P39936 (IF4F2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TIF4632
Ordered Locus Names:	YGL049C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	914 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA metabolic process Inferred from electronic annotation. Source: InterPro regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW stress granule assembly Inferred from mutant phenotype PubMed 18981231. Source: SGD
Cellular_component	cytoplasmic stress granule Inferred from direct assay PubMed 17908917PubMed 18981231PubMed 19470581. Source: SGD eukaryotic translation initiation factor 4F complex Inferred from genetic interaction Ref.1. Source: SGD
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro mRNA binding Inferred from direct assay PubMed 22851688. Source: SGD translation initiation factor activity Inferred from mutant phenotype PubMed 22851688. Source: SGD translation initiation factor binding Inferred from mutant phenotype PubMed 22851688. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAB1	P04147	2	EBI-9006,EBI-12823
PUB1	P32588	3	EBI-9006,EBI-14231

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 914	914	Eukaryotic initiation factor 4F subunit p130		PRO_0000213332
Regions
	Domain	567 – 810	244	MIF4G
	Region	201 – 315	115	Interaction with PAB1
	Compositional bias	32 – 97	66	Asn-rich
	Compositional bias	459 – 510	52	Arg/Ser-rich
	Compositional bias	840 – 863	24	Arg/Ser-rich
Amino acid modifications
	Modified residue	196	1	Phosphothreonine Ref.14 Ref.15
	Modified residue	301	1	Phosphothreonine Ref.12
	Modified residue	314	1	Phosphothreonine Ref.15
	Modified residue	347	1	Phosphothreonine Ref.14 Ref.15
	Modified residue	351	1	Phosphoserine Ref.14 Ref.15
	Modified residue	503	1	Phosphoserine Ref.13
	Modified residue	508	1	Phosphothreonine Ref.13
	Modified residue	509	1	Phosphoserine Ref.13
	Modified residue	913	1	Phosphoserine Ref.12
Experimental info
	Mutagenesis	233 – 236	4	RLRK → AVAA in TIF4632-233; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P39936 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: BF5E9805CD47908E	FASTA	914	103,899
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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, MASS SPECTROMETRY. 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; THR-508 AND SER-509, MASS SPECTROMETRY.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196; THR-347 AND SER-351, MASS SPECTROMETRY.
[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 THR-196; THR-314; THR-347 AND SER-351, MASS SPECTROMETRY.
+	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.
PIR	B48086.
RefSeq	NP_011466.1. NM_001180914.1.
3D structure databases
ProteinModelPortal	P39936.
SMR	P39936. Positions 382-459, 537-813.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-330N.
IntAct	P39936. 32 interactions.
MINT	MINT-424681.
STRING	4932.YGL049C.
Proteomic databases
PaxDb	P39936.
PeptideAtlas	P39936.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL049C; YGL049C; YGL049C.
GeneID	852833.
KEGG	sce:YGL049C.
Organism-specific databases
CYGD	YGL049c.
SGD	S000003017. TIF4632.
Phylogenomic databases
eggNOG	NOG301289.
GeneTree	ENSGT00530000063038.
HOGENOM	HOG000065985.
KO	K03260.
OMA	RWIPKSR.
OrthoDB	EOG4CRQ7C.
Gene expression databases
Genevestigator	P39936.
GermOnline	YGL049C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.25.40.180. 1 hit.
InterPro	IPR016024. ARM-type_fold. IPR022745. eIF4G1_eIF4E-bd. IPR016021. MIF4-like_typ_1/2/3. IPR003890. MIF4G-like_typ-3. [Graphical view]
Pfam	PF12152. eIF_4G1. 1 hit. PF02854. MIF4G. 1 hit. [Graphical view]
SMART	SM00543. MIF4G. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF101489. eIF4G1_eIF4E-bd. 1 hit.
ProtoNet	Search...
Other
NextBio	972400.

Entry information

Entry name

IF4F2_YEAST

Accession

Primary (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 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program