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Q6NZJ6 (IF4G1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:Eif4g1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1600 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 By similarity.

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. Interacts with CIRBP and MIF4GD. Interacts with RBM4 By similarity. Interacts with EIF4E3. Ref.3

Post-translational modification

Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1187 by PRKCA induces binding to MKNK1 By similarity.

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 1 MI domain.

Contains 1 MIF4G domain.

Contains 1 W2 domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
Translation regulation
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Inferred from electronic annotation. Source: InterPro

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12388085. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6NZJ6-1)

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 2 (identifier: Q6NZJ6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     49-55: Missing.
     1046-1052: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16001600Eukaryotic translation initiation factor 4 gamma 1
PRO_0000213322

Regions

Domain765 – 993229MIF4G
Domain1241 – 1363123MI
Domain1429 – 1599171W2
Region179 – 20729PABPC1-binding By similarity
Region611 – 62212EIF4E-binding By similarity
Region686 – 1089404eIF3/EIF4A-binding By similarity
Region1450 – 1600151EIF4A-binding By similarity
Region1585 – 160016Necessary but not sufficient for MKNK1-binding By similarity
Compositional bias464 – 48724Asp/Glu-rich

Amino acid modifications

Modified residue2121Phosphothreonine Ref.4
Modified residue2141Phosphothreonine Ref.4
Modified residue6511Phosphothreonine By similarity
Modified residue10321Phosphoserine By similarity
Modified residue10961Phosphoserine By similarity
Modified residue10991N6-acetyllysine By similarity
Modified residue11471Phosphoserine By similarity
Modified residue11491Phosphoserine By similarity
Modified residue11871Phosphoserine; by PKC/PRKCA By similarity
Modified residue11891Phosphoserine By similarity
Modified residue12111Phosphoserine Ref.4 Ref.5
Modified residue12131Phosphothreonine By similarity
Modified residue12311Phosphoserine Ref.6 Ref.7 Ref.8
Modified residue15971Phosphoserine Ref.7 Ref.8

Natural variations

Alternative sequence49 – 557Missing in isoform 2.
VSP_013974
Alternative sequence1046 – 10527Missing in isoform 2.
VSP_013975

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 8664A8B449C7A128

FASTA1,600176,077
        10         20         30         40         50         60 
MNKAPQPTGP PPARSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQG GFRSLQHFYP 

        70         80         90        100        110        120 
SRAQPPSSAA SRVQSAAPAR PGPAPHVYPA GSQVMMIPSQ ISYSASQGAY YIPGQGRSTY 

       130        140        150        160        170        180 
VVPTQQYPVQ PGAPGFYPGA SPTEFGTYAG AYYPAQGVQQ FPASVAPAPV LMNQPPQIAP 

       190        200        210        220        230        240 
KRERKTIRIR DPNQGGKDIT EEIMSGARTA STPTPPQTGG SLEPQPNGES PQVAVIIRPD 

       250        260        270        280        290        300 
DRSQGAAIGG RPGLPGPEHS PGTESQPSSP SPTPSPPPIL EPGSESNLGV LSIPGDTMTT 

       310        320        330        340        350        360 
GMIPMSVEES TPISCETGEP YCLSPEPTLA EPILEVEVTL SKPIPESEFS SSPLQVSTAL 

       370        380        390        400        410        420 
VPHKVETHEP NGVIPSEDLE PEVESSTEPA PPPLSPCASE SLVPIAPTAQ PEELLNGAPS 

       430        440        450        460        470        480 
PPAVDLSPVS EPEEQAKKVS SAALASILSP APPVAPSDTS PAQEEEMEED DDDEEGGEAE 

       490        500        510        520        530        540 
SEKGGEDVPL DSTPVPAQLS QNLEVAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE 

       550        560        570        580        590        600 
VDPAVPEVEN QPPTGSNPSP ESEGSMVPTQ PEETEETWDS KEDKIHNAEN IQPGEQKYEY 

       610        620        630        640        650        660 
KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI TDVVLDKANK TPLRQLDPSR 

       670        680        690        700        710        720 
LPGINCGPDF TPSFANLGRP ALSNRGPPRG GPGGELPRGP AGLGPRRSQQ GPRKETRKII 

       730        740        750        760        770        780 
SSVIMTEDIK LNKAEKAWKP SSKRTAADKD RGEEDADGSK TQDLFRRVRS ILNKLTPQMF 

       790        800        810        820        830        840 
QQLMKQVTQL AIDTEERLKG VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT 

       850        860        870        880        890        900 
VNFRKLLLNR CQKEFEKDKD DDEVFEKKQK EMDEAATAEE RGRLKEELEE ARDIARRRSL 

       910        920        930        940        950        960 
GNIKFIGELF KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFAKAKPRMD 

       970        980        990       1000       1010       1020 
QYFNQMEKII KEKKTSSRIR FMLQDVLDLR QSNWVPRRGD QGPKTIDQIH KEAEMEEHRE 

      1030       1040       1050       1060       1070       1080 
HIKVQQLMAK GSDKRRGGPP GPPINRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG 

      1090       1100       1110       1120       1130       1140 
SIDSNNQLFA PGGRLSWGKG SSGGSGAKPS DTASEATRPA TLNRFSALQQ TLPAENTDNR 

      1150       1160       1170       1180       1190       1200 
RVVQRSSLSR ERGEKAGDRG DRLERSERGG DRGDRLDRAR TPATKRSFSK EVEERSRERP 

      1210       1220       1230       1240       1250       1260 
SQPEGLRKAA SLTEDRGRDP VKREATLPPV SPPKAALSVD EVEKKSKAII EEYLHLNDMK 

      1270       1280       1290       1300       1310       1320 
EAVQCVQELA SPSLLFIFVR LGIESTLERS TIAREHMGRL LHQLLCAGHL STAQYYQGLY 

      1330       1340       1350       1360       1370       1380 
ETLELAEDME IDIPHVWLYL AELITPILQE DGVPMGELFR EITKPLRPMG KATSLLLEIL 

      1390       1400       1410       1420       1430       1440 
GLLCKSMGPK KVGMLWREAG LSWREFLAEG QDVGSFVAEK KVEYTLGEES EAPGQRTLAF 

      1450       1460       1470       1480       1490       1500 
EELRRQLEKL LKDGGSNQRV FDWIDANLNE QQIASNTLVR ALMTTVCYSA IIFETPLRVD 

      1510       1520       1530       1540       1550       1560 
VQVLKVRARL LQKYLCDEQK ELQALYALQA LVVTLEQPAN LLRMFFDALY DEDVVKEDAF 

      1570       1580       1590       1600 
YSWESSKDPA EQQGKGVALK SVTAFFNWLR EAEDEESDHN

« Hide

Isoform 2 [UniParc].

Checksum: 78C8FF512118F134
Show »

FASTA1,586174,580

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6.
Tissue: Brain and Fetal brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Lung.
[3]"Characterization of mammalian eIF4E-family members."
Joshi B., Cameron A., Jagus R.
Eur. J. Biochem. 271:2189-2203(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4E3.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-214 AND SER-1211, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, MASS SPECTROMETRY.
Tissue: Melanoma.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1597, MASS SPECTROMETRY.
Tissue: Macrophage.
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1597, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC066038 mRNA. Translation: AAH66038.1.
BC066103 mRNA. Translation: AAH66103.1.
BC079675 mRNA. Translation: AAH79675.1.
AK053144 mRNA. Translation: BAC35282.1.
IPIIPI00421179.
IPI00515195.
RefSeqNP_001005331.1. NM_001005331.1.
NP_666053.2. NM_145941.2.
UniGeneMm.260256.

3D structure databases

ProteinModelPortalQ6NZJ6.
SMRQ6NZJ6. Positions 180-206, 755-995, 1234-1592.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1856450.

PTM databases

PhosphoSiteQ6NZJ6.

Proteomic databases

PaxDbQ6NZJ6.
PRIDEQ6NZJ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044783; ENSMUSP00000047678; ENSMUSG00000045983.
ENSMUST00000115460; ENSMUSP00000111120; ENSMUSG00000045983.
ENSMUST00000115463; ENSMUSP00000111123; ENSMUSG00000045983.
GeneID208643.
KEGGmmu:208643.
UCSCuc007yqs.1. mouse.
uc007yqu.1. mouse.

Organism-specific databases

CTD1981.
MGIMGI:2384784. Eif4g1.

Phylogenomic databases

eggNOGNOG301289.
GeneTreeENSGT00530000063038.
HOGENOMHOG000231658.
HOVERGENHBG052083.
InParanoidQ6NZJ6.
KOK03260.
OMAHLSTAQY.
OrthoDBEOG4HX50F.

Gene expression databases

ArrayExpressQ6NZJ6.
BgeeQ6NZJ6.
GenevestigatorQ6NZJ6.
GermOnlineENSMUSG00000045983. Mus musculus.

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. ARM-type_fold. 3 hits.
PROSITEPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372353.
SOURCESearch...

Entry information

Entry nameIF4G1_MOUSE
AccessionPrimary (citable) accession number: Q6NZJ6
Secondary accession number(s): Q6NZN8, Q8BW99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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