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Protein

Eukaryotic initiation factor 4F subunit p130

Gene

TIF4632

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. mRNA binding Source: SGD
  2. translation initiation factor activity Source: SGD
  3. translation initiation factor binding Source: SGD

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. stress granule assembly Source: SGD
  3. translational initiation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30559-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_303457. S6K1 signalling.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TIF4632
Ordered Locus Names:YGL049C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL049c.
SGDiS000003017. TIF4632.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: SGD
  2. cytoplasmic stress granule Source: SGD
  3. eukaryotic translation initiation factor 4F complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi233 – 2364RLRK → AVAA in TIF4632-233; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 914914Eukaryotic initiation factor 4F subunit p130PRO_0000213332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741Phosphoserine1 Publication
Modified residuei196 – 1961Phosphothreonine2 Publications
Modified residuei301 – 3011Phosphothreonine1 Publication
Modified residuei503 – 5031Phosphoserine1 Publication
Modified residuei913 – 9131Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39936.
PaxDbiP39936.
PeptideAtlasiP39936.

Expressioni

Gene expression databases

GenevestigatoriP39936.

Interactioni

Subunit structurei

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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PAB1P041472EBI-9006,EBI-12823
PUB1P325883EBI-9006,EBI-14231

Protein-protein interaction databases

BioGridi33199. 73 interactions.
DIPiDIP-330N.
IntActiP39936. 28 interactions.
MINTiMINT-424681.
STRINGi4932.YGL049C.

Structurei

3D structure databases

ProteinModelPortaliP39936.
SMRiP39936. Positions 382-459, 537-813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini567 – 810244MIF4GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 315115Interaction with PAB1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 9766Asn-richAdd
BLAST
Compositional biasi459 – 51052Arg/Ser-richAdd
BLAST
Compositional biasi840 – 86324Arg/Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 MIF4G domain.Curated

Phylogenomic databases

eggNOGiNOG301289.
GeneTreeiENSGT00530000063038.
HOGENOMiHOG000065985.
InParanoidiP39936.
KOiK03260.
OMAiNIPPRTH.
OrthoDBiEOG7VTDWG.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR022745. eIF4G1_eIF4E-bd.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamiPF12152. eIF_4G1. 1 hit.
PF02854. MIF4G. 1 hit.
[Graphical view]
SMARTiSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF101489. SSF101489. 1 hit.
SSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

P39936-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDQRGPPPP HPQQANGYKK FPPHDNQYSG ANNSQPNNHY NENLYSAREP
60 70 80 90 100
HNNKQYQSKN GKYGTNKYNN RNNSQGNAQY YNNRFNNGYR LNNNDYNPAM
110 120 130 140 150
LPGMQWPANY YAPQMYYIPQ QMVPVASPPY THQPLNTNPE PPSTPKTTKI
160 170 180 190 200
EITTKTGERL NLKKFHEEKK ASKGEEKNDG VEQKSKSGTP FEKEATPVLP
210 220 230 240 250
ANEAVKDTLT ETSNEKSTSE AENTKRLFLE QVRLRKAAME RKKNGLISET
260 270 280 290 300
EKKQETSNHD NTDTTKPNSV IESEPIKEAP KPTGEANEVV IDGKSGASVK
310 320 330 340 350
TPQHVTGSVT KSVTFNEPEN ESSSQDVDEL VKDDDTTEIS DTTGGKTVNK
360 370 380 390 400
SDDETINSVI TTEENTVKET EPSTSDIEMP TVSQLLETLG KAQPISDIYE
410 420 430 440 450
FAYPENVERP DIKYKKPSVK YTYGPTFLLQ FKDKLKFRPD PAWVEAVSSK
460 470 480 490 500
IVIPPHIARN KPKDSGRFGG DFRSPSMRGM DHTSSSRVSS KRRSKRMGDD
510 520 530 540 550
RRSNRGYTSR KDREKAAEKA EEQAPKEEIA PLVPSANRWI PKSRVKKTEK
560 570 580 590 600
KLAPDGKTEL FDKEEVERKM KSLLNKLTLE MFDSISSEIL DIANQSKWED
610 620 630 640 650
DGETLKIVIE QIFHKACDEP HWSSMYAQLC GKVVKDLDPN IKDKENEGKN
660 670 680 690 700
GPKLVLHYLV ARCHEEFEKG WADKLPAGED GNPLEPEMMS DEYYIAAAAK
710 720 730 740 750
RRGLGLVRFI GYLYCLNLLT GKMMFECFRR LMKDLNNDPS EETLESVIEL
760 770 780 790 800
LNTVGEQFEH DKFVTPQATL EGSVLLDNLF MLLQHIIDGG TISNRIKFKL
810 820 830 840 850
IDVKELREIK HWNSAKKDAG PKTIQQIHQE EEQLRQKKNS QRSNSRFNNH
860 870 880 890 900
NQSNSNRYSS NRRNMQNTQR DSFASTKTGS FRNNQRNARK VEEVSQAPRA
910
NMFDALMNND GDSD
Length:914
Mass (Da):103,899
Last modified:February 1, 1995 - v1
Checksum:iBF5E9805CD47908E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16924 Unassigned DNA. Translation: AAA18474.1.
Z72571 Genomic DNA. Translation: CAA96751.1.
BK006941 Genomic DNA. Translation: DAA08052.1.
PIRiB48086.
RefSeqiNP_011466.1. NM_001180914.1.

Genome annotation databases

EnsemblFungiiYGL049C; YGL049C; YGL049C.
GeneIDi852833.
KEGGisce:YGL049C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16924 Unassigned DNA. Translation: AAA18474.1.
Z72571 Genomic DNA. Translation: CAA96751.1.
BK006941 Genomic DNA. Translation: DAA08052.1.
PIRiB48086.
RefSeqiNP_011466.1. NM_001180914.1.

3D structure databases

ProteinModelPortaliP39936.
SMRiP39936. Positions 382-459, 537-813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33199. 73 interactions.
DIPiDIP-330N.
IntActiP39936. 28 interactions.
MINTiMINT-424681.
STRINGi4932.YGL049C.

Proteomic databases

MaxQBiP39936.
PaxDbiP39936.
PeptideAtlasiP39936.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL049C; YGL049C; YGL049C.
GeneIDi852833.
KEGGisce:YGL049C.

Organism-specific databases

CYGDiYGL049c.
SGDiS000003017. TIF4632.

Phylogenomic databases

eggNOGiNOG301289.
GeneTreeiENSGT00530000063038.
HOGENOMiHOG000065985.
InParanoidiP39936.
KOiK03260.
OMAiNIPPRTH.
OrthoDBiEOG7VTDWG.

Enzyme and pathway databases

BioCyciYEAST:G3O-30559-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_303457. S6K1 signalling.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.

Miscellaneous databases

NextBioi972400.

Gene expression databases

GenevestigatoriP39936.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR022745. eIF4G1_eIF4E-bd.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamiPF12152. eIF_4G1. 1 hit.
PF02854. MIF4G. 1 hit.
[Graphical view]
SMARTiSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF101489. SSF101489. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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(1996) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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(1995) [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(1996) [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(1997) [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(1998) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAT1.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. 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(2006) [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(2006) [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(2007) [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(2008) [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].

Entry informationi

Entry nameiIF4F2_YEAST
AccessioniPrimary (citable) accession number: P39936
Secondary accession number(s): D6VU91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 1, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3390 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.