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P39936 (IF4F2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic initiation factor 4F subunit p130

Short name=eIF-4F p130
Short name=eIF4F p130
Alternative name(s):
eIF4G2
mRNA cap-binding protein complex subunit p130
Gene names
Name:TIF4632
Ordered Locus Names:YGL049C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length914 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4632 is probably essential when TIF4631 is missing. Ref.6 Ref.8

Subunit structure

Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) By similarity. Interacts with PAT1 in a RNA-dependent manner. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm Ref.10.

Miscellaneous

Present with 3390 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 1 MIF4G domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAB1P041472EBI-9006,EBI-12823
PUB1P325883EBI-9006,EBI-14231

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 914914Eukaryotic initiation factor 4F subunit p130
PRO_0000213332

Regions

Domain567 – 810244MIF4G
Region201 – 315115Interaction with PAB1
Compositional bias32 – 9766Asn-rich
Compositional bias459 – 51052Arg/Ser-rich
Compositional bias840 – 86324Arg/Ser-rich

Amino acid modifications

Modified residue741Phosphoserine Ref.15
Modified residue1961Phosphothreonine Ref.14 Ref.15
Modified residue3011Phosphothreonine Ref.12
Modified residue5031Phosphoserine Ref.13
Modified residue9131Phosphoserine Ref.12 Ref.15

Experimental info

Mutagenesis233 – 2364RLRK → AVAA in TIF4632-233; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P39936 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BF5E9805CD47908E

FASTA914103,899
        10         20         30         40         50         60 
MTDQRGPPPP HPQQANGYKK FPPHDNQYSG ANNSQPNNHY NENLYSAREP HNNKQYQSKN 

        70         80         90        100        110        120 
GKYGTNKYNN RNNSQGNAQY YNNRFNNGYR LNNNDYNPAM LPGMQWPANY YAPQMYYIPQ 

       130        140        150        160        170        180 
QMVPVASPPY THQPLNTNPE PPSTPKTTKI EITTKTGERL NLKKFHEEKK ASKGEEKNDG 

       190        200        210        220        230        240 
VEQKSKSGTP FEKEATPVLP ANEAVKDTLT ETSNEKSTSE AENTKRLFLE QVRLRKAAME 

       250        260        270        280        290        300 
RKKNGLISET EKKQETSNHD NTDTTKPNSV IESEPIKEAP KPTGEANEVV IDGKSGASVK 

       310        320        330        340        350        360 
TPQHVTGSVT KSVTFNEPEN ESSSQDVDEL VKDDDTTEIS DTTGGKTVNK SDDETINSVI 

       370        380        390        400        410        420 
TTEENTVKET EPSTSDIEMP TVSQLLETLG KAQPISDIYE FAYPENVERP DIKYKKPSVK 

       430        440        450        460        470        480 
YTYGPTFLLQ FKDKLKFRPD PAWVEAVSSK IVIPPHIARN KPKDSGRFGG DFRSPSMRGM 

       490        500        510        520        530        540 
DHTSSSRVSS KRRSKRMGDD RRSNRGYTSR KDREKAAEKA EEQAPKEEIA PLVPSANRWI 

       550        560        570        580        590        600 
PKSRVKKTEK KLAPDGKTEL FDKEEVERKM KSLLNKLTLE MFDSISSEIL DIANQSKWED 

       610        620        630        640        650        660 
DGETLKIVIE QIFHKACDEP HWSSMYAQLC GKVVKDLDPN IKDKENEGKN GPKLVLHYLV 

       670        680        690        700        710        720 
ARCHEEFEKG WADKLPAGED GNPLEPEMMS DEYYIAAAAK RRGLGLVRFI GYLYCLNLLT 

       730        740        750        760        770        780 
GKMMFECFRR LMKDLNNDPS EETLESVIEL LNTVGEQFEH DKFVTPQATL EGSVLLDNLF 

       790        800        810        820        830        840 
MLLQHIIDGG TISNRIKFKL IDVKELREIK HWNSAKKDAG PKTIQQIHQE EEQLRQKKNS 

       850        860        870        880        890        900 
QRSNSRFNNH NQSNSNRYSS NRRNMQNTQR DSFASTKTGS FRNNQRNARK VEEVSQAPRA 

       910 
NMFDALMNND GDSD 

« Hide

References

« Hide 'large scale' references
[1]"TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function."
Goyer C., Altmann M., Lee H.S., Blanc A., Deshmukh M., Woolford J.L. Jr., Trachsel H., Sonenberg N.
Mol. Cell. Biol. 13:4860-4874(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G."
Tarun S.Z. Jr., Sachs A.B.
EMBO J. 15:7168-7177(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAB1.
[6]"Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation."
Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.
Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAB1, MUTAGENESIS OF 233-ARG--LYS-236.
[7]"RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G."
Kessler S.H., Sachs A.B.
Mol. Cell. Biol. 18:51-57(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAB1.
[8]"The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms."
Otero L.J., Ashe M.P., Sachs A.B.
EMBO J. 18:3153-3163(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAB1.
[9]"Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs."
Tharun S., Parker R.
Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAT1.
[10]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-301 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[13]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; THR-196 AND SER-913, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16924 Unassigned DNA. Translation: AAA18474.1.
Z72571 Genomic DNA. Translation: CAA96751.1.
BK006941 Genomic DNA. Translation: DAA08052.1.
PIRB48086.
RefSeqNP_011466.1. NM_001180914.1.

3D structure databases

ProteinModelPortalP39936.
SMRP39936. Positions 382-459, 537-813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33199. 71 interactions.
DIPDIP-330N.
IntActP39936. 28 interactions.
MINTMINT-424681.
STRING4932.YGL049C.

Proteomic databases

PaxDbP39936.
PeptideAtlasP39936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL049C; YGL049C; YGL049C.
GeneID852833.
KEGGsce:YGL049C.

Organism-specific databases

CYGDYGL049c.
SGDS000003017. TIF4632.

Phylogenomic databases

eggNOGNOG301289.
GeneTreeENSGT00530000063038.
HOGENOMHOG000065985.
KOK03260.
OMANIPPRTH.
OrthoDBEOG7VTDWG.

Enzyme and pathway databases

BioCycYEAST:G3O-30559-MONOMER.

Gene expression databases

GenevestigatorP39936.

Family and domain databases

Gene3D1.25.40.180. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR022745. eIF4G1_eIF4E-bd.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamPF12152. eIF_4G1. 1 hit.
PF02854. MIF4G. 1 hit.
[Graphical view]
SMARTSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMSSF101489. SSF101489. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio972400.

Entry information

Entry nameIF4F2_YEAST
AccessionPrimary (citable) accession number: P39936
Secondary accession number(s): D6VU91
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families