing in isoform B.
VSP_018720Add
BLAST
Alternative sequencei48 – 481R → RQGGFRSL in isoform 9.
VSP_047396
Alternative sequencei696 – 6961P → PQ in isoform 7 and isoform 8.
VSP_047397

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301P → R in AAC78443. 1 Publication
Sequence conflicti138 – 1381F → L in AAL92872. 1 Publication
Sequence conflicti138 – 1381F → L in AAM69365. 1 Publication
Sequence conflicti149 – 1491Q → R in AAL92872. 1 Publication
Sequence conflicti149 – 1491Q → R in AAM69365. 1 Publication
Sequence conflicti214 – 2141G → S in BAA02185. 1 Publication
Sequence conflicti462 – 4621E → D in BAA02185. 1 Publication
Sequence conflicti468 – 4681A → V in BAA02185. 1 Publication
Sequence conflicti474 – 4741A → G in BAA02185. 1 Publication
Sequence conflicti479 – 4791G → R in BAA02185. 1 Publication
Sequence conflicti604 – 6041L → P in BAA02185. 1 Publication
Sequence conflicti604 – 6041L → P in AAL92872. 1 Publication
Sequence conflicti604 – 6041L → P in AAM69365. 1 Publication
Sequence conflicti604 – 6041L → P in AAC82471. 1 Publication
Sequence conflicti625 – 6262AS → CQ in BAA02185. 1 Publication
Sequence conflicti693 – 6931P → A in BAA02185. 1 Publication
Sequence conflicti696 – 6961P → A in BAA02185. 1 Publication
Sequence conflicti764 – 7641V → W in BAA02185. 1 Publication
Sequence conflicti878 – 8781G → E in BAA02185. 1 Publication
Sequence conflicti894 – 8941R → C in BAA02185. 1 Publication
Sequence conflicti1104 – 11041K → Q in BAA02185. 1 Publication
Sequence conflicti1121 – 11211N → I in BAA02185. 1 Publication
Sequence conflicti1185 – 11851S → T in BAA02185. 1 Publication
Sequence conflicti1384 – 13841C → Y in CAI46013. 1 Publication
Sequence conflicti1472 – 14721Missing in BAA02185. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12686 mRNA. Translation: BAA02185.1. Frameshift.
AY082886 mRNA. Translation: AAL92872.1.
AF281070 mRNA. Translation: AAM69365.1.
AK131407 mRNA. Translation: BAD18554.1. Sequence problems.
BX647812 mRNA. Translation: CAI46013.1.
AC078797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78257.1.
CH471052 Genomic DNA. Translation: EAW78259.1.
CH471052 Genomic DNA. Translation: EAW78262.1.
CH471052 Genomic DNA. Translation: EAW78263.1.
CH471052 Genomic DNA. Translation: EAW78264.1.
CH471052 Genomic DNA. Translation: EAW78265.1.
CH471052 Genomic DNA. Translation: EAW78266.1.
CH471052 Genomic DNA. Translation: EAW78267.1.
AF002816 mRNA. Translation: AAC78443.1.
AF004836 Genomic DNA. Translation: AAC78444.1. Different initiation.
AF104913 mRNA. Translation: AAC82471.1. Different initiation.
AJ001046 mRNA. Translation: CAA04500.1.
CCDSiCCDS3259.1. [Q04637-1]
CCDS3260.1. [Q04637-4]
CCDS3261.1. [Q04637-5]
CCDS46970.2. [Q04637-7]
CCDS54687.1. [Q04637-9]
CCDS54688.1. [Q04637-8]
PIRiA44453.
RefSeqiNP_004944.3. NM_004953.4. [Q04637-7]
NP_886553.3. NM_182917.4.
NP_937884.1. NM_198241.2.
NP_937885.1. NM_198242.2. [Q04637-5]
UniGeneiHs.433750.

Genome annotation databases

EnsembliENST00000319274; ENSP00000323737; ENSG00000114867. [Q04637-1]
ENST00000342981; ENSP00000343450; ENSG00000114867. [Q04637-8]
ENST00000346169; ENSP00000316879; ENSG00000114867. [Q04637-1]
ENST00000350481; ENSP00000317600; ENSG00000114867. [Q04637-5]
ENST00000352767; ENSP00000338020; ENSG00000114867. [Q04637-9]
ENST00000382330; ENSP00000371767; ENSG00000114867. [Q04637-9]
ENST00000392537; ENSP00000376320; ENSG00000114867. [Q04637-4]
ENST00000414031; ENSP00000391935; ENSG00000114867. [Q04637-3]
ENST00000424196; ENSP00000416255; ENSG00000114867. [Q04637-9]
ENST00000434061; ENSP00000411826; ENSG00000114867. [Q04637-7]
ENST00000435046; ENSP00000404754; ENSG00000114867. [Q04637-6]
GeneIDi1981.
KEGGihsa:1981.
UCSCiuc003fnp.3. human. [Q04637-1]
uc003fnv.4. human.
uc003fnx.3. human.

Polymorphism databases

DMDMi294862538.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12686 mRNA. Translation: BAA02185.1 . Frameshift.
AY082886 mRNA. Translation: AAL92872.1 .
AF281070 mRNA. Translation: AAM69365.1 .
AK131407 mRNA. Translation: BAD18554.1 . Sequence problems.
BX647812 mRNA. Translation: CAI46013.1 .
AC078797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78257.1 .
CH471052 Genomic DNA. Translation: EAW78259.1 .
CH471052 Genomic DNA. Translation: EAW78262.1 .
CH471052 Genomic DNA. Translation: EAW78263.1 .
CH471052 Genomic DNA. Translation: EAW78264.1 .
CH471052 Genomic DNA. Translation: EAW78265.1 .
CH471052 Genomic DNA. Translation: EAW78266.1 .
CH471052 Genomic DNA. Translation: EAW78267.1 .
AF002816 mRNA. Translation: AAC78443.1 .
AF004836 Genomic DNA. Translation: AAC78444.1 . Different initiation.
AF104913 mRNA. Translation: AAC82471.1 . Different initiation.
AJ001046 mRNA. Translation: CAA04500.1 .
CCDSi CCDS3259.1. [Q04637-1 ]
CCDS3260.1. [Q04637-4 ]
CCDS3261.1. [Q04637-5 ]
CCDS46970.2. [Q04637-7 ]
CCDS54687.1. [Q04637-9 ]
CCDS54688.1. [Q04637-8 ]
PIRi A44453.
RefSeqi NP_004944.3. NM_004953.4. [Q04637-7 ]
NP_886553.3. NM_182917.4.
NP_937884.1. NM_198241.2.
NP_937885.1. NM_198242.2. [Q04637-5 ]
UniGenei Hs.433750.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LJ2 X-ray 2.38 C/D 172-199 [» ]
1UG3 X-ray 2.24 A/B 1233-1571 [» ]
2W97 X-ray 2.29 E/F 609-622 [» ]
4F02 X-ray 2.00 C/F 178-203 [» ]
DisProti DP00406.
ProteinModelPortali Q04637.
SMRi Q04637. Positions 173-199, 751-991, 1234-1592.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108296. 60 interactions.
DIPi DIP-1161N.
IntActi Q04637. 35 interactions.
MINTi MINT-135718.
STRINGi 9606.ENSP00000316879.

Chemistry

BindingDBi Q04637.

PTM databases

PhosphoSitei Q04637.

Polymorphism databases

DMDMi 294862538.

Proteomic databases

MaxQBi Q04637.
PaxDbi Q04637.
PRIDEi Q04637.

Protocols and materials databases

DNASUi 1981.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319274 ; ENSP00000323737 ; ENSG00000114867 . [Q04637-1 ]
ENST00000342981 ; ENSP00000343450 ; ENSG00000114867 . [Q04637-8 ]
ENST00000346169 ; ENSP00000316879 ; ENSG00000114867 . [Q04637-1 ]
ENST00000350481 ; ENSP00000317600 ; ENSG00000114867 . [Q04637-5 ]
ENST00000352767 ; ENSP00000338020 ; ENSG00000114867 . [Q04637-9 ]
ENST00000382330 ; ENSP00000371767 ; ENSG00000114867 . [Q04637-9 ]
ENST00000392537 ; ENSP00000376320 ; ENSG00000114867 . [Q04637-4 ]
ENST00000414031 ; ENSP00000391935 ; ENSG00000114867 . [Q04637-3 ]
ENST00000424196 ; ENSP00000416255 ; ENSG00000114867 . [Q04637-9 ]
ENST00000434061 ; ENSP00000411826 ; ENSG00000114867 . [Q04637-7 ]
ENST00000435046 ; ENSP00000404754 ; ENSG00000114867 . [Q04637-6 ]
GeneIDi 1981.
KEGGi hsa:1981.
UCSCi uc003fnp.3. human. [Q04637-1 ]
uc003fnv.4. human.
uc003fnx.3. human.

Organism-specific databases

CTDi 1981.
GeneCardsi GC03P184032.
HGNCi HGNC:3296. EIF4G1.
HPAi CAB014774.
HPA028487.
HPA043866.
MIMi 600495. gene.
614251. phenotype.
neXtProti NX_Q04637.
Orphaneti 2828. Young adult-onset Parkinsonism.
PharmGKBi PA27722.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301289.
HOVERGENi HBG052083.
KOi K03260.
OMAi GSNWVPR.
OrthoDBi EOG7D59N2.
PhylomeDBi Q04637.
TreeFami TF101527.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
REACT_1979. Translation initiation complex formation.
REACT_20514. Deadenylation of mRNA.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_6772. S6K1 signalling.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.

Miscellaneous databases

ChiTaRSi EIF4G1. human.
EvolutionaryTracei Q04637.
GeneWikii Eukaryotic_translation_initiation_factor_4_gamma.
GenomeRNAii 1981.
NextBioi 35489794.
PMAP-CutDB Q04637.
PROi Q04637.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q04637.
Bgeei Q04637.
CleanExi HS_EIF4G1.
Genevestigatori Q04637.

Family and domain databases

Gene3Di 1.25.40.180. 3 hits.
InterProi IPR016024. 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 ]
Pfami PF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view ]
SMARTi SM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
PROSITEi PS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma."
    Yan R., Rychlik W., Etchison D., Rhoads R.E.
    J. Biol. Chem. 267:23226-23231(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), VARIANT VAL-432.
    Tissue: Brain.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PABPC1.
  3. "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 C).
  4. "Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons."
    Byrd M.P., Zamora M., Lloyd R.E.
    Mol. Cell. Biol. 22:4499-4511(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), VARIANTS ALA-161 AND VAL-432, ALTERNATIVE INITIATION.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ALA-161.
    Tissue: Endometrial tumor.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts the poly(A) binding protein from eIF4F."
    Piron M., Vende P., Cohen J., Poncet D.
    EMBO J. 17:5811-5821(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-234, VARIANT ALA-161, INTERACTION WITH ROTAVIRAL NSP3.
  10. "Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A."
    Imataka H., Sonenberg N.
    Mol. Cell. Biol. 17:6940-6947(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH EIF4A, VARIANTS ALA-161 AND VAL-432, MUTAGENESIS OF LEU-768; LEU-771; PHE-776; 842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902; LEU-905; ARG-974; PHE-977; LEU-985 AND TRP-990.
  11. "The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins."
    Mader S., Lee H., Pause A., Sonenberg N.
    Mol. Cell. Biol. 15:4990-4997(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
  12. De Gregorio E.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 682-912 (ISOFORM 8).
  13. "Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus."
    Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H., Kuechler E., Skern T., Rhoads R.E.
    J. Biol. Chem. 268:19200-19203(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
  14. "Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function."
    Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., Lawrence J.C. Jr., Sonenberg N.
    Nature 371:762-767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF4E.
    Tissue: Placenta.
  15. "Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
    Haghighat A., Mader S., Pause A., Sonenberg N.
    EMBO J. 14:5701-5709(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF4E AND EIF4EBP1.
  16. "A single amino acid change in protein synthesis initiation factor 4G renders cap-dependent translation resistant to picornaviral 2A proteases."
    Lamphear B.J., Rhoads R.E.
    Biochemistry 35:15726-15733(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-682.
  17. "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."
    Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.
    FEBS Lett. 435:79-83(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY POLIOVIRUS.
  18. "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.
  19. "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.
  20. "Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation."
    Wakiyama M., Imataka H., Sonenberg N.
    Curr. Biol. 10:1147-1150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PABPC1, MUTAGENESIS OF 174-LYS--LYS-178 AND 184-ASP--GLN-197.
  21. "Multiple portions of poly(A)-binding protein stimulate translation in vivo."
    Gray N.K., Coller J.M., Dickson K.S., Wickens M.
    EMBO J. 19:4723-4733(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PABPC1.
  22. "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
    Glaser W., Skern T.
    FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY FMDV AND HRV-2.
  23. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
    Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
    Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MKNK2.
  24. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "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-1231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Post-transcriptional regulation of thioredoxin by the stress inducible heterogeneous ribonucleoprotein A18."
    Yang R., Weber D.J., Carrier F.
    Nucleic Acids Res. 34:1224-1236(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIRBP.
  27. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
    Lin J.C., Hsu M., Tarn W.Y.
    Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM4.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  30. "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
    Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
    J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROTAVIRUS A NSP3.
  31. "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.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-223; THR-647; SER-1092 AND SER-1209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "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].
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "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-1028; SER-1092; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1."
    Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.
    Mol. Cell. Biol. 31:2947-2959(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1185.
  40. "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-1028; SER-1092; SER-1145; SER-1147; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation."
    Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., Hong K.Y., Jang S.K., Kim K.T.
    Nucleic Acids Res. 42:3590-3606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRPD, RNA-BINDING.
  43. "Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."
    Groft C.M., Burley S.K.
    Mol. Cell 9:1273-1283(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH ROTAVIRAL NSP3, INTERACTION WITH PABPC1, MUTAGENESIS OF ILE-180; ILE-182; ILE-192 AND ILE-196.
  44. "Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1."
    Bellsolell L., Cho-Park P.F., Poulin F., Sonenberg N., Burley S.K.
    Structure 14:913-923(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571.
  45. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-696.
  46. "Translation initiator EIF4G1 mutations in familial Parkinson disease."
    Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J., Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L., Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A., Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K.
    , Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.
    Am. J. Hum. Genet. 89:398-406(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK18 VAL-502 AND HIS-1205, VARIANTS SER-71; ALA-161; CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829; ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.

Entry informationi

Entry nameiIF4G1_HUMAN
AccessioniPrimary (citable) accession number: Q04637
Secondary accession number(s): D3DNT2
, D3DNT4, D3DNT5, E9PFM1, G5E9S1, O43177, O95066, Q5HYG0, Q6ZN21, Q8N102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 20, 2010
Last modified: September 3, 2014
This is version 164 of the entry and version 4 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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