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Protein

Eukaryotic translation initiation factor 4 gamma 1

Gene

EIF4G1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • eukaryotic initiation factor 4E binding Source: AgBase
  • poly(A) RNA binding Source: UniProtKB
  • translation factor activity, RNA binding Source: ParkinsonsUK-UCL
  • translation initiation factor activity Source: UniProtKB

GO - Biological processi

  • behavioral fear response Source: Ensembl
  • cellular macromolecule biosynthetic process Source: ParkinsonsUK-UCL
  • mitochondrion organization Source: ParkinsonsUK-UCL
  • negative regulation of autophagy Source: ParkinsonsUK-UCL
  • negative regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  • positive regulation of cell growth Source: ParkinsonsUK-UCL
  • positive regulation of cell proliferation Source: ParkinsonsUK-UCL
  • positive regulation of cellular protein metabolic process Source: ParkinsonsUK-UCL
  • positive regulation of energy homeostasis Source: ParkinsonsUK-UCL
  • positive regulation of eukaryotic translation initiation factor 4F complex assembly Source: ParkinsonsUK-UCL
  • positive regulation of G1/S transition of mitotic cell cycle Source: ParkinsonsUK-UCL
  • positive regulation of neuron differentiation Source: Ensembl
  • positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • regulation of mRNA stability Source: Reactome
  • regulation of translational initiation Source: UniProtKB
  • translational initiation Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor, Translational shunt

Keywords - Biological processi

Host-virus interaction, Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114867-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-429947. Deadenylation of mRNA.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiQ04637.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:3296. EIF4G1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: AgBase
  • cytosol Source: Reactome
  • eukaryotic translation initiation factor 4F complex Source: ProtInc
  • membrane Source: UniProtKB
  • nucleus Source: ParkinsonsUK-UCL
  • polysome Source: ParkinsonsUK-UCL
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 18 (PARK18)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:614251
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066573502A → V in PARK18. 1 PublicationCorresponds to variant rs111290936dbSNPEnsembl.1
Natural variantiVAR_0665791205R → H in PARK18. 1 PublicationCorresponds to variant rs112176450dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi174 – 178KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. 1 Publication5
Mutagenesisi180I → A: Loss of PABPC1 binding. 1 Publication1
Mutagenesisi182I → A: Loss of PABPC1 binding. 1 Publication1
Mutagenesisi184 – 187DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178. 4
Mutagenesisi192I → A: Loss of PABPC1 binding. 1 Publication1
Mutagenesisi196I → A: Loss of PABPC1 binding. 1 Publication1
Mutagenesisi612Y → A or F: Abolishes binding to EIF4E. 1 Publication1
Mutagenesisi617 – 618LL → AA: Abolishes binding to EIF4E. 1 Publication2
Mutagenesisi682G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. 1 Publication1
Mutagenesisi768L → A: Abolishes binding to EIF4A; when associated with A-770 and A-775. 1 Publication1
Mutagenesisi771L → A: Abolishes binding to EIF4A; when associated with A-767 and A-775. 1 Publication1
Mutagenesisi776F → A: Abolishes binding to EIF4A; when associated with A-767 and A-770. 1 Publication1
Mutagenesisi842 – 843LL → AA: Abolishes binding to EIF4A; when associated with A-850 and K-851. 1 Publication2
Mutagenesisi851 – 852FE → AK: Abolishes binding to EIF4A; when associated with A-841 and A-842. 1 Publication2
Mutagenesisi896L → A: Abolishes binding to EIF4A; when associated with A-92 and A-95. 1 Publication1
Mutagenesisi902I → A: Abolishes binding to EIF4A; when associated with A-895 and A-95. 1 Publication1
Mutagenesisi905L → A: Abolishes binding to EIF4A; when associated with A-895 and A-92. 1 Publication1
Mutagenesisi974R → A: Abolishes binding to EIF4A; when associated with A-976. 1 Publication1
Mutagenesisi977F → A: Abolishes binding to EIF4A; when associated with A-973. 1 Publication1
Mutagenesisi985L → A: Slightly reduced binding to EIF4A; when associated with A-989. 1 Publication1
Mutagenesisi990W → A: Slightly reduced binding to EIF4A; when associated with A-984. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

Organism-specific databases

DisGeNETi1981.
MalaCardsiEIF4G1.
MIMi614251. phenotype.
OpenTargetsiENSG00000114867.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA27722.

Polymorphism and mutation databases

BioMutaiEIF4G1.
DMDMi294862538.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000077861 – 1599Eukaryotic translation initiation factor 4 gamma 1Add BLAST1599
Isoform C (identifier: Q04637-4)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphoserineBy similarity1
Modified residuei73Omega-N-methylarginineCombined sources1
Modified residuei110Omega-N-methylarginineCombined sources1
Modified residuei207PhosphothreonineCombined sources1
Modified residuei223PhosphothreonineCombined sources1
Modified residuei314PhosphoserineCombined sources1
Modified residuei602N6-acetyllysineBy similarity1
Modified residuei647PhosphothreonineCombined sources1
Modified residuei685Omega-N-methylarginineCombined sources1
Modified residuei694Omega-N-methylarginineCombined sources1
Modified residuei1028PhosphoserineCombined sources1
Modified residuei1032Omega-N-methylarginineCombined sources1
Modified residuei1042Omega-N-methylarginineCombined sources1
Modified residuei1077PhosphoserineCombined sources1
Modified residuei1092PhosphoserineCombined sources1
Modified residuei1095N6-acetyllysineCombined sources1
Modified residuei1145PhosphoserineCombined sources1
Modified residuei1147PhosphoserineCombined sources1
Modified residuei1185Phosphoserine; by PKC/PRKCACombined sources1 Publication1
Modified residuei1187PhosphoserineCombined sources1
Modified residuei1194PhosphoserineCombined sources1
Modified residuei1209PhosphoserineCombined sources1
Modified residuei1211PhosphothreonineCombined sources1
Modified residuei1231PhosphoserineCombined sources1
Modified residuei1238PhosphoserineCombined sources1
Modified residuei1596PhosphoserineCombined sources1
Isoform C (identifier: Q04637-4)
Modified residuei2N-acetylmethionineCombined sources1
Isoform 7 (identifier: Q04637-7)
Modified residuei489Omega-N-methylarginineCombined sources1
Modified residuei498Omega-N-methylarginineCombined sources1
Modified residuei509PhosphoserineCombined sources1
Isoform 8 (identifier: Q04637-8)
Modified residuei685Omega-N-methylarginineCombined sources1
Modified residuei694Omega-N-methylarginineCombined sources1
Modified residuei705PhosphoserineCombined sources1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei674 – 675Cleavage; by foot-and-mouth disease virus leader protease2
Sitei681 – 682Cleavage; by enterovirus/rhinovirus protease 2A2

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ04637.
MaxQBiQ04637.
PaxDbiQ04637.
PeptideAtlasiQ04637.
PRIDEiQ04637.

PTM databases

iPTMnetiQ04637.
PhosphoSitePlusiQ04637.
SwissPalmiQ04637.

Miscellaneous databases

PMAP-CutDBQ04637.

Expressioni

Gene expression databases

BgeeiENSG00000114867.
CleanExiHS_EIF4G1.
ExpressionAtlasiQ04637. baseline and differential.
GenevisibleiQ04637. HS.

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 (cap-binding) 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. Interacts with human adenovirus 5 100K protein; this interaction promotes translational shunt in presence of polysomes containing viral tripartite leader mRNAs (PubMed:15314025).17 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
UL54Q9J0X93EBI-73711,EBI-7967856From a different organism.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • eukaryotic initiation factor 4E binding Source: AgBase

Protein-protein interaction databases

BioGridi108296. 93 interactors.
DIPiDIP-1161N.
IntActiQ04637. 55 interactors.
MINTiMINT-135718.
STRINGi9606.ENSP00000338020.

Chemistry databases

BindingDBiQ04637.

Structurei

Secondary structure

11599
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi181 – 183Combined sources3
Helixi185 – 187Combined sources3
Helixi193 – 197Combined sources5
Helixi614 – 619Combined sources6
Helixi1234 – 1256Combined sources23
Helixi1259 – 1267Combined sources9
Helixi1272 – 1274Combined sources3
Helixi1275 – 1286Combined sources12
Turni1287 – 1289Combined sources3
Helixi1291 – 1306Combined sources16
Helixi1312 – 1329Combined sources18
Turni1330 – 1332Combined sources3
Helixi1336 – 1344Combined sources9
Helixi1345 – 1348Combined sources4
Helixi1355 – 1362Combined sources8
Turni1363 – 1365Combined sources3
Helixi1366 – 1369Combined sources4
Helixi1372 – 1387Combined sources16
Helixi1389 – 1398Combined sources10
Helixi1403 – 1405Combined sources3
Helixi1413 – 1419Combined sources7
Helixi1423 – 1425Combined sources3
Helixi1439 – 1452Combined sources14
Helixi1457 – 1467Combined sources11
Helixi1470 – 1473Combined sources4
Helixi1476 – 1489Combined sources14
Beta strandi1494 – 1496Combined sources3
Helixi1501 – 1514Combined sources14
Helixi1518 – 1534Combined sources17
Helixi1541 – 1551Combined sources11
Helixi1557 – 1563Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LJ2X-ray2.38C/D172-199[»]
1UG3X-ray2.24A/B1233-1571[»]
2W97X-ray2.29E/F609-622[»]
4AZAX-ray2.16B/D609-620[»]
4F02X-ray2.00C/F178-203[»]
5EHCX-ray2.40B609-622[»]
5EI3X-ray1.71B609-622[»]
5EIRX-ray2.69B609-622[»]
DisProtiDP00406.
ProteinModelPortaliQ04637.
SMRiQ04637.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04637.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini565 – 792MIF4GPROSITE-ProRule annotationAdd BLAST228
Domaini1241 – 1363MIPROSITE-ProRule annotationAdd BLAST123
Domaini1433 – 1599W2PROSITE-ProRule annotationAdd BLAST167

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni172 – 200PABPC1-bindingAdd BLAST29
Regioni607 – 618EIF4E-bindingAdd BLAST12
Regioni682 – 1085eIF3/EIF4A-bindingAdd BLAST404
Regioni1450 – 1599EIF4A-bindingAdd BLAST150
Regioni1585 – 1599Necessary but not sufficient for MKNK1-bindingAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi454 – 467Poly-GluAdd BLAST14
Compositional biasi501 – 504Poly-Ala4

Sequence similaritiesi

Contains 1 MI domain.PROSITE-ProRule annotation
Contains 1 MIF4G domain.Curated
Contains 1 W2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0401. Eukaryota.
ENOG410XS4P. LUCA.
GeneTreeiENSGT00530000063038.
HOGENOMiHOG000231658.
HOVERGENiHBG052083.
InParanoidiQ04637.
KOiK03260.
OMAiAIAREHM.
OrthoDBiEOG091G03ZW.
PhylomeDBiQ04637.
TreeFamiTF101527.

Family and domain databases

Gene3Di1.25.40.180. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

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

        10         20         30         40         50
MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH
60 70 80 90 100
FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ
110 120 130 140 150
GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG
160 170 180 190 200
VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA
210 220 230 240 250
RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI IADRPGLPGP
260 270 280 290 300
EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES
310 320 330 340 350
TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP
360 370 380 390 400
LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP
410 420 430 440 450
EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS
460 470 480 490 500
PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE
510 520 530 540 550
AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA VPEVENQPPA
560 570 580 590 600
GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ
610 620 630 640 650
WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR
660 670 680 690 700
PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG
710 720 730 740 750
PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR TAADKDRGEE
760 770 780 790 800
DADGSKTQDL FRRVRSILNK LTPQMFQQLM KQVTQLAIDT EERLKGVIDL
810 820 830 840 850
IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR KLLLNRCQKE
860 870 880 890 900
FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK
910 920 930 940 950
FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK
960 970 980 990 1000
AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK
1010 1020 1030 1040 1050
TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG
1060 1070 1080 1090 1100
GWNTVPISKG SRPIDTSRLT KITKPGSIDS NNQLFAPGGR LSWGKGSSGG
1110 1120 1130 1140 1150
SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV VQRSSLSRER
1160 1170 1180 1190 1200
GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ
1210 1220 1230 1240 1250
PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII
1260 1270 1280 1290 1300
EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL
1310 1320 1330 1340 1350
LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL AELVTPILQE
1360 1370 1380 1390 1400
GGVPMGELFR EITKPLRPLG KAASLLLEIL GLLCKSMGPK KVGTLWREAG
1410 1420 1430 1440 1450
LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS EELNRQLEKL
1460 1470 1480 1490 1500
LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD
1510 1520 1530 1540 1550
VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY
1560 1570 1580 1590
DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN
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.Combined sources
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.Combined sources
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.Combined sources
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 AAC78444 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC82471 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA02185 differs from that shown. Reason: Frameshift at several positions.Curated
The sequence BAD18554 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30P → R in AAC78443 (PubMed:9755181).Curated1
Sequence conflicti138F → L in AAL92872 (PubMed:14702039).Curated1
Sequence conflicti138F → L in AAM69365 (PubMed:14702039).Curated1
Sequence conflicti149Q → R in AAL92872 (PubMed:14702039).Curated1
Sequence conflicti149Q → R in AAM69365 (PubMed:14702039).Curated1
Sequence conflicti214G → S in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti462E → D in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti468A → V in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti474A → G in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti479G → R in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti604L → P in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti604L → P in AAL92872 (PubMed:14702039).Curated1
Sequence conflicti604L → P in AAM69365 (PubMed:14702039).Curated1
Sequence conflicti604L → P in AAC82471 (PubMed:9372926).Curated1
Sequence conflicti625 – 626AS → CQ in BAA02185 (PubMed:1429670).Curated2
Sequence conflicti693P → A in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti696P → A in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti764V → W in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti878G → E in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti894R → C in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti1104K → Q in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti1121N → I in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti1185S → T in BAA02185 (PubMed:1429670).Curated1
Sequence conflicti1384C → Y in CAI46013 (PubMed:17974005).Curated1
Sequence conflicti1472Missing in BAA02185 (PubMed:1429670).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06657171P → S.1 PublicationCorresponds to variant rs113810947dbSNPEnsembl.1
Natural variantiVAR_061147161T → A.5 PublicationsCorresponds to variant rs13319149dbSNPEnsembl.1
Natural variantiVAR_055704311Y → C.1 PublicationCorresponds to variant rs16858632dbSNPEnsembl.1
Natural variantiVAR_063040432M → V.Combined sources4 PublicationsCorresponds to variant rs2178403dbSNPEnsembl.1
Natural variantiVAR_066572466 – 468Missing .1 Publication3
Natural variantiVAR_066573502A → V in PARK18. 1 PublicationCorresponds to variant rs111290936dbSNPEnsembl.1
Natural variantiVAR_066574686G → C Found in patients with Parkinson disease; unknown pathological significance. 1 PublicationCorresponds to variant rs112019125dbSNPEnsembl.1
Natural variantiVAR_036117696P → L in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs754755344dbSNPEnsembl.1
Natural variantiVAR_066575806I → V.1 PublicationCorresponds to variant rs62287499dbSNPEnsembl.1
Natural variantiVAR_066576829T → S.1 PublicationCorresponds to variant rs111500185dbSNPEnsembl.1
Natural variantiVAR_0665771164S → R Found in a patient with Parkinson disease; unknown pathological significance. 1 PublicationCorresponds to variant rs113169049dbSNPEnsembl.1
Natural variantiVAR_0665781197R → W Found in a patient with Parkinson disease; unknown pathological significance. 1 PublicationCorresponds to variant rs113388242dbSNPEnsembl.1
Natural variantiVAR_0665791205R → H in PARK18. 1 PublicationCorresponds to variant rs112176450dbSNPEnsembl.1
Natural variantiVAR_0611481229P → A.1 PublicationCorresponds to variant rs35629949dbSNPEnsembl.1
Natural variantiVAR_0557051233L → P.1 PublicationCorresponds to variant rs2230570dbSNPEnsembl.1
Natural variantiVAR_0665801257N → S.1 PublicationCorresponds to variant rs73053766dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187231 – 196Missing in isoform E and isoform 7. 1 PublicationAdd BLAST196
Alternative sequenceiVSP_0187221 – 164Missing in isoform D. CuratedAdd BLAST164
Alternative sequenceiVSP_0187211 – 87Missing in isoform C. 1 PublicationAdd BLAST87
Alternative sequenceiVSP_0187201 – 40Missing in isoform B. 1 PublicationAdd BLAST40
Alternative sequenceiVSP_04739648R → RQGGFRSL in isoform 9. Curated1
Alternative sequenceiVSP_047397696P → PQ in isoform 7 and isoform 8. 4 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS77866.1. [Q04637-3]
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

EnsembliENST00000342981; 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]
GeneDBiLmjF.10.1080:pep.
GeneIDi1981.
KEGGihsa:1981.
UCSCiuc003fnp.4. human. [Q04637-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS77866.1. [Q04637-3]
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LJ2X-ray2.38C/D172-199[»]
1UG3X-ray2.24A/B1233-1571[»]
2W97X-ray2.29E/F609-622[»]
4AZAX-ray2.16B/D609-620[»]
4F02X-ray2.00C/F178-203[»]
5EHCX-ray2.40B609-622[»]
5EI3X-ray1.71B609-622[»]
5EIRX-ray2.69B609-622[»]
DisProtiDP00406.
ProteinModelPortaliQ04637.
SMRiQ04637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108296. 93 interactors.
DIPiDIP-1161N.
IntActiQ04637. 55 interactors.
MINTiMINT-135718.
STRINGi9606.ENSP00000338020.

Chemistry databases

BindingDBiQ04637.

PTM databases

iPTMnetiQ04637.
PhosphoSitePlusiQ04637.
SwissPalmiQ04637.

Polymorphism and mutation databases

BioMutaiEIF4G1.
DMDMi294862538.

Proteomic databases

EPDiQ04637.
MaxQBiQ04637.
PaxDbiQ04637.
PeptideAtlasiQ04637.
PRIDEiQ04637.

Protocols and materials databases

DNASUi1981.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342981; 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]
GeneDBiLmjF.10.1080:pep.
GeneIDi1981.
KEGGihsa:1981.
UCSCiuc003fnp.4. human. [Q04637-1]

Organism-specific databases

CTDi1981.
DisGeNETi1981.
GeneCardsiEIF4G1.
HGNCiHGNC:3296. EIF4G1.
HPAiCAB014774.
HPA028487.
HPA043866.
MalaCardsiEIF4G1.
MIMi600495. gene.
614251. phenotype.
neXtProtiNX_Q04637.
OpenTargetsiENSG00000114867.
Orphaneti2828. Young adult-onset Parkinsonism.
PharmGKBiPA27722.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0401. Eukaryota.
ENOG410XS4P. LUCA.
GeneTreeiENSGT00530000063038.
HOGENOMiHOG000231658.
HOVERGENiHBG052083.
InParanoidiQ04637.
KOiK03260.
OMAiAIAREHM.
OrthoDBiEOG091G03ZW.
PhylomeDBiQ04637.
TreeFamiTF101527.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114867-MONOMER.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-429947. Deadenylation of mRNA.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiQ04637.

Miscellaneous databases

ChiTaRSiEIF4G1. human.
EvolutionaryTraceiQ04637.
GeneWikiiEukaryotic_translation_initiation_factor_4_gamma.
GenomeRNAii1981.
PMAP-CutDBQ04637.
PROiQ04637.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114867.
CleanExiHS_EIF4G1.
ExpressionAtlasiQ04637. baseline and differential.
GenevisibleiQ04637. HS.

Family and domain databases

Gene3Di1.25.40.180. 3 hits.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 190 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.