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P39935 (IF4F1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 p150

Short name=eIF-4F p150
Short name=eIF4F p150
Alternative name(s):
eIF4G1
mRNA cap-binding protein complex subunit p150
Gene names
Name:TIF4631
Ordered Locus Names:YGR162W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length952 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. TIF4631 is probably essential when TIF4632 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.6 Ref.7 Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm Ref.11.

Miscellaneous

Present with 9760 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 1 MIF4G domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 952952Eukaryotic initiation factor 4F subunit p150
PRO_0000213331

Regions

Domain607 – 850244MIF4G
Region188 – 299112Interaction with PAB1
Compositional bias173 – 20028Pro/Ser/Thr-rich
Compositional bias375 – 38410Ala/Glu-rich
Compositional bias488 – 55366Arg/Ser-rich
Compositional bias869 – 8724Poly-Glu
Compositional bias873 – 89927Arg/Ser-rich

Amino acid modifications

Modified residue1811Phosphothreonine Ref.13
Modified residue8831Phosphoserine Ref.14
Modified residue8881Phosphothreonine Ref.14
Modified residue9081Phosphoserine Ref.15
Modified residue9481Phosphoserine Ref.13 Ref.15 Ref.16

Experimental info

Mutagenesis214 – 2174KLRK → AAAA in TIF4631-213; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. Ref.6
Sequence conflict71H → Q in AAA02757. Ref.1
Sequence conflict371T → N in AAA02757. Ref.1
Sequence conflict1101Q → K in AAA02757. Ref.1
Sequence conflict2071R → K in AAA02757. Ref.1
Sequence conflict3611D → E in AAA02757. Ref.1

Secondary structure

.................................. 952
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39935 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 391256802F86118E

FASTA952107,101
        10         20         30         40         50         60 
MTDETAHPTQ SASKQESAAL KQTGDDQQES QQQRGYTNYN NGSNYTQKKP YNSNRPHQQR 

        70         80         90        100        110        120 
GGKFGPNRYN NRGNYNGGGS FRGGHMGANS SNVPWTGYYN NYPVYYQPQQ MAAAGSAPAN 

       130        140        150        160        170        180 
PIPVEEKSPV PTKIEITTKS GEHLDLKEQH KAKLQSQERS TVSPQPESKL KETSDSTSTS 

       190        200        210        220        230        240 
TPTPTPSTND SKASSEENIS EAEKTRRNFI EQVKLRKAAL EKKRKEQLEG SSGNNNIPMK 

       250        260        270        280        290        300 
TTPENVEEKG SDKPEVTEKT KPAEEKSAEP EVKQETPAEE GEQGEKGQIK EESTPKVLTF 

       310        320        330        340        350        360 
AERLKLKKQQ KEREEKTEGK ENKEVPVQEE TKSAIESAPV PPSEQVKEET EVAETEQSNI 

       370        380        390        400        410        420 
DESATTPAIP TKSDEAEAEV EAEAGDAGTK IGLEAEIETT TDETDDGTNT VSHILNVLKD 

       430        440        450        460        470        480 
ATPIEDVFSF NYPEGIEGPD IKYKKEHVKY TYGPTFLLQF KDKLNVKADA EWVQSTASKI 

       490        500        510        520        530        540 
VIPPGMGRGN RSRDSGRFGN NSSRGHDFRN TSVRNMDDRA NSRTSSKRRS KRMNDDRRSN 

       550        560        570        580        590        600 
RSYTSRRDRE RGSYRNEEKR EDDKPKEEVA PLVPSANRWV PKFKSKKTEK KLAPDGKTEL 

       610        620        630        640        650        660 
LDKDEVERKM KSLLNKLTLE MFDAISSEIL AIANISVWET NGETLKAVIE QIFLKACDEP 

       670        680        690        700        710        720 
HWSSMYAQLC GKVVKELNPD ITDETNEGKT GPKLVLHYLV ARCHAEFDKG WTDKLPTNED 

       730        740        750        760        770        780 
GTPLEPEMMS EEYYAAASAK RRGLGLVRFI GFLYRLNLLT GKMMFECFRR LMKDLTDSPS 

       790        800        810        820        830        840 
EETLESVVEL LNTVGEQFET DSFRTGQATL EGSQLLDSLF GILDNIIQTA KISSRIKFKL 

       850        860        870        880        890        900 
IDIKELRHDK NWNSDKKDNG PKTIQQIHEE EERQRQLKNN SRSNSRRTNN SSNRHSFRRD 

       910        920        930        940        950 
APPASKDSFI TTRTYSQRNS QRAPPPKEEP AAPTSTATNM FSALMGESDD EE 

« 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]"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
Yeast 13:1077-1090(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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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 214-LYS--LYS-217.
[7]"Circularization of mRNA by eukaryotic translation initiation factors."
Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.
Mol. Cell 2:135-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAB1, ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP STRUCTURE.
[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]"The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex."
Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.
EMBO J. 19:4372-4382(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAB1.
[10]"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.
[11]"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].
[12]"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].
[13]"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-181 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[14]"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-883 AND THR-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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 SER-908 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E."
Gross J.D., Moerke N.J., von der Haar T., Lugovskoy A.A., Sachs A.B., McCarthy J.E.G., Wagner G.
Cell 115:739-750(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 389-488.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16923 Genomic DNA. Translation: AAA02757.1.
Z72947 Genomic DNA. Translation: CAA97184.1.
AY692973 Genomic DNA. Translation: AAT92992.1.
BK006941 Genomic DNA. Translation: DAA08257.1.
PIRS64473.
RefSeqNP_011678.3. NM_001181291.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RF8NMR-B391-488[»]
2VSOX-ray2.60E/F572-854[»]
2VSXX-ray2.80E/F572-854[»]
DisProtDP00082.
ProteinModelPortalP39935.
SMRP39935. Positions 391-488, 577-853.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33414. 143 interactions.
DIPDIP-985N.
IntActP39935. 62 interactions.
MINTMINT-617040.
STRING4932.YGR162W.

Proteomic databases

MaxQBP39935.
PaxDbP39935.
PeptideAtlasP39935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR162W; YGR162W; YGR162W.
GeneID853071.
KEGGsce:YGR162W.

Organism-specific databases

CYGDYGR162w.
SGDS000003394. TIF4631.

Phylogenomic databases

eggNOGNOG301289.
GeneTreeENSGT00530000063038.
HOGENOMHOG000065985.
KOK03260.
OMAEQFETDS.
OrthoDBEOG7VTDWG.

Enzyme and pathway databases

BioCycYEAST:G3O-30861-MONOMER.

Gene expression databases

GenevestigatorP39935.

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

EvolutionaryTraceP39935.
NextBio973024.

Entry information

Entry nameIF4F1_YEAST
AccessionPrimary (citable) accession number: P39935
Secondary accession number(s): D6VUU6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 144 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references