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Reviewed, UniProtKB/Swiss-Prot Q04637 (IF4G1_HUMAN)

Last modified June 16, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16001600Eukaryotic translation initiation factor 4 gamma 1
PRO_0000007786

Regions

Domain565 – 792228MIF4G
Domain1242 – 1364123MI
Domain1434 – 1600167W2
Region172 – 20029PABPC1-binding
Region607 – 61812EIF4E-binding
Region682 – 1086405eIF3/EIF4A-binding
Region1451 – 1600150EIF4A-binding
Region1586 – 160015Necessary but not sufficient for MKNK1-binding
Compositional bias454 – 46714Poly-Glu
Compositional bias501 – 5044Poly-Ala

Sites

Site674 – 6752Cleavage; by foot-and-mouth disease virus leader protease
Site681 – 6822Cleavage; by enterovirus/rhinovirus protease 2A

Amino acid modifications

Modified residue2051Phosphothreonine Ref.33
Modified residue2071Phosphothreonine Ref.33
Modified residue2231Phosphothreonine Ref.33
Modified residue5941Phosphotyrosine Ref.23
Modified residue6471Phosphothreonine Ref.33
Modified residue10931Phosphoserine Ref.26 Ref.33
Modified residue11461Phosphoserine Ref.24
Modified residue11481Phosphoserine Ref.24
Modified residue11861Phosphoserine Ref.24 Ref.33
Modified residue11881Phosphoserine Ref.33
Modified residue12101Phosphoserine Ref.22 Ref.27 Ref.29 Ref.33
Modified residue12321Phosphoserine Ref.22 Ref.24 Ref.25 Ref.26 Ref.28 Ref.31 Ref.33
Modified residue15971Phosphoserine Ref.33

Natural variations

Alternative sequence1 – 196196Missing in isoform E.
VSP_018723
Alternative sequence1 – 164164Missing in isoform D.
VSP_018722
Alternative sequence1 – 8787Missing in isoform C.
VSP_018721
Alternative sequence1 – 4040Missing in isoform B.
VSP_018720
Natural variant3111Y → C: dbSNP rs16858632.
VAR_055704
Natural variant6961P → L in a colorectal cancer sample; somatic mutation. Ref.37
VAR_036117
Natural variant12341L → P: dbSNP rs2230570.
VAR_055705

Experimental info

Mutagenesis174 – 1785KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. Ref.18
Mutagenesis1801I → A: Loss of PABPC1 binding. Ref.35
Mutagenesis1821I → A: Loss of PABPC1 binding. Ref.35
Mutagenesis184 – 1874DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178.
Mutagenesis1921I → A: Loss of PABPC1 binding. Ref.35
Mutagenesis1961I → A: Loss of PABPC1 binding. Ref.35
Mutagenesis6121Y → A or F: Abolishes binding to EIF4E. Ref.9
Mutagenesis617 – 6182LL → AA: Abolishes binding to EIF4E.
Mutagenesis6821G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. Ref.14
Mutagenesis7691L → A: Abolishes binding to EIF4A; when associated with A-772 and A-777. Ref.2
Mutagenesis7721L → A: Abolishes binding to EIF4A; when associated with A-769 and A-777. Ref.2
Mutagenesis7771F → A: Abolishes binding to EIF4A; when associated with A-769 and A-772. Ref.2
Mutagenesis843 – 8442LL → AA: Abolishes binding to EIF4A; when associated with A-852 and K-853.
Mutagenesis852 – 8532FE → AK: Abolishes binding to EIF4A; when associated with A-843 and A-844.
Mutagenesis8971L → A: Abolishes binding to EIF4A; when associated with A-903 and A-906. Ref.2
Mutagenesis9031I → A: Abolishes binding to EIF4A; when associated with A-897 and A-906. Ref.2
Mutagenesis9061L → A: Abolishes binding to EIF4A; when associated with A-897 and A-903. Ref.2
Mutagenesis9751R → A: Abolishes binding to EIF4A; when associated with A-978. Ref.2
Mutagenesis9781F → A: Abolishes binding to EIF4A; when associated with A-975. Ref.2
Mutagenesis9861L → A: Slightly reduced binding to EIF4A; when associated with A-991. Ref.2
Mutagenesis9911W → A: Slightly reduced binding to EIF4A; when associated with A-986. Ref.2
Sequence conflict301P → R in AAC78443. Ref.8
Sequence conflict1381L → F Ref.3
Sequence conflict1381L → F Ref.7
Sequence conflict1381L → F in AAC78443. Ref.8
Sequence conflict1491R → Q Ref.3
Sequence conflict1491R → Q Ref.7
Sequence conflict1491R → Q in AAC78443. Ref.8
Sequence conflict2141G → S in BAA02185. Ref.4
Sequence conflict4321V → M in CAI46013. Ref.7
Sequence conflict4621E → D in BAA02185. Ref.4
Sequence conflict4681A → V in BAA02185. Ref.4
Sequence conflict4741A → G in BAA02185. Ref.4
Sequence conflict4791G → R in BAA02185. Ref.4
Sequence conflict6041P → L in CAI46013. Ref.7
Sequence conflict625 – 6262AS → CQ in BAA02185. Ref.4
Sequence conflict6971Missing Ref.4
Sequence conflict6971Missing Ref.7
Sequence conflict7651V → W in BAA02185. Ref.4
Sequence conflict8791G → E in BAA02185. Ref.4
Sequence conflict8951R → C in BAA02185. Ref.4
Sequence conflict11051K → Q in BAA02185. Ref.4
Sequence conflict11221N → I in BAA02185. Ref.4
Sequence conflict11861S → T in BAA02185. Ref.4
Sequence conflict13851C → Y in CAI46013. Ref.7
Sequence conflict14721Missing in BAA02185. Ref.4

Secondary structure

....................................................... 1600
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified January 16, 2004. Version 3.
Checksum: 9D9B058A9939AD1E

FASTA1,600175,535
        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 

« Hide

Isoform B.

Checksum: BE6BB32C0EAFAC58
Show »

FASTA1,560171,558
Isoform C.

Checksum: 46C0986FED5288E8
Show »

FASTA1,513166,663
Isoform D.

Checksum: 86912E3939EB8003
Show »

FASTA1,436158,597
Isoform E.

Checksum: 9DC0C302B31831AD
Show »

FASTA1,404154,885

References

« Hide 'large scale' references
[1]"Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma."
Yan R., Rychlik W., Etchison D., Rhoads R.E.
J. Biol. Chem. 267:23226-23231(1992) [PubMed: 1429670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E).
Tissue: Brain.
[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. expand/collapse author list , 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. expand/collapse author list , 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

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.
IPIIPI00479262.
IPI00552639.
IPI00759560.
IPI00927510.
IPI00927765.
PIRA44453.
RefSeqNP_937884.1.
UniGeneHs.433750

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LJ2X-ray2.38C/D172-199[»]
1UG3X-ray2.24A/B1235-1572[»]
SMRQ04637. Positions 752-992.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1161N.
IntActQ04637. 32 interactions.

PTM databases

PhosphoSiteQ04637.

Proteomic databases

PRIDEQ04637.

Genome annotation databases

EnsemblENSG00000114867. Homo sapiens. [Contig view]
GeneID1981.

Organism-specific databases

GeneCardsGC03P185515.
H-InvDBHIX0003910.
HGNCHGNC:3296. EIF4G1.
HPACAB014774.
MIM600495. gene.
PharmGKBPA27722.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ04637.

Enzyme and pathway databases

Pathway_Interaction_DBmtor_4pathway. mTOR signaling pathway.
ReactomeREACT_1762. 3' -UTR-mediated translational regulation.
REACT_498. Signaling by Insulin receptor.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ04637.
BgeeQ04637.
CleanExHS_EIF4G1.
GermOnlineENSG00000114867. Homo sapiens.

Family and domain databases

InterProIPR003307. eIF5C.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
Gene3DG3DSA:1.25.40.230. eIF5C. 1 hit.
G3DSA:1.25.40.180. MIF4-like_typ_1/2/3. 1 hit.
PfamPF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTSM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
PROSITEPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8013.
PMAP-CutDBQ04637.
SOURCESearch...

Entry information

Entry nameIF4G1_HUMAN
AccessionPrimary (citable) accession number: Q04637
Secondary accession number(s): O43177 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Translation initiation factors

List of translation initiation factor entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents