Q04637 (IF4G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EIF4G1
Synonyms:	EIF4F, EIF4G, EIF4GI

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1599 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.2 Ref.3 Ref.10 Ref.11 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21 Ref.23 Ref.28 Ref.31 Ref.34 Ref.36 Ref.44
Post-translational modification	Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1. Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.43 Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription. Ref.13 Ref.17 Ref.22
Involvement in disease	Defects in EIF4G1 are the cause of Parkinson disease type 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. Ref.47
Sequence similarities	Belongs to the eIF4G family. Contains 1 MI domain. Contains 1 MIF4G domain. Contains 1 W2 domain.
Sequence caution	The sequence AAC78444.1 differs from that shown. Reason: Erroneous initiation. The sequence AAC82471.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA02185.1 differs from that shown. Reason: Frameshift at several positions. The sequence BAD18554.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	Host-virus interaction Protein biosynthesis Translation regulation
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Disease	Disease mutation Neurodegeneration Parkinson disease Parkinsonism
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	insulin receptor signaling pathway Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA poly(A) tail shortening Traceable author statement. Source: Reactome regulation of translational initiation Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome eukaryotic translation initiation factor 4F complex Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction Ref.21Ref.20Ref.28Ref.31. Source: UniProtKB translation initiation factor activity Traceable author statement Ref.16Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4A1	P60842	7	EBI-73711,EBI-73449
EIF4A2	Q14240	3	EBI-73711,EBI-73473
EIF4E	P06730	2	EBI-73711,EBI-73440
HNRNPD	Q14103-4	3	EBI-73711,EBI-432545
MKNK1	Q9BUB5	2	EBI-73711,EBI-73837

Alternative products

This entry describes 5 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform A (identifier: Q04637-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: Q04637-3)

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.

Isoform C (identifier: Q04637-4)

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.

Isoform D (identifier: Q04637-5)

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.

Isoform E (identifier: Q04637-6)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1599

1599

Eukaryotic translation initiation factor 4 gamma 1

PRO_0000007786

Regions

Domain

565 – 792

228

MIF4G

Domain

1241 – 1363

123

MI

Domain

1433 – 1599

167

W2

Region

172 – 200

29

PABPC1-binding

Region

607 – 618

12

EIF4E-binding

Region

682 – 1085

404

eIF3/EIF4A-binding

Region

1450 – 1599

150

EIF4A-binding

Region

1585 – 1599

15

Necessary but not sufficient for MKNK1-binding

Compositional bias

454 – 467

14

Poly-Glu

Compositional bias

501 – 504

4

Poly-Ala

Sites

Site

674 – 675

2

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

Site

681 – 682

2

Cleavage; by enterovirus/rhinovirus protease 2A

Amino acid modifications

Modified residue

205

1

Phosphothreonine Ref.37 Ref.38

Modified residue

207

1

Phosphothreonine Ref.37 Ref.38

Modified residue

223

1

Phosphothreonine Ref.37

Modified residue

450

1

Phosphoserine Ref.38

Modified residue

594

1

Phosphotyrosine Ref.25

Modified residue

647

1

Phosphothreonine Ref.37

Modified residue

1092

1

Phosphoserine Ref.29 Ref.37 Ref.40

Modified residue

1095

1

N6-acetyllysine Ref.41

Modified residue

1145

1

Phosphoserine Ref.26

Modified residue

1147

1

Phosphoserine Ref.26

Modified residue

1185

1

Phosphoserine; by PKC/PRKCA Ref.37 Ref.39 Ref.43

Modified residue

1187

1

Phosphoserine Ref.26 Ref.37

Modified residue

1188

1

N6-acetyllysine Ref.41

Modified residue

1209

1

Phosphoserine Ref.24 Ref.30 Ref.33 Ref.37

Modified residue

1231

1

Phosphoserine Ref.24 Ref.26 Ref.27 Ref.29 Ref.32 Ref.35 Ref.37 Ref.38 Ref.40

Modified residue

1238

1

Phosphoserine Ref.38

Modified residue

1596

1

Phosphoserine Ref.37

Natural variations

Alternative sequence

1 – 196

196

Missing in isoform E.

VSP_018723

Alternative sequence

1 – 164

164

Missing in isoform D.

VSP_018722

Alternative sequence

1 – 87

87

Missing in isoform C.

VSP_018721

Alternative sequence

1 – 40

40

Missing in isoform B.

VSP_018720

Natural variant

71

1

P → S. Ref.47
Corresponds to variant rs113810947 [ dbSNP | Ensembl ].

VAR_066571

Natural variant

161

1

T → A. Ref.2 Ref.5 Ref.7 Ref.10 Ref.47
Corresponds to variant rs13319149 [ dbSNP | Ensembl ].

VAR_061147

Natural variant

311

1

Y → C. Ref.47
Corresponds to variant rs16858632 [ dbSNP | Ensembl ].

VAR_055704

Natural variant

432

1

M → V. Ref.1 Ref.2 Ref.5 Ref.47
Corresponds to variant rs2178403 [ dbSNP | Ensembl ].

VAR_063040

Natural variant

466 – 468

3

Missing.

VAR_066572

Natural variant

502

1

A → V in PARK18. Ref.47
Corresponds to variant rs111290936 [ dbSNP | Ensembl ].

VAR_066573

Natural variant

686

1

G → C Found in patients with Parkinson disease. Ref.47
Corresponds to variant rs112019125 [ dbSNP | Ensembl ].

VAR_066574

Natural variant

696

1

P → L in a colorectal cancer sample; somatic mutation. Ref.46

VAR_036117

Natural variant

806

1

I → V. Ref.47
Corresponds to variant rs62287499 [ dbSNP | Ensembl ].

VAR_066575

Natural variant

829

1

T → S. Ref.47
Corresponds to variant rs111500185 [ dbSNP | Ensembl ].

VAR_066576

Natural variant

1164

1

S → R Found in a patient with Parkinson disease. Ref.47
Corresponds to variant rs113169049 [ dbSNP | Ensembl ].

VAR_066577

Natural variant

1197

1

R → W Found in a patient with Parkinson disease. Ref.47
Corresponds to variant rs113388242 [ dbSNP | Ensembl ].

VAR_066578

Natural variant

1205

1

R → H in PARK18. Ref.47
Corresponds to variant rs112176450 [ dbSNP | Ensembl ].

VAR_066579

Natural variant

1229

1

P → A. Ref.47
Corresponds to variant rs35629949 [ dbSNP | Ensembl ].

VAR_061148

Natural variant

1233

1

L → P. Ref.47
Corresponds to variant rs2230570 [ dbSNP | Ensembl ].

VAR_055705

Natural variant

1257

1

N → S. Ref.47
Corresponds to variant rs73053766 [ dbSNP | Ensembl ].

VAR_066580

Experimental info

Mutagenesis

174 – 178

5

KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. Ref.20

Mutagenesis

180

1

I → A: Loss of PABPC1 binding. Ref.44

Mutagenesis

182

1

I → A: Loss of PABPC1 binding. Ref.44

Mutagenesis

184 – 187

4

DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178.

Mutagenesis

192

1

I → A: Loss of PABPC1 binding. Ref.44

Mutagenesis

196

1

I → A: Loss of PABPC1 binding. Ref.44

Mutagenesis

612

1

Y → A or F: Abolishes binding to EIF4E. Ref.11

Mutagenesis

617 – 618

2

LL → AA: Abolishes binding to EIF4E.

Mutagenesis

682

1

G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. Ref.16

Mutagenesis

768

1

L → A: Abolishes binding to EIF4A; when associated with A-770 and A-775. Ref.2

Mutagenesis

771

1

L → A: Abolishes binding to EIF4A; when associated with A-767 and A-775. Ref.2

Mutagenesis

776

1

F → A: Abolishes binding to EIF4A; when associated with A-767 and A-770. Ref.2

Mutagenesis

842 – 843

2

LL → AA: Abolishes binding to EIF4A; when associated with A-850 and K-851.

Mutagenesis

851 – 852

2

FE → AK: Abolishes binding to EIF4A; when associated with A-841 and A-842.

Mutagenesis

896

1

L → A: Abolishes binding to EIF4A; when associated with A-92 and A-95. Ref.2

Mutagenesis

902

1

I → A: Abolishes binding to EIF4A; when associated with A-895 and A-95. Ref.2

Mutagenesis

905

1

L → A: Abolishes binding to EIF4A; when associated with A-895 and A-92. Ref.2

Mutagenesis

974

1

R → A: Abolishes binding to EIF4A; when associated with A-976. Ref.2

Mutagenesis

977

1

F → A: Abolishes binding to EIF4A; when associated with A-973. Ref.2

Mutagenesis

985

1

L → A: Slightly reduced binding to EIF4A; when associated with A-989. Ref.2

Mutagenesis

990

1

W → A: Slightly reduced binding to EIF4A; when associated with A-984. Ref.2

Sequence conflict

30

1

P → R in AAC78443. Ref.10

Sequence conflict

138

1

F → L in AAL92872. Ref.5

Sequence conflict

138

1

F → L in AAM69365. Ref.5

Sequence conflict

149

1

Q → R in AAL92872. Ref.5

Sequence conflict

149

1

Q → R in AAM69365. Ref.5

Sequence conflict

214

1

G → S in BAA02185. Ref.1

Sequence conflict

462

1

E → D in BAA02185. Ref.1

Sequence conflict

468

1

A → V in BAA02185. Ref.1

Sequence conflict

474

1

A → G in BAA02185. Ref.1

Sequence conflict

479

1

G → R in BAA02185. Ref.1

Sequence conflict

604

1

L → P in BAA02185. Ref.1

Sequence conflict

604

1

L → P in AAC82471. Ref.2

Sequence conflict

604

1

L → P in AAL92872. Ref.5

Sequence conflict

604

1

L → P in AAM69365. Ref.5

Sequence conflict

625 – 626

2

AS → CQ in BAA02185. Ref.1

Sequence conflict

693

1

P → A in BAA02185. Ref.1

Sequence conflict

696

1

P → AQ in BAA02185. Ref.1

Sequence conflict

696

1

P → PQ in AAC82471. Ref.2

Sequence conflict

696

1

P → PQ in AAL92872. Ref.5

Sequence conflict

696

1

P → PQ in AAM69365. Ref.5

Sequence conflict

696

1

P → PQ in CAA04500. Ref.11

Sequence conflict

764

1

V → W in BAA02185. Ref.1

Sequence conflict

878

1

G → E in BAA02185. Ref.1

Sequence conflict

894

1

R → C in BAA02185. Ref.1

Sequence conflict

1104

1

K → Q in BAA02185. Ref.1

Sequence conflict

1121

1

N → I in BAA02185. Ref.1

Sequence conflict

1185

1

S → T in BAA02185. Ref.1

Sequence conflict

1384

1

C → Y in CAI46013. Ref.7

Sequence conflict

1472

1

Missing in BAA02185. Ref.1

Secondary structure

1

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1599

Helix Strand Turn

Details...

Beta strand

181 – 183

3

Helix

185 – 187

3

Helix

193 – 196

4

Helix

1234 – 1256

23

Helix

1259 – 1267

9

Helix

1272 – 1274

3

Helix

1275 – 1286

12

Turn

1287 – 1289

3

Helix

1291 – 1306

16

Helix

1312 – 1329

18

Turn

1330 – 1332

3

Helix

1336 – 1344

9

Helix

1345 – 1348

4

Helix

1355 – 1362

8

Turn

1363 – 1365

3

Helix

1366 – 1369

4

Helix

1372 – 1387

16

Helix

1389 – 1398

10

Helix

1403 – 1405

3

Helix

1413 – 1419

7

Helix

1423 – 1425

3

Helix

1439 – 1452

14

Helix

1457 – 1467

11

Helix

1470 – 1473

4

Helix

1476 – 1489

14

Beta strand

1494 – 1496

3

Helix

1501 – 1514

14

Helix

1518 – 1534

17

Helix

1541 – 1551

11

Helix

1557 – 1563

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified April 20, 2010. Version 4. Checksum: 324088B60863DA34	FASTA	1,599	175,491
	10 20 30 40 50 60 MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH FYPSRAQPPS 70 80 90 100 110 120 SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ GAYYIPGQGR STYVVPTQQY 130 140 150 160 170 180 PVQPGAPGFY PGASPTEFGT YAGAYYPAQG VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI 190 200 210 220 230 240 RIRDPNQGGK DITEEIMSGA RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI 250 260 270 280 290 300 IADRPGLPGP EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES 310 320 330 340 350 360 TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP LASHTVEIHE 370 380 390 400 410 420 PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP EELLNGAPSP PAVDLSPVSE 430 440 450 460 470 480 PEEQAKEVTA SMAPPTIPSA TPATAPSATS PAQEEEMEEE EEEEEGEAGE AGEAESEKGG 490 500 510 520 530 540 EELLPPESTP IPANLSQNLE AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA 550 560 570 580 590 600 VPEVENQPPA GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ 610 620 630 640 650 660 WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR PLDPTRLQGI 670 680 690 700 710 720 NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG PRRSQQGPRK EPRKIIATVL 730 740 750 760 770 780 MTEDIKLNKA EKAWKPSSKR TAADKDRGEE DADGSKTQDL FRRVRSILNK LTPQMFQQLM 790 800 810 820 830 840 KQVTQLAIDT EERLKGVIDL IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR 850 860 870 880 890 900 KLLLNRCQKE FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK 910 920 930 940 950 960 FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK AKPRMDQYFN 970 980 990 1000 1010 1020 QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK TIDQIHKEAE MEEHREHIKV 1030 1040 1050 1060 1070 1080 QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG GWNTVPISKG SRPIDTSRLT KITKPGSIDS 1090 1100 1110 1120 1130 1140 NNQLFAPGGR LSWGKGSSGG SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV 1150 1160 1170 1180 1190 1200 VQRSSLSRER GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ 1210 1220 1230 1240 1250 1260 PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII EEYLHLNDMK 1270 1280 1290 1300 1310 1320 EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL LHQLLCAGHL STAQYYQGLY 1330 1340 1350 1360 1370 1380 EILELAEDME IDIPHVWLYL AELVTPILQE GGVPMGELFR EITKPLRPLG KAASLLLEIL 1390 1400 1410 1420 1430 1440 GLLCKSMGPK KVGTLWREAG LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS 1450 1460 1470 1480 1490 1500 EELNRQLEKL LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD 1510 1520 1530 1540 1550 1560 VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY DEDVVKEDAF 1570 1580 1590 YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN
	Isoform B [UniParc]. Checksum: 22F62E219E629C0E	FASTA	1,559	171,514
	10 20 30 40 50 60 MNTPSQPRQH FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ 70 80 90 100 110 120 GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG VQQFPTGVAP 130 140 150 160 170 180 TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA RTASTPTPPQ TGGGLEPQAN 190 200 210 220 230 240 GETPQVAVIV RPDDRSQGAI IADRPGLPGP EHSPSESQPS SPSPTPSPSP VLEPGSEPNL 250 260 270 280 290 300 AVLSIPGDTM TTIQMSVEES TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF 310 320 330 340 350 360 SSSPLQAPTP LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP 370 380 390 400 410 420 EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS PAQEEEMEEE 430 440 450 460 470 480 EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE AAAATQVAVS VPKRRRKIKE 490 500 510 520 530 540 LNKKEAVGDL LDAFKEANPA VPEVENQPPA GSNPGPESEG SGVPPRPEEA DETWDSKEDK 550 560 570 580 590 600 IHNAENIQPG EQKYEYKSDQ WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV 610 620 630 640 650 660 LDKANKTPLR PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG 670 680 690 700 710 720 PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR TAADKDRGEE DADGSKTQDL 730 740 750 760 770 780 FRRVRSILNK LTPQMFQQLM KQVTQLAIDT EERLKGVIDL IFEKAISEPN FSVAYANMCR 790 800 810 820 830 840 CLMALKVPTT EKPTVTVNFR KLLLNRCQKE FEKDKDDDEV FEKKQKEMDE AATAEERGRL 850 860 870 880 890 900 KEELEEARDI ARRRSLGNIK FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT 910 920 930 940 950 960 TIGKDLDFEK AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK 970 980 990 1000 1010 1020 TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG GWNTVPISKG 1030 1040 1050 1060 1070 1080 SRPIDTSRLT KITKPGSIDS NNQLFAPGGR LSWGKGSSGG SGAKPSDAAS EAARPATSTL 1090 1100 1110 1120 1130 1140 NRFSALQQAV PTESTDNRRV VQRSSLSRER GEKAGDRGDR LERSERGGDR GDRLDRARTP 1150 1160 1170 1180 1190 1200 ATKRSFSKEV EERSRERPSQ PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE 1210 1220 1230 1240 1250 1260 ELEKKSKAII EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL 1270 1280 1290 1300 1310 1320 LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL AELVTPILQE GGVPMGELFR 1330 1340 1350 1360 1370 1380 EITKPLRPLG KAASLLLEIL GLLCKSMGPK KVGTLWREAG LSWKEFLPEG QDIGAFVAEQ 1390 1400 1410 1420 1430 1440 KVEYTLGEES EAPGQRALPS EELNRQLEKL LKEGSSNQRV FDWIEANLSE QQIVSNTLVR 1450 1460 1470 1480 1490 1500 ALMTAVCYSA IIFETPLRVD VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN 1510 1520 1530 1540 1550 LLRMFFDALY DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN
	Isoform C [UniParc]. Checksum: 09DD6DC263462CB6	FASTA	1,512	166,619
	10 20 30 40 50 60 MMIPSQISYP ASQGAYYIPG QGRSTYVVPT QQYPVQPGAP GFYPGASPTE FGTYAGAYYP 70 80 90 100 110 120 AQGVQQFPTG VAPTPVLMNQ PPQIAPKRER KTIRIRDPNQ GGKDITEEIM SGARTASTPT 130 140 150 160 170 180 PPQTGGGLEP QANGETPQVA VIVRPDDRSQ GAIIADRPGL PGPEHSPSES QPSSPSPTPS 190 200 210 220 230 240 PSPVLEPGSE PNLAVLSIPG DTMTTIQMSV EESTPISRET GEPYRLSPEP TPLAEPILEV 250 260 270 280 290 300 EVTLSKPVPE SEFSSSPLQA PTPLASHTVE IHEPNGMVPS EDLEPEVESS PELAPPPACP 310 320 330 340 350 360 SESPVPIAPT AQPEELLNGA PSPPAVDLSP VSEPEEQAKE VTASMAPPTI PSATPATAPS 370 380 390 400 410 420 ATSPAQEEEM EEEEEEEEGE AGEAGEAESE KGGEELLPPE STPIPANLSQ NLEAAAATQV 430 440 450 460 470 480 AVSVPKRRRK IKELNKKEAV GDLLDAFKEA NPAVPEVENQ PPAGSNPGPE SEGSGVPPRP 490 500 510 520 530 540 EEADETWDSK EDKIHNAENI QPGEQKYEYK SDQWKPLNLE EKKRYDREFL LGFQFIFASM 550 560 570 580 590 600 QKPEGLPHIS DVVLDKANKT PLRPLDPTRL QGINCGPDFT PSFANLGRTT LSTRGPPRGG 610 620 630 640 650 660 PGGELPRGPA GLGPRRSQQG PRKEPRKIIA TVLMTEDIKL NKAEKAWKPS SKRTAADKDR 670 680 690 700 710 720 GEEDADGSKT QDLFRRVRSI LNKLTPQMFQ QLMKQVTQLA IDTEERLKGV IDLIFEKAIS 730 740 750 760 770 780 EPNFSVAYAN MCRCLMALKV PTTEKPTVTV NFRKLLLNRC QKEFEKDKDD DEVFEKKQKE 790 800 810 820 830 840 MDEAATAEER GRLKEELEEA RDIARRRSLG NIKFIGELFK LKMLTEAIMH DCVVKLLKNH 850 860 870 880 890 900 DEESLECLCR LLTTIGKDLD FEKAKPRMDQ YFNQMEKIIK EKKTSSRIRF MLQDVLDLRG 910 920 930 940 950 960 SNWVPRRGDQ GPKTIDQIHK EAEMEEHREH IKVQQLMAKG SDKRRGGPPG PPISRGLPLV 970 980 990 1000 1010 1020 DDGGWNTVPI SKGSRPIDTS RLTKITKPGS IDSNNQLFAP GGRLSWGKGS SGGSGAKPSD 1030 1040 1050 1060 1070 1080 AASEAARPAT STLNRFSALQ QAVPTESTDN RRVVQRSSLS RERGEKAGDR GDRLERSERG 1090 1100 1110 1120 1130 1140 GDRGDRLDRA RTPATKRSFS KEVEERSRER PSQPEGLRKA ASLTEDRDRG RDAVKREAAL 1150 1160 1170 1180 1190 1200 PPVSPLKAAL SEEELEKKSK AIIEEYLHLN DMKEAVQCVQ ELASPSLLFI FVRHGVESTL 1210 1220 1230 1240 1250 1260 ERSAIAREHM GQLLHQLLCA GHLSTAQYYQ GLYEILELAE DMEIDIPHVW LYLAELVTPI 1270 1280 1290 1300 1310 1320 LQEGGVPMGE LFREITKPLR PLGKAASLLL EILGLLCKSM GPKKVGTLWR EAGLSWKEFL 1330 1340 1350 1360 1370 1380 PEGQDIGAFV AEQKVEYTLG EESEAPGQRA LPSEELNRQL EKLLKEGSSN QRVFDWIEAN 1390 1400 1410 1420 1430 1440 LSEQQIVSNT LVRALMTAVC YSAIIFETPL RVDVAVLKAR AKLLQKYLCD EQKELQALYA 1450 1460 1470 1480 1490 1500 LQALVVTLEQ PPNLLRMFFD ALYDEDVVKE DAFYSWESSK DPAEQQGKGV ALKSVTAFFK 1510 WLREAEEESD HN
	Isoform D [UniParc]. Checksum: 6F7E9DE4106E73B9	FASTA	1,435	158,517
	10 20 30 40 50 60 MNQPPQIAPK RERKTIRIRD PNQGGKDITE EIMSGARTAS TPTPPQTGGG LEPQANGETP 70 80 90 100 110 120 QVAVIVRPDD RSQGAIIADR PGLPGPEHSP SESQPSSPSP TPSPSPVLEP GSEPNLAVLS 130 140 150 160 170 180 IPGDTMTTIQ MSVEESTPIS RETGEPYRLS PEPTPLAEPI LEVEVTLSKP VPESEFSSSP 190 200 210 220 230 240 LQAPTPLASH TVEIHEPNGM VPSEDLEPEV ESSPELAPPP ACPSESPVPI APTAQPEELL 250 260 270 280 290 300 NGAPSPPAVD LSPVSEPEEQ AKEVTASMAP PTIPSATPAT APSATSPAQE EEMEEEEEEE 310 320 330 340 350 360 EGEAGEAGEA ESEKGGEELL PPESTPIPAN LSQNLEAAAA TQVAVSVPKR RRKIKELNKK 370 380 390 400 410 420 EAVGDLLDAF KEANPAVPEV ENQPPAGSNP GPESEGSGVP PRPEEADETW DSKEDKIHNA 430 440 450 460 470 480 ENIQPGEQKY EYKSDQWKPL NLEEKKRYDR EFLLGFQFIF ASMQKPEGLP HISDVVLDKA 490 500 510 520 530 540 NKTPLRPLDP TRLQGINCGP DFTPSFANLG RTTLSTRGPP RGGPGGELPR GPAGLGPRRS 550 560 570 580 590 600 QQGPRKEPRK IIATVLMTED IKLNKAEKAW KPSSKRTAAD KDRGEEDADG SKTQDLFRRV 610 620 630 640 650 660 RSILNKLTPQ MFQQLMKQVT QLAIDTEERL KGVIDLIFEK AISEPNFSVA YANMCRCLMA 670 680 690 700 710 720 LKVPTTEKPT VTVNFRKLLL NRCQKEFEKD KDDDEVFEKK QKEMDEAATA EERGRLKEEL 730 740 750 760 770 780 EEARDIARRR SLGNIKFIGE LFKLKMLTEA IMHDCVVKLL KNHDEESLEC LCRLLTTIGK 790 800 810 820 830 840 DLDFEKAKPR MDQYFNQMEK IIKEKKTSSR IRFMLQDVLD LRGSNWVPRR GDQGPKTIDQ 850 860 870 880 890 900 IHKEAEMEEH REHIKVQQLM AKGSDKRRGG PPGPPISRGL PLVDDGGWNT VPISKGSRPI 910 920 930 940 950 960 DTSRLTKITK PGSIDSNNQL FAPGGRLSWG KGSSGGSGAK PSDAASEAAR PATSTLNRFS 970 980 990 1000 1010 1020 ALQQAVPTES TDNRRVVQRS SLSRERGEKA GDRGDRLERS ERGGDRGDRL DRARTPATKR 1030 1040 1050 1060 1070 1080 SFSKEVEERS RERPSQPEGL RKAASLTEDR DRGRDAVKRE AALPPVSPLK AALSEEELEK 1090 1100 1110 1120 1130 1140 KSKAIIEEYL HLNDMKEAVQ CVQELASPSL LFIFVRHGVE STLERSAIAR EHMGQLLHQL 1150 1160 1170 1180 1190 1200 LCAGHLSTAQ YYQGLYEILE LAEDMEIDIP HVWLYLAELV TPILQEGGVP MGELFREITK 1210 1220 1230 1240 1250 1260 PLRPLGKAAS LLLEILGLLC KSMGPKKVGT LWREAGLSWK EFLPEGQDIG AFVAEQKVEY 1270 1280 1290 1300 1310 1320 TLGEESEAPG QRALPSEELN RQLEKLLKEG SSNQRVFDWI EANLSEQQIV SNTLVRALMT 1330 1340 1350 1360 1370 1380 AVCYSAIIFE TPLRVDVAVL KARAKLLQKY LCDEQKELQA LYALQALVVT LEQPPNLLRM 1390 1400 1410 1420 1430 FFDALYDEDV VKEDAFYSWE SSKDPAEQQG KGVALKSVTA FFKWLREAEE ESDHN
	Isoform E [UniParc]. Checksum: 3E93A66EE3DFDDA9	FASTA	1,403	154,805
	10 20 30 40 50 60 MSGARTASTP TPPQTGGGLE PQANGETPQV AVIVRPDDRS QGAIIADRPG LPGPEHSPSE 70 80 90 100 110 120 SQPSSPSPTP SPSPVLEPGS EPNLAVLSIP GDTMTTIQMS VEESTPISRE TGEPYRLSPE 130 140 150 160 170 180 PTPLAEPILE VEVTLSKPVP ESEFSSSPLQ APTPLASHTV EIHEPNGMVP SEDLEPEVES 190 200 210 220 230 240 SPELAPPPAC PSESPVPIAP TAQPEELLNG APSPPAVDLS PVSEPEEQAK EVTASMAPPT 250 260 270 280 290 300 IPSATPATAP SATSPAQEEE MEEEEEEEEG EAGEAGEAES EKGGEELLPP ESTPIPANLS 310 320 330 340 350 360 QNLEAAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE ANPAVPEVEN QPPAGSNPGP 370 380 390 400 410 420 ESEGSGVPPR PEEADETWDS KEDKIHNAEN IQPGEQKYEY KSDQWKPLNL EEKKRYDREF 430 440 450 460 470 480 LLGFQFIFAS MQKPEGLPHI SDVVLDKANK TPLRPLDPTR LQGINCGPDF TPSFANLGRT 490 500 510 520 530 540 TLSTRGPPRG GPGGELPRGP AGLGPRRSQQ GPRKEPRKII ATVLMTEDIK LNKAEKAWKP 550 560 570 580 590 600 SSKRTAADKD RGEEDADGSK TQDLFRRVRS ILNKLTPQMF QQLMKQVTQL AIDTEERLKG 610 620 630 640 650 660 VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT VNFRKLLLNR CQKEFEKDKD 670 680 690 700 710 720 DDEVFEKKQK EMDEAATAEE RGRLKEELEE ARDIARRRSL GNIKFIGELF KLKMLTEAIM 730 740 750 760 770 780 HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD QYFNQMEKII KEKKTSSRIR 790 800 810 820 830 840 FMLQDVLDLR GSNWVPRRGD QGPKTIDQIH KEAEMEEHRE HIKVQQLMAK GSDKRRGGPP 850 860 870 880 890 900 GPPISRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG SIDSNNQLFA PGGRLSWGKG 910 920 930 940 950 960 SSGGSGAKPS DAASEAARPA TSTLNRFSAL QQAVPTESTD NRRVVQRSSL SRERGEKAGD 970 980 990 1000 1010 1020 RGDRLERSER GGDRGDRLDR ARTPATKRSF SKEVEERSRE RPSQPEGLRK AASLTEDRDR 1030 1040 1050 1060 1070 1080 GRDAVKREAA LPPVSPLKAA LSEEELEKKS KAIIEEYLHL NDMKEAVQCV QELASPSLLF 1090 1100 1110 1120 1130 1140 IFVRHGVEST LERSAIAREH MGQLLHQLLC AGHLSTAQYY QGLYEILELA EDMEIDIPHV 1150 1160 1170 1180 1190 1200 WLYLAELVTP ILQEGGVPMG ELFREITKPL RPLGKAASLL LEILGLLCKS MGPKKVGTLW 1210 1220 1230 1240 1250 1260 REAGLSWKEF LPEGQDIGAF VAEQKVEYTL GEESEAPGQR ALPSEELNRQ LEKLLKEGSS 1270 1280 1290 1300 1310 1320 NQRVFDWIEA NLSEQQIVSN TLVRALMTAV CYSAIIFETP LRVDVAVLKA RAKLLQKYLC 1330 1340 1350 1360 1370 1380 DEQKELQALY ALQALVVTLE QPPNLLRMFF DALYDEDVVK EDAFYSWESS KDPAEQQGKG 1390 1400 VALKSVTAFF KWLREAEEES DHN

References

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[2]	"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: 9372926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), 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.
[3]	"A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation." Imataka H., Gradi A., Sonenberg N. EMBO J. 17:7480-7489(1998) [PubMed: 9857202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PABPC1.
[4]	"A novel functional human eukaryotic translation initiation factor 4G." Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N. Mol. Cell. Biol. 18:334-342(1998) [PubMed: 9418880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
[5]	"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: 12052860] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANTS ALA-161 AND VAL-432, ALTERNATIVE INITIATION.
[6]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ALA-161. Tissue: Endometrial tumor.
[8]	"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: 16641997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 9755181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-234, VARIANT ALA-161, INTERACTION WITH ROTAVIRAL NSP3.
[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: 7651417] [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.
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[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: 7935836] [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: 8521827] [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: 8961935] [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: 9755863] [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: 10872469] [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: 9878069] [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: 10996799] [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: 10970864] [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: 11034318] [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: 11154262] [Abstract] Cited for: INTERACTION WITH MKNK2.
[24]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209 AND SER-1231, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-594, MASS SPECTROMETRY.
[26]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145; SER-1147; SER-1187 AND SER-1231, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"Post-transcriptional regulation of thioredoxin by the stress inducible heterogenous ribonucleoprotein A18." Yang R., Weber D.J., Carrier F. Nucleic Acids Res. 34:1224-1236(2006) [PubMed: 16513844] [Abstract] Cited for: INTERACTION WITH CIRBP.
[29]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092 AND SER-1231, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[31]	"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: 17284590] [Abstract] Cited for: INTERACTION WITH RBM4.
[32]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209, MASS SPECTROMETRY. Tissue: Platelet.
[34]	"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: 18799579] [Abstract] Cited for: INTERACTION WITH ROTAVIRUS A NSP3.
[35]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"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: 18025107] [Abstract] Cited for: INTERACTION WITH MIF4GD.
[37]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; THR-207; THR-223; THR-647; SER-1092; SER-1185; SER-1187; SER-1209; SER-1231 AND SER-1596, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[38]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; THR-207; SER-450; SER-1231 AND SER-1238, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[39]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185, MASS SPECTROMETRY.
[40]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092 AND SER-1231, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[41]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095 AND LYS-1188, MASS SPECTROMETRY.
[42]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]	"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: 21576361] [Abstract] Cited for: PHOSPHORYLATION AT SER-1185.
[44]	"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: 12086624] [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.
[45]	"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: 16698552] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571.
[46]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-696.
[47]	"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: 21907011] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D12686 mRNA. Translation: BAA02185.1. Frameshift.
AF104913 mRNA. Translation: AAC82471.1. Different initiation.
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: EAW78262.1.
CH471052 Genomic DNA. Translation: EAW78264.1.
CH471052 Genomic DNA. Translation: EAW78265.1.
CH471052 Genomic DNA. Translation: EAW78267.1.
AF002816 mRNA. Translation: AAC78443.1.
AF004836 Genomic DNA. Translation: AAC78444.1. Different initiation.
AJ001046 mRNA. Translation: CAA04500.1.

IPI

IPI00386533.
IPI00552639.
IPI00759560.
IPI00798400.
IPI00955980.

PIR

A44453.

RefSeq

NP_886553.3. NM_182917.4.
NP_937884.1. NM_198241.2.
NP_937885.1. NM_198242.2.

UniGene

Hs.433750.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LJ2	X-ray	2.38	C/D	172-199	[»]
1UG3	X-ray	2.24	A/B	1234-1571	[»]
2W97	X-ray	2.29	E/F	609-622	[»]

ProteinModelPortal

Q04637.

SMR

Q04637. Positions 173-199, 751-991, 1234-1592.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1161N.

IntAct

Q04637. 23 interactions.

MINT

MINT-135718.

STRING

Q04637.

PTM databases

PhosphoSite

Q04637.

Polymorphism databases

DMDM

294862538.

Proteomic databases

PRIDE

Q04637.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342981; ENSP00000343450; ENSG00000114867.
ENST00000434841; ENSP00000392521; ENSG00000114867.

GeneID

1981.

KEGG

hsa:1981.

UCSC

uc003fnp.1. human.
uc003fnt.1. human.

Organism-specific databases

CTD

1981.

GeneCards

GC03P184032.

HGNC

HGNC:3296. EIF4G1.

HPA

CAB014774.
HPA028487.

MIM

600495. gene.
614251. phenotype.

neXtProt

NX_Q04637.

PharmGKB

PA27722.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10297.

HOVERGEN

HBG052083.

PhylomeDB

Q04637.

Enzyme and pathway databases

Pathway_Interaction_DB

mtor_4pathway. mTOR signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q04637.

Bgee

Q04637.

CleanEx

HS_EIF4G1.

Genevestigator

Q04637.

GermOnline

ENSG00000114867. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR003307. eIF5C.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]

Gene3D

G3DSA:1.25.40.180. MIF4-like_typ_1/2/3. 2 hits.

KO

K03260.

Pfam

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

SMART

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

SUPFAM

SSF48371. ARM-type_fold. 3 hits.

PROSITE

PS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

8013.

PMAP-CutDB

Q04637.

SOURCE

Search...

Entry information

Entry name

IF4G1_HUMAN

Accession

Primary (citable) accession number: Q04637
Secondary accession number(s): D3DNT4 , D3DNT5, O43177, O95066, Q5HYG0, Q6ZN21, Q8N102

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	April 20, 2010
Last modified:	January 25, 2012
This is version 135 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.