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Q04637 (IF4G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1599 AA.
Sequence statusComplete.
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 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.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21 Ref.23 Ref.26 Ref.28 Ref.30 Ref.31 Ref.42

Post-translational modification

Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1. Ref.39

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

Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.45

Sequence similarities

Belongs to the eukaryotic initiation factor 4G 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. Translation N-terminally extended.

The sequence AAC82471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 processHost-virus interaction
Protein biosynthesis
Translation regulation
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Parkinson disease
Parkinsonism
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

regulation of translational initiation

Inferred from mutant phenotype PubMed 19648179. Source: UniProtKB

response to ethanol

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic translation initiation factor 4F complex

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functiontranslation initiation factor activity

Traceable author statement Ref.16Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 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.
Isoform 7 (identifier: Q04637-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.
     696-696: P → PQ
Note: Produced by alternative splicing.
Isoform 8 (identifier: Q04637-8)

The sequence of this isoform differs from the canonical sequence as follows:
     696-696: P → PQ
Note: Produced by alternative splicing.
Isoform 9 (identifier: Q04637-9)

The sequence of this isoform differs from the canonical sequence as follows:
     48-48: R → RQGGFRSL
Note: Produced by alternative splicing. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15991599Eukaryotic translation initiation factor 4 gamma 1
PRO_0000007786

Regions

Domain565 – 792228MIF4G
Domain1241 – 1363123MI
Domain1433 – 1599167W2
Region172 – 20029PABPC1-binding
Region607 – 61812EIF4E-binding
Region682 – 1085404eIF3/EIF4A-binding
Region1450 – 1599150EIF4A-binding
Region1585 – 159915Necessary 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 residue2071Phosphothreonine Ref.32
Modified residue2231Phosphothreonine Ref.32
Modified residue6021N6-acetyllysine By similarity
Modified residue6471Phosphothreonine Ref.32
Modified residue10281Phosphoserine Ref.37 Ref.40
Modified residue10921Phosphoserine Ref.27 Ref.32 Ref.37 Ref.40
Modified residue10951N6-acetyllysine Ref.36
Modified residue11451Phosphoserine Ref.40
Modified residue11471Phosphoserine Ref.40
Modified residue11851Phosphoserine; by PKC/PRKCA Ref.37 Ref.39 Ref.40
Modified residue11871Phosphoserine Ref.37 Ref.40
Modified residue12091Phosphoserine Ref.32 Ref.37 Ref.40
Modified residue12111Phosphothreonine Ref.37 Ref.40
Modified residue12311Phosphoserine Ref.24 Ref.25 Ref.37 Ref.40
Modified residue15961Phosphoserine Ref.37 Ref.40

Natural variations

Alternative sequence1 – 196196Missing in isoform E and isoform 7.
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
Alternative sequence481R → RQGGFRSL in isoform 9.
VSP_047396
Alternative sequence6961P → PQ in isoform 7 and isoform 8.
VSP_047397
Natural variant711P → S. Ref.45
Corresponds to variant rs113810947 [ dbSNP | Ensembl ].
VAR_066571
Natural variant1611T → A. Ref.4 Ref.6 Ref.9 Ref.10 Ref.45
Corresponds to variant rs13319149 [ dbSNP | Ensembl ].
VAR_061147
Natural variant3111Y → C. Ref.45
Corresponds to variant rs16858632 [ dbSNP | Ensembl ].
VAR_055704
Natural variant4321M → V. Ref.1 Ref.4 Ref.10 Ref.45
Corresponds to variant rs2178403 [ dbSNP | Ensembl ].
VAR_063040
Natural variant466 – 4683Missing.
VAR_066572
Natural variant5021A → V in PARK18. Ref.45
Corresponds to variant rs111290936 [ dbSNP | Ensembl ].
VAR_066573
Natural variant6861G → C Found in patients with Parkinson disease. Ref.45
Corresponds to variant rs112019125 [ dbSNP | Ensembl ].
VAR_066574
Natural variant6961P → L in a colorectal cancer sample; somatic mutation. Ref.44
VAR_036117
Natural variant8061I → V. Ref.45
Corresponds to variant rs62287499 [ dbSNP | Ensembl ].
VAR_066575
Natural variant8291T → S. Ref.45
Corresponds to variant rs111500185 [ dbSNP | Ensembl ].
VAR_066576
Natural variant11641S → R Found in a patient with Parkinson disease. Ref.45
Corresponds to variant rs113169049 [ dbSNP | Ensembl ].
VAR_066577
Natural variant11971R → W Found in a patient with Parkinson disease. Ref.45
Corresponds to variant rs113388242 [ dbSNP | Ensembl ].
VAR_066578
Natural variant12051R → H in PARK18. Ref.45
Corresponds to variant rs112176450 [ dbSNP | Ensembl ].
VAR_066579
Natural variant12291P → A. Ref.45
Corresponds to variant rs35629949 [ dbSNP | Ensembl ].
VAR_061148
Natural variant12331L → P. Ref.45
Corresponds to variant rs2230570 [ dbSNP | Ensembl ].
VAR_055705
Natural variant12571N → S. Ref.45
Corresponds to variant rs73053766 [ dbSNP | Ensembl ].
VAR_066580

Experimental info

Mutagenesis174 – 1785KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. Ref.20
Mutagenesis1801I → A: Loss of PABPC1 binding. Ref.42
Mutagenesis1821I → A: Loss of PABPC1 binding. Ref.42
Mutagenesis184 – 1874DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178.
Mutagenesis1921I → A: Loss of PABPC1 binding. Ref.42
Mutagenesis1961I → A: Loss of PABPC1 binding. Ref.42
Mutagenesis6121Y → A or F: Abolishes binding to EIF4E. Ref.11
Mutagenesis617 – 6182LL → AA: Abolishes binding to EIF4E.
Mutagenesis6821G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. Ref.16
Mutagenesis7681L → A: Abolishes binding to EIF4A; when associated with A-770 and A-775. Ref.10
Mutagenesis7711L → A: Abolishes binding to EIF4A; when associated with A-767 and A-775. Ref.10
Mutagenesis7761F → A: Abolishes binding to EIF4A; when associated with A-767 and A-770. Ref.10
Mutagenesis842 – 8432LL → AA: Abolishes binding to EIF4A; when associated with A-850 and K-851.
Mutagenesis851 – 8522FE → AK: Abolishes binding to EIF4A; when associated with A-841 and A-842.
Mutagenesis8961L → A: Abolishes binding to EIF4A; when associated with A-92 and A-95. Ref.10
Mutagenesis9021I → A: Abolishes binding to EIF4A; when associated with A-895 and A-95. Ref.10
Mutagenesis9051L → A: Abolishes binding to EIF4A; when associated with A-895 and A-92. Ref.10
Mutagenesis9741R → A: Abolishes binding to EIF4A; when associated with A-976. Ref.10
Mutagenesis9771F → A: Abolishes binding to EIF4A; when associated with A-973. Ref.10
Mutagenesis9851L → A: Slightly reduced binding to EIF4A; when associated with A-989. Ref.10
Mutagenesis9901W → A: Slightly reduced binding to EIF4A; when associated with A-984. Ref.10
Sequence conflict301P → R in AAC78443. Ref.9
Sequence conflict1381F → L in AAL92872. Ref.5
Sequence conflict1381F → L in AAM69365. Ref.5
Sequence conflict1491Q → R in AAL92872. Ref.5
Sequence conflict1491Q → R in AAM69365. Ref.5
Sequence conflict2141G → S in BAA02185. Ref.1
Sequence conflict4621E → D in BAA02185. Ref.1
Sequence conflict4681A → V in BAA02185. Ref.1
Sequence conflict4741A → G in BAA02185. Ref.1
Sequence conflict4791G → R in BAA02185. Ref.1
Sequence conflict6041L → P in BAA02185. Ref.1
Sequence conflict6041L → P in AAL92872. Ref.5
Sequence conflict6041L → P in AAM69365. Ref.5
Sequence conflict6041L → P in AAC82471. Ref.10
Sequence conflict625 – 6262AS → CQ in BAA02185. Ref.1
Sequence conflict6931P → A in BAA02185. Ref.1
Sequence conflict6961P → A in BAA02185. Ref.1
Sequence conflict7641V → W in BAA02185. Ref.1
Sequence conflict8781G → E in BAA02185. Ref.1
Sequence conflict8941R → C in BAA02185. Ref.1
Sequence conflict11041K → Q in BAA02185. Ref.1
Sequence conflict11211N → I in BAA02185. Ref.1
Sequence conflict11851S → T in BAA02185. Ref.1
Sequence conflict13841C → Y in CAI46013. Ref.6
Sequence conflict14721Missing in BAA02185. Ref.1

Secondary structure

......................................................... 1599
Helix Strand Turn

Details...

Sequences

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

Last modified April 20, 2010. Version 4.
Checksum: 324088B60863DA34

FASTA1,599175,491
        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 

« Hide

Isoform B [UniParc].

Checksum: 22F62E219E629C0E
Show »

FASTA1,559171,514
Isoform C [UniParc].

Checksum: 09DD6DC263462CB6
Show »

FASTA1,512166,619
Isoform D [UniParc].

Checksum: 6F7E9DE4106E73B9
Show »

FASTA1,435158,517
Isoform E [UniParc].

Checksum: 3E93A66EE3DFDDA9
Show »

FASTA1,403154,805
Isoform 7 [UniParc].

Checksum: E2CE3C54B5BB0A50
Show »

FASTA1,404154,933
Isoform 8 [UniParc].

Checksum: 2B32EF7A6D50B657
Show »

FASTA1,600175,619
Isoform 9 [UniParc].

Checksum: E4464821E0BA5FF6
Show »

FASTA1,606176,237

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), VARIANT VAL-432.
Tissue: Brain.
[2]"A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation."
Imataka H., Gradi A., Sonenberg N.
EMBO J. 17:7480-7489(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PABPC1.
[3]"A novel functional human eukaryotic translation initiation factor 4G."
Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N.
Mol. Cell. Biol. 18:334-342(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
[4]"Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons."
Byrd M.P., Zamora M., Lloyd R.E.
Mol. Cell. Biol. 22:4499-4511(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), VARIANTS ALA-161 AND VAL-432, ALTERNATIVE INITIATION.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ALA-161.
Tissue: Endometrial tumor.
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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].
[9]"Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts the poly(A) binding protein from eIF4F."
Piron M., Vende P., Cohen J., Poncet D.
EMBO J. 17:5811-5821(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-234, VARIANT ALA-161, INTERACTION WITH ROTAVIRAL NSP3.
[10]"Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A."
Imataka H., Sonenberg N.
Mol. Cell. Biol. 17:6940-6947(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH EIF4A, VARIANTS ALA-161 AND VAL-432, MUTAGENESIS OF LEU-768; LEU-771; PHE-776; 842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902; LEU-905; ARG-974; PHE-977; LEU-985 AND TRP-990.
[11]"The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins."
Mader S., Lee H., Pause A., Sonenberg N.
Mol. Cell. Biol. 15:4990-4997(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
[12]De Gregorio E.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 682-912 (ISOFORM 8).
[13]"Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus."
Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H., Kuechler E., Skern T., Rhoads R.E.
J. Biol. Chem. 268:19200-19203(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
[14]"Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function."
Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., Lawrence J.C. Jr., Sonenberg N.
Nature 371:762-767(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4E.
Tissue: Placenta.
[15]"Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
Haghighat A., Mader S., Pause A., Sonenberg N.
EMBO J. 14:5701-5709(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4E AND EIF4EBP1.
[16]"A single amino acid change in protein synthesis initiation factor 4G renders cap-dependent translation resistant to picornaviral 2A proteases."
Lamphear B.J., Rhoads R.E.
Biochemistry 35:15726-15733(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-682.
[17]"Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."
Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.
FEBS Lett. 435:79-83(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY POLIOVIRUS.
[18]"eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation."
Gingras A.-C., Raught B., Sonenberg N.
Annu. Rev. Biochem. 68:913-963(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[19]"Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKNK1.
[20]"Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation."
Wakiyama M., Imataka H., Sonenberg N.
Curr. Biol. 10:1147-1150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1, MUTAGENESIS OF 174-LYS--LYS-178 AND 184-ASP--GLN-197.
[21]"Multiple portions of poly(A)-binding protein stimulate translation in vivo."
Gray N.K., Coller J.M., Dickson K.S., Wickens M.
EMBO J. 19:4723-4733(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1.
[22]"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
Glaser W., Skern T.
FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY FMDV AND HRV-2.
[23]"The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MKNK2.
[24]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Post-transcriptional regulation of thioredoxin by the stress inducible heterogeneous ribonucleoprotein A18."
Yang R., Weber D.J., Carrier F.
Nucleic Acids Res. 34:1224-1236(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIRBP.
[27]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
Lin J.C., Hsu M., Tarn W.Y.
Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBM4.
[29]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[30]"Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROTAVIRUS A NSP3.
[31]"SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIF4GD.
[32]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-223; THR-647; SER-1092 AND SER-1209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[33]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1."
Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.
Mol. Cell. Biol. 31:2947-2959(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1185.
[40]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092; SER-1145; SER-1147; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."
Groft C.M., Burley S.K.
Mol. Cell 9:1273-1283(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH ROTAVIRAL NSP3, INTERACTION WITH PABPC1, MUTAGENESIS OF ILE-180; ILE-182; ILE-192 AND ILE-196.
[43]"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1."
Bellsolell L., Cho-Park P.F., Poulin F., Sonenberg N., Burley S.K.
Structure 14:913-923(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571.
[44]"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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-696.
[45]"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. expand/collapse author list , Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.
Am. J. Hum. Genet. 89:398-406(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PARK18 VAL-502 AND HIS-1205, VARIANTS SER-71; ALA-161; CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829; ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D12686 mRNA. Translation: BAA02185.1. Frameshift.
AY082886 mRNA. Translation: AAL92872.1.
AF281070 mRNA. Translation: AAM69365.1.
AK131407 mRNA. Translation: BAD18554.1. Sequence problems.
BX647812 mRNA. Translation: CAI46013.1.
AC078797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78257.1.
CH471052 Genomic DNA. Translation: EAW78259.1.
CH471052 Genomic DNA. Translation: EAW78262.1.
CH471052 Genomic DNA. Translation: EAW78263.1.
CH471052 Genomic DNA. Translation: EAW78264.1.
CH471052 Genomic DNA. Translation: EAW78265.1.
CH471052 Genomic DNA. Translation: EAW78266.1.
CH471052 Genomic DNA. Translation: EAW78267.1.
AF002816 mRNA. Translation: AAC78443.1.
AF004836 Genomic DNA. Translation: AAC78444.1. Different initiation.
AF104913 mRNA. Translation: AAC82471.1. Different initiation.
AJ001046 mRNA. Translation: CAA04500.1.
PIRA44453.
RefSeqNP_004944.3. NM_004953.4.
NP_886553.3. NM_182917.4.
NP_937884.1. NM_198241.2.
NP_937885.1. NM_198242.2.
XP_005247244.1. XM_005247187.1.
XP_005247245.1. XM_005247188.1.
XP_005247249.1. XM_005247192.1.
XP_005247253.1. XM_005247196.1.
XP_005247254.1. XM_005247197.1.
UniGeneHs.433750.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LJ2X-ray2.38C/D172-199[»]
1UG3X-ray2.24A/B1234-1571[»]
2W97X-ray2.29E/F609-622[»]
4F02X-ray2.00C/F178-203[»]
DisProtDP00406.
ProteinModelPortalQ04637.
SMRQ04637. Positions 173-199, 751-991, 1234-1592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108296. 59 interactions.
DIPDIP-1161N.
IntActQ04637. 30 interactions.
MINTMINT-135718.
STRING9606.ENSP00000316879.

Chemistry

BindingDBQ04637.

PTM databases

PhosphoSiteQ04637.

Polymorphism databases

DMDM294862538.

Proteomic databases

PaxDbQ04637.
PRIDEQ04637.

Protocols and materials databases

DNASU1981.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319274; ENSP00000323737; ENSG00000114867. [Q04637-1]
ENST00000342981; ENSP00000343450; ENSG00000114867. [Q04637-8]
ENST00000346169; ENSP00000316879; ENSG00000114867. [Q04637-1]
ENST00000350481; ENSP00000317600; ENSG00000114867. [Q04637-5]
ENST00000352767; ENSP00000338020; ENSG00000114867. [Q04637-9]
ENST00000382330; ENSP00000371767; ENSG00000114867. [Q04637-9]
ENST00000392537; ENSP00000376320; ENSG00000114867. [Q04637-4]
ENST00000414031; ENSP00000391935; ENSG00000114867. [Q04637-3]
ENST00000424196; ENSP00000416255; ENSG00000114867. [Q04637-9]
ENST00000434061; ENSP00000411826; ENSG00000114867. [Q04637-7]
ENST00000435046; ENSP00000404754; ENSG00000114867. [Q04637-6]
GeneID1981.
KEGGhsa:1981.
UCSCuc003fnp.3. human. [Q04637-1]

Organism-specific databases

CTD1981.
GeneCardsGC03P184032.
HGNCHGNC:3296. EIF4G1.
HPACAB014774.
HPA028487.
HPA043866.
MIM600495. gene.
614251. phenotype.
neXtProtNX_Q04637.
Orphanet2828. Young adult-onset Parkinsonism.
PharmGKBPA27722.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG301289.
HOVERGENHBG052083.
KOK03260.
OMAGSNWVPR.
OrthoDBEOG7D59N2.
TreeFamTF101527.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ04637.
BgeeQ04637.
CleanExHS_EIF4G1.
GenevestigatorQ04637.

Family and domain databases

Gene3D1.25.40.180. 3 hits.
InterProIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
IPR003307. W2_domain.
[Graphical view]
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]
SUPFAMSSF48371. SSF48371. 3 hits.
PROSITEPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4G1. human.
EvolutionaryTraceQ04637.
GeneWikiEukaryotic_translation_initiation_factor_4_gamma.
GenomeRNAi1981.
NextBio35489794.
PMAP-CutDBQ04637.
PROQ04637.
SOURCESearch...

Entry information

Entry nameIF4G1_HUMAN
AccessionPrimary (citable) accession number: Q04637
Secondary accession number(s): D3DNT2 expand/collapse secondary AC list , D3DNT4, D3DNT5, E9PFM1, G5E9S1, O43177, O95066, Q5HYG0, Q6ZN21, Q8N102
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 20, 2010
Last modified: March 19, 2014
This is version 159 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

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