Reviewed, UniProtKB/Swiss-Prot Q04637 (IF4G1_HUMAN)

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	1600 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis. Ref.2 Ref.3 Ref.8 Ref.9 Ref.12 Ref.13 Ref.17 Ref.18 Ref.19 Ref.21 Ref.30 Ref.32 Ref.35
Post-translational modification	Phosphorylated at multiple sites in vivo. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.33 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.11 Ref.15 Ref.20
Sequence similarities	Belongs to the eIF4G family. Contains 1 MI domain. Contains 1 MIF4G domain. Contains 1 W2 domain.
Sequence caution	The sequence BAA02185.1 differs from that shown. Reason: Frameshift at several positions. The sequence BAD18554.1 differs from that shown. Reason: Miscellaneous discrepancy. Aberrant splicing.

Ontologies

Keywords
Biological process	Host-virus interaction Protein biosynthesis Translation regulation
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	RNA metabolic process Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of translational initiation Ref.2 Ref.14 Non-traceable author statement. Source: UniProtKB translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation initiation factor 4F complex Ref.3 Traceable author statement. Source: ProtInc
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.17 Ref.18 Ref.19 Ref.35 Inferred from physical interaction. Source: UniProtKB translation initiation factor activity Ref.2 Ref.14 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P03536	1	EBI-73711,EBI-296448	From a different organism.
EIF4A1	P60842	5	EBI-73711,EBI-73449
EIF4A2	Q14240	3	EBI-73711,EBI-73473
EIF4E	P06730	1	EBI-73711,EBI-73440
Eif4e2	Q8BMB3	1	EBI-73711,EBI-398682	From a different organism.
GABARAPL2	P60520	1	EBI-73711,EBI-720116
HNRNPD	Q14103-1	1	EBI-73711,EBI-432527
HNRNPD	Q14103-2	1	EBI-73711,EBI-432533
HNRNPD	Q14103-3	1	EBI-73711,EBI-432539
HNRNPD	Q14103-4	1	EBI-73711,EBI-432545
MAGEA6	P43360	1	EBI-73711,EBI-1045155
MKNK1	Q9BUB5	1	EBI-73711,EBI-73837
PABPC1	P11940	1	EBI-73711,EBI-81531
PDCD4	Q53EL6	1	EBI-73711,EBI-935824

Alternative products

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

Isoform 1 (identifier: Q04637-1)

Also known as: A;

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 1.

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 1.

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 1.

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 1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1600

1600

Eukaryotic translation initiation factor 4 gamma 1

PRO_0000007786

Regions

Domain

565 – 792

228

MIF4G

Domain

1242 – 1364

123

MI

Domain

1434 – 1600

167

W2

Region

172 – 200

29

PABPC1-binding

Region

607 – 618

12

EIF4E-binding

Region

682 – 1086

405

eIF3/EIF4A-binding

Region

1451 – 1600

150

EIF4A-binding

Region

1586 – 1600

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.33

Modified residue

207

1

Phosphothreonine Ref.33

Modified residue

223

1

Phosphothreonine Ref.33

Modified residue

594

1

Phosphotyrosine Ref.23

Modified residue

647

1

Phosphothreonine Ref.33

Modified residue

1093

1

Phosphoserine Ref.26 Ref.33

Modified residue

1146

1

Phosphoserine Ref.24

Modified residue

1148

1

Phosphoserine Ref.24

Modified residue

1186

1

Phosphoserine Ref.24 Ref.33

Modified residue

1188

1

Phosphoserine Ref.33

Modified residue

1210

1

Phosphoserine Ref.22 Ref.27 Ref.29 Ref.33

Modified residue

1232

1

Phosphoserine Ref.22 Ref.24 Ref.25 Ref.26 Ref.28 Ref.31 Ref.33

Modified residue

1597

1

Phosphoserine Ref.33

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

311

1

Y → C: dbSNP rs16858632.

VAR_055704

Natural variant

696

1

P → L in a colorectal cancer sample; somatic mutation. Ref.37

VAR_036117

Natural variant

1234

1

L → P: dbSNP rs2230570.

VAR_055705

Experimental info

Mutagenesis

174 – 178

5

KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. Ref.18

Mutagenesis

180

1

I → A: Loss of PABPC1 binding. Ref.35

Mutagenesis

182

1

I → A: Loss of PABPC1 binding. Ref.35

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.35

Mutagenesis

196

1

I → A: Loss of PABPC1 binding. Ref.35

Mutagenesis

612

1

Y → A or F: Abolishes binding to EIF4E. Ref.9

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.14

Mutagenesis

769

1

L → A: Abolishes binding to EIF4A; when associated with A-772 and A-777. Ref.2

Mutagenesis

772

1

L → A: Abolishes binding to EIF4A; when associated with A-769 and A-777. Ref.2

Mutagenesis

777

1

F → A: Abolishes binding to EIF4A; when associated with A-769 and A-772. Ref.2

Mutagenesis

843 – 844

2

LL → AA: Abolishes binding to EIF4A; when associated with A-852 and K-853.

Mutagenesis

852 – 853

2

FE → AK: Abolishes binding to EIF4A; when associated with A-843 and A-844.

Mutagenesis

897

1

L → A: Abolishes binding to EIF4A; when associated with A-903 and A-906. Ref.2

Mutagenesis

903

1

I → A: Abolishes binding to EIF4A; when associated with A-897 and A-906. Ref.2

Mutagenesis

906

1

L → A: Abolishes binding to EIF4A; when associated with A-897 and A-903. Ref.2

Mutagenesis

975

1

R → A: Abolishes binding to EIF4A; when associated with A-978. Ref.2

Mutagenesis

978

1

F → A: Abolishes binding to EIF4A; when associated with A-975. Ref.2

Mutagenesis

986

1

L → A: Slightly reduced binding to EIF4A; when associated with A-991. Ref.2

Mutagenesis

991

1

W → A: Slightly reduced binding to EIF4A; when associated with A-986. Ref.2

Sequence conflict

30

1

P → R in AAC78443. Ref.8

Sequence conflict

138

1

L → F Ref.3

Sequence conflict

138

1

L → F Ref.7

Sequence conflict

138

1

L → F in AAC78443. Ref.8

Sequence conflict

149

1

R → Q Ref.3

Sequence conflict

149

1

R → Q Ref.7

Sequence conflict

149

1

R → Q in AAC78443. Ref.8

Sequence conflict

214

1

G → S in BAA02185. Ref.4

Sequence conflict

432

1

V → M in CAI46013. Ref.7

Sequence conflict

462

1

E → D in BAA02185. Ref.4

Sequence conflict

468

1

A → V in BAA02185. Ref.4

Sequence conflict

474

1

A → G in BAA02185. Ref.4

Sequence conflict

479

1

G → R in BAA02185. Ref.4

Sequence conflict

604

1

P → L in CAI46013. Ref.7

Sequence conflict

625 – 626

2

AS → CQ in BAA02185. Ref.4

Sequence conflict

697

1

Missing Ref.4

Sequence conflict

697

1

Missing Ref.7

Sequence conflict

765

1

V → W in BAA02185. Ref.4

Sequence conflict

879

1

G → E in BAA02185. Ref.4

Sequence conflict

895

1

R → C in BAA02185. Ref.4

Sequence conflict

1105

1

K → Q in BAA02185. Ref.4

Sequence conflict

1122

1

N → I in BAA02185. Ref.4

Sequence conflict

1186

1

S → T in BAA02185. Ref.4

Sequence conflict

1385

1

C → Y in CAI46013. Ref.7

Sequence conflict

1472

1

Missing in BAA02185. Ref.4

Secondary structure

1

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1600

Helix Strand Turn

Details...

Beta strand

181 – 183

3

Helix

185 – 187

3

Helix

193 – 196

4

Helix

1235 – 1257

23

Helix

1260 – 1268

9

Helix

1273 – 1275

3

Helix

1276 – 1287

12

Turn

1288 – 1290

3

Helix

1292 – 1307

16

Helix

1313 – 1330

18

Turn

1331 – 1333

3

Helix

1337 – 1345

9

Helix

1346 – 1349

4

Helix

1356 – 1363

8

Turn

1364 – 1366

3

Helix

1367 – 1370

4

Helix

1373 – 1388

16

Helix

1390 – 1399

10

Helix

1404 – 1406

3

Helix

1414 – 1420

7

Helix

1424 – 1426

3

Helix

1440 – 1453

14

Helix

1458 – 1468

11

Helix

1471 – 1474

4

Helix

1477 – 1490

14

Beta strand

1495 – 1497

3

Helix

1502 – 1515

14

Helix

1519 – 1535

17

Helix

1542 – 1552

11

Helix

1558 – 1564

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified January 16, 2004. Version 3. Checksum: 9D9B058A9939AD1E	FASTA	1,600	175,535
	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 PGASPTELGT YAGAYYPARG VQQFPTGVAP APVLMNQPPQ 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 SVAPPTIPSA 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 WKPPNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR PLDPTRLQGI 670 680 690 700 710 720 NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPQAGL GPRRSQQGPR KEPRKIIATV 730 740 750 760 770 780 LMTEDIKLNK AEKAWKPSSK RTAADKDRGE EDADGSKTQD LFRRVRSILN KLTPQMFQQL 790 800 810 820 830 840 MKQVTQLAID TEERLKGVID LIFEKAISEP NFSVAYANMC RCLMALKVPT TEKPTVTVNF 850 860 870 880 890 900 RKLLLNRCQK EFEKDKDDDE VFEKKQKEMD EAATAEERGR LKEELEEARD IARRRSLGNI 910 920 930 940 950 960 KFIGELFKLK MLTEAIMHDC VVKLLKNHDE ESLECLCRLL TTIGKDLDFE KAKPRMDQYF 970 980 990 1000 1010 1020 NQMEKIIKEK KTSSRIRFML QDVLDLRGSN WVPRRGDQGP KTIDQIHKEA EMEEHREHIK 1030 1040 1050 1060 1070 1080 VQQLMAKGSD KRRGGPPGPP ISRGLPLVDD GGWNTVPISK GSRPIDTSRL TKITKPGSID 1090 1100 1110 1120 1130 1140 SNNQLFAPGG RLSWGKGSSG GSGAKPSDAA SEAARPATST LNRFSALQQA VPTESTDNRR 1150 1160 1170 1180 1190 1200 VVQRSSLSRE RGEKAGDRGD RLERSERGGD RGDRLDRART PATKRSFSKE VEERSRERPS 1210 1220 1230 1240 1250 1260 QPEGLRKAAS LTEDRDRGRD AVKREAALPP VSPLKAALSE EELEKKSKAI IEEYLHLNDM 1270 1280 1290 1300 1310 1320 KEAVQCVQEL ASPSLLFIFV RHGVESTLER SAIAREHMGQ LLHQLLCAGH LSTAQYYQGL 1330 1340 1350 1360 1370 1380 YEILELAEDM EIDIPHVWLY LAELVTPILQ EGGVPMGELF REITKPLRPL GKAASLLLEI 1390 1400 1410 1420 1430 1440 LGLLCKSMGP KKVGTLWREA GLSWKEFLPE GQDIGAFVAE QKVEYTLGEE SEAPGQRALP 1450 1460 1470 1480 1490 1500 SEELNRQLEK LLKEGSSNQR VFDWIEANLS EQQIVSNTLV RALMTAVCYS AIIFETPLRV 1510 1520 1530 1540 1550 1560 DVAVLKARAK LLQKYLCDEQ KELQALYALQ ALVVTLEQPP NLLRMFFDAL YDEDVVKEDA 1570 1580 1590 1600 FYSWESSKDP AEQQGKGVAL KSVTAFFKWL REAEEESDHN
	Isoform B. Checksum: BE6BB32C0EAFAC58	FASTA	1,560	171,558
	10 20 30 40 50 60 MNTPSQPRQH FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ 70 80 90 100 110 120 GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTELGT YAGAYYPARG VQQFPTGVAP 130 140 150 160 170 180 APVLMNQPPQ 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 SVAPPTIPSA 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 WKPPNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV 610 620 630 640 650 660 LDKANKTPLR PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPQAGL 670 680 690 700 710 720 GPRRSQQGPR KEPRKIIATV LMTEDIKLNK AEKAWKPSSK RTAADKDRGE EDADGSKTQD 730 740 750 760 770 780 LFRRVRSILN KLTPQMFQQL MKQVTQLAID TEERLKGVID LIFEKAISEP NFSVAYANMC 790 800 810 820 830 840 RCLMALKVPT TEKPTVTVNF RKLLLNRCQK EFEKDKDDDE VFEKKQKEMD EAATAEERGR 850 860 870 880 890 900 LKEELEEARD IARRRSLGNI KFIGELFKLK MLTEAIMHDC VVKLLKNHDE ESLECLCRLL 910 920 930 940 950 960 TTIGKDLDFE KAKPRMDQYF NQMEKIIKEK KTSSRIRFML QDVLDLRGSN WVPRRGDQGP 970 980 990 1000 1010 1020 KTIDQIHKEA EMEEHREHIK VQQLMAKGSD KRRGGPPGPP ISRGLPLVDD GGWNTVPISK 1030 1040 1050 1060 1070 1080 GSRPIDTSRL TKITKPGSID SNNQLFAPGG RLSWGKGSSG GSGAKPSDAA SEAARPATST 1090 1100 1110 1120 1130 1140 LNRFSALQQA VPTESTDNRR VVQRSSLSRE RGEKAGDRGD RLERSERGGD RGDRLDRART 1150 1160 1170 1180 1190 1200 PATKRSFSKE VEERSRERPS QPEGLRKAAS LTEDRDRGRD AVKREAALPP VSPLKAALSE 1210 1220 1230 1240 1250 1260 EELEKKSKAI IEEYLHLNDM KEAVQCVQEL ASPSLLFIFV RHGVESTLER SAIAREHMGQ 1270 1280 1290 1300 1310 1320 LLHQLLCAGH LSTAQYYQGL YEILELAEDM EIDIPHVWLY LAELVTPILQ EGGVPMGELF 1330 1340 1350 1360 1370 1380 REITKPLRPL GKAASLLLEI LGLLCKSMGP KKVGTLWREA GLSWKEFLPE GQDIGAFVAE 1390 1400 1410 1420 1430 1440 QKVEYTLGEE SEAPGQRALP SEELNRQLEK LLKEGSSNQR VFDWIEANLS EQQIVSNTLV 1450 1460 1470 1480 1490 1500 RALMTAVCYS AIIFETPLRV DVAVLKARAK LLQKYLCDEQ KELQALYALQ ALVVTLEQPP 1510 1520 1530 1540 1550 1560 NLLRMFFDAL YDEDVVKEDA FYSWESSKDP AEQQGKGVAL KSVTAFFKWL REAEEESDHN
	Isoform C. Checksum: 46C0986FED5288E8	FASTA	1,513	166,663
	10 20 30 40 50 60 MMIPSQISYP ASQGAYYIPG QGRSTYVVPT QQYPVQPGAP GFYPGASPTE LGTYAGAYYP 70 80 90 100 110 120 ARGVQQFPTG VAPAPVLMNQ 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 VTASVAPPTI 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 SDQWKPPNLE EKKRYDREFL LGFQFIFASM 550 560 570 580 590 600 QKPEGLPHIS DVVLDKANKT PLRPLDPTRL QGINCGPDFT PSFANLGRTT LSTRGPPRGG 610 620 630 640 650 660 PGGELPRGPQ AGLGPRRSQQ GPRKEPRKII ATVLMTEDIK LNKAEKAWKP SSKRTAADKD 670 680 690 700 710 720 RGEEDADGSK TQDLFRRVRS ILNKLTPQMF QQLMKQVTQL AIDTEERLKG VIDLIFEKAI 730 740 750 760 770 780 SEPNFSVAYA NMCRCLMALK VPTTEKPTVT VNFRKLLLNR CQKEFEKDKD DDEVFEKKQK 790 800 810 820 830 840 EMDEAATAEE RGRLKEELEE ARDIARRRSL GNIKFIGELF KLKMLTEAIM HDCVVKLLKN 850 860 870 880 890 900 HDEESLECLC RLLTTIGKDL DFEKAKPRMD QYFNQMEKII KEKKTSSRIR FMLQDVLDLR 910 920 930 940 950 960 GSNWVPRRGD QGPKTIDQIH KEAEMEEHRE HIKVQQLMAK GSDKRRGGPP GPPISRGLPL 970 980 990 1000 1010 1020 VDDGGWNTVP ISKGSRPIDT SRLTKITKPG SIDSNNQLFA PGGRLSWGKG SSGGSGAKPS 1030 1040 1050 1060 1070 1080 DAASEAARPA TSTLNRFSAL QQAVPTESTD NRRVVQRSSL SRERGEKAGD RGDRLERSER 1090 1100 1110 1120 1130 1140 GGDRGDRLDR ARTPATKRSF SKEVEERSRE RPSQPEGLRK AASLTEDRDR GRDAVKREAA 1150 1160 1170 1180 1190 1200 LPPVSPLKAA LSEEELEKKS KAIIEEYLHL NDMKEAVQCV QELASPSLLF IFVRHGVEST 1210 1220 1230 1240 1250 1260 LERSAIAREH MGQLLHQLLC AGHLSTAQYY QGLYEILELA EDMEIDIPHV WLYLAELVTP 1270 1280 1290 1300 1310 1320 ILQEGGVPMG ELFREITKPL RPLGKAASLL LEILGLLCKS MGPKKVGTLW REAGLSWKEF 1330 1340 1350 1360 1370 1380 LPEGQDIGAF VAEQKVEYTL GEESEAPGQR ALPSEELNRQ LEKLLKEGSS NQRVFDWIEA 1390 1400 1410 1420 1430 1440 NLSEQQIVSN TLVRALMTAV CYSAIIFETP LRVDVAVLKA RAKLLQKYLC DEQKELQALY 1450 1460 1470 1480 1490 1500 ALQALVVTLE QPPNLLRMFF DALYDEDVVK EDAFYSWESS KDPAEQQGKG VALKSVTAFF 1510 KWLREAEEES DHN
	Isoform D. Checksum: 86912E3939EB8003	FASTA	1,436	158,597
	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 AKEVTASVAP 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 EYKSDQWKPP NLEEKKRYDR EFLLGFQFIF ASMQKPEGLP HISDVVLDKA 490 500 510 520 530 540 NKTPLRPLDP TRLQGINCGP DFTPSFANLG RTTLSTRGPP RGGPGGELPR GPQAGLGPRR 550 560 570 580 590 600 SQQGPRKEPR KIIATVLMTE DIKLNKAEKA WKPSSKRTAA DKDRGEEDAD GSKTQDLFRR 610 620 630 640 650 660 VRSILNKLTP QMFQQLMKQV TQLAIDTEER LKGVIDLIFE KAISEPNFSV AYANMCRCLM 670 680 690 700 710 720 ALKVPTTEKP TVTVNFRKLL LNRCQKEFEK DKDDDEVFEK KQKEMDEAAT AEERGRLKEE 730 740 750 760 770 780 LEEARDIARR RSLGNIKFIG ELFKLKMLTE AIMHDCVVKL LKNHDEESLE CLCRLLTTIG 790 800 810 820 830 840 KDLDFEKAKP RMDQYFNQME KIIKEKKTSS RIRFMLQDVL DLRGSNWVPR RGDQGPKTID 850 860 870 880 890 900 QIHKEAEMEE HREHIKVQQL MAKGSDKRRG GPPGPPISRG LPLVDDGGWN TVPISKGSRP 910 920 930 940 950 960 IDTSRLTKIT KPGSIDSNNQ LFAPGGRLSW GKGSSGGSGA KPSDAASEAA RPATSTLNRF 970 980 990 1000 1010 1020 SALQQAVPTE STDNRRVVQR SSLSRERGEK AGDRGDRLER SERGGDRGDR LDRARTPATK 1030 1040 1050 1060 1070 1080 RSFSKEVEER SRERPSQPEG LRKAASLTED RDRGRDAVKR EAALPPVSPL KAALSEEELE 1090 1100 1110 1120 1130 1140 KKSKAIIEEY LHLNDMKEAV QCVQELASPS LLFIFVRHGV ESTLERSAIA REHMGQLLHQ 1150 1160 1170 1180 1190 1200 LLCAGHLSTA QYYQGLYEIL ELAEDMEIDI PHVWLYLAEL VTPILQEGGV PMGELFREIT 1210 1220 1230 1240 1250 1260 KPLRPLGKAA SLLLEILGLL CKSMGPKKVG TLWREAGLSW KEFLPEGQDI GAFVAEQKVE 1270 1280 1290 1300 1310 1320 YTLGEESEAP GQRALPSEEL NRQLEKLLKE GSSNQRVFDW IEANLSEQQI VSNTLVRALM 1330 1340 1350 1360 1370 1380 TAVCYSAIIF ETPLRVDVAV LKARAKLLQK YLCDEQKELQ ALYALQALVV TLEQPPNLLR 1390 1400 1410 1420 1430 MFFDALYDED VVKEDAFYSW ESSKDPAEQQ GKGVALKSVT AFFKWLREAE EESDHN
	Isoform E. Checksum: 9DC0C302B31831AD	FASTA	1,404	154,885
	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 EVTASVAPPT 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 KSDQWKPPNL EEKKRYDREF 430 440 450 460 470 480 LLGFQFIFAS MQKPEGLPHI SDVVLDKANK TPLRPLDPTR LQGINCGPDF TPSFANLGRT 490 500 510 520 530 540 TLSTRGPPRG GPGGELPRGP QAGLGPRRSQ QGPRKEPRKI IATVLMTEDI KLNKAEKAWK 550 560 570 580 590 600 PSSKRTAADK DRGEEDADGS KTQDLFRRVR SILNKLTPQM FQQLMKQVTQ LAIDTEERLK 610 620 630 640 650 660 GVIDLIFEKA ISEPNFSVAY ANMCRCLMAL KVPTTEKPTV TVNFRKLLLN RCQKEFEKDK 670 680 690 700 710 720 DDDEVFEKKQ KEMDEAATAE ERGRLKEELE EARDIARRRS LGNIKFIGEL FKLKMLTEAI 730 740 750 760 770 780 MHDCVVKLLK NHDEESLECL CRLLTTIGKD LDFEKAKPRM DQYFNQMEKI IKEKKTSSRI 790 800 810 820 830 840 RFMLQDVLDL RGSNWVPRRG DQGPKTIDQI HKEAEMEEHR EHIKVQQLMA KGSDKRRGGP 850 860 870 880 890 900 PGPPISRGLP LVDDGGWNTV PISKGSRPID TSRLTKITKP GSIDSNNQLF APGGRLSWGK 910 920 930 940 950 960 GSSGGSGAKP SDAASEAARP ATSTLNRFSA LQQAVPTEST DNRRVVQRSS LSRERGEKAG 970 980 990 1000 1010 1020 DRGDRLERSE RGGDRGDRLD RARTPATKRS FSKEVEERSR ERPSQPEGLR KAASLTEDRD 1030 1040 1050 1060 1070 1080 RGRDAVKREA ALPPVSPLKA ALSEEELEKK SKAIIEEYLH LNDMKEAVQC VQELASPSLL 1090 1100 1110 1120 1130 1140 FIFVRHGVES TLERSAIARE HMGQLLHQLL CAGHLSTAQY YQGLYEILEL AEDMEIDIPH 1150 1160 1170 1180 1190 1200 VWLYLAELVT PILQEGGVPM GELFREITKP LRPLGKAASL LLEILGLLCK SMGPKKVGTL 1210 1220 1230 1240 1250 1260 WREAGLSWKE FLPEGQDIGA FVAEQKVEYT LGEESEAPGQ RALPSEELNR QLEKLLKEGS 1270 1280 1290 1300 1310 1320 SNQRVFDWIE ANLSEQQIVS NTLVRALMTA VCYSAIIFET PLRVDVAVLK ARAKLLQKYL 1330 1340 1350 1360 1370 1380 CDEQKELQAL YALQALVVTL EQPPNLLRMF FDALYDEDVV KEDAFYSWES SKDPAEQQGK 1390 1400 GVALKSVTAF FKWLREAEEE SDHN

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, MUTAGENESIS OF LEU-769; LEU-772; PHE-777; 843-LEU-LEU-844; 852-PHE-GLU-852; LEU-897; ILE-903; LEU-906; ARG-975; PHE-978; LEU-986 AND TRP-991.
[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), 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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder 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). Tissue: Endometrial tumor.
[8]	"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, INTERACTION WITH ROTAVIRAL NSP3.
[9]	"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 605-722, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
[10]	De Gregorio E. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 682-913.
[11]	"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: 8396129] [Abstract] Cited for: CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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-1210 AND SER-1232, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"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.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1146; SER-1148; SER-1186 AND SER-1232, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232, MASS SPECTROMETRY. Tissue: Epithelium.
[26]	"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-1093 AND SER-1232, MASS SPECTROMETRY. Tissue: Epithelium.
[27]	"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-1210, MASS SPECTROMETRY.
[28]	"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-1232, MASS SPECTROMETRY.
[29]	"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-1210, MASS SPECTROMETRY. 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: 18799579] [Abstract] Cited for: INTERACTION WITH ROTAVIRUS A NSP3.
[31]	"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-1232, MASS SPECTROMETRY.
[32]	"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.
[33]	"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-1093; SER-1186; SER-1188; SER-1210; SER-1232 AND SER-1597, MASS SPECTROMETRY.
[34]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[35]	"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.
[36]	"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 1235-1572.
[37]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AF002816 mRNA. Translation: AAC78443.1.
AF004836 Genomic DNA. Translation: AAC78444.1. Different initiation.
AJ001046 mRNA. Translation: CAA04500.1.

IPI

IPI00479262.
IPI00552639.
IPI00759560.
IPI00927510.
IPI00927765.

PIR

A44453.

RefSeq

NP_937884.1.

UniGene

Hs.433750

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LJ2	X-ray	2.38	C/D	172-199	[»]
1UG3	X-ray	2.24	A/B	1235-1572	[»]

SMR

Q04637. Positions 752-992.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1161N.

IntAct

Q04637. 32 interactions.

PTM databases

PhosphoSite

Q04637.

Proteomic databases

PRIDE

Q04637.

Genome annotation databases

Ensembl

ENSG00000114867. Homo sapiens. [Contig view]

GeneID

1981.

Organism-specific databases

GeneCards

GC03P185515.

H-InvDB

HIX0003910.

HGNC

HGNC:3296. EIF4G1.

HPA

CAB014774.

MIM

600495. gene.

PharmGKB

PA27722.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q04637.

Enzyme and pathway databases

Pathway_Interaction_DB

mtor_4pathway. mTOR signaling pathway.

Reactome

REACT_1762. 3' -UTR-mediated translational regulation.
REACT_498. Signaling by Insulin receptor.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q04637.

Bgee

Q04637.

CleanEx

HS_EIF4G1.

GermOnline

ENSG00000114867. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

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

Pfam

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

SMART

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

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

8013.

PMAP-CutDB

Q04637.

SOURCE

Search...

Entry information

Entry name

IF4G1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 16, 2004
Last modified:	June 16, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)