P39935 (IF4F1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	952 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. 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.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Initiation factor
PTM	Phosphoprotein
Technical term	3D-structure 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 ribosomal large subunit biogenesis Inferred from mutant phenotype PubMed 19806183. Source: SGD stress granule assembly Inferred from mutant phenotype PubMed 18981231. Source: SGD
Cellular_component	cytoplasmic stress granule Inferred from direct assay PubMed 17908917PubMed 18981231. Source: SGD eukaryotic translation initiation factor 4F complex Inferred from mutant phenotype Ref.1. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD ribosome Traceable author statement PubMed 9841679. Source: SGD
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro translation initiation factor activity Traceable author statement PubMed 9841679. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC33	P07260	10	EBI-9002,EBI-150
PAB1	P04147	2	EBI-9002,EBI-12823
TIF2	P10081	8	EBI-9002,EBI-9017

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 952

952

Eukaryotic initiation factor 4F subunit p150

PRO_0000213331

Regions

Domain

607 – 850

244

MIF4G

Region

188 – 299

112

Interaction with PAB1

Compositional bias

173 – 200

28

Pro/Ser/Thr-rich

Compositional bias

375 – 384

10

Ala/Glu-rich

Compositional bias

488 – 553

66

Arg/Ser-rich

Compositional bias

869 – 872

4

Poly-Glu

Compositional bias

873 – 899

27

Arg/Ser-rich

Amino acid modifications

Modified residue

163

1

Phosphoserine Ref.16

Modified residue

181

1

Phosphothreonine Ref.13

Modified residue

195

1

Phosphoserine Ref.16

Modified residue

276

1

Phosphothreonine Ref.15

Modified residue

293

1

Phosphoserine Ref.16

Modified residue

881

1

Phosphoserine Ref.14

Modified residue

885

1

Phosphoserine Ref.14

Modified residue

888

1

Phosphothreonine Ref.14

Modified residue

891

1

Phosphoserine Ref.14

Modified residue

892

1

Phosphoserine Ref.14 Ref.16

Modified residue

896

1

Phosphoserine Ref.14 Ref.16

Modified residue

908

1

Phosphoserine Ref.15 Ref.16

Modified residue

916

1

Phosphoserine Ref.16

Modified residue

920

1

Phosphoserine Ref.16

Modified residue

948

1

Phosphoserine Ref.13 Ref.16

Experimental info

Mutagenesis

214 – 217

4

KLRK → AAAA in TIF4631-213; abolishes interaction with PAB1 and inhibits poly(A)-dependent translation. Ref.6

Sequence conflict

7

1

H → Q in AAA02757. Ref.1

Sequence conflict

37

1

T → N in AAA02757. Ref.1

Sequence conflict

110

1

Q → K in AAA02757. Ref.1

Sequence conflict

207

1

R → K in AAA02757. Ref.1

Sequence conflict

361

1

D → E in AAA02757. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

952

Helix Strand Turn

Details...

Helix

411 – 419

9

Helix

427 – 429

3

Helix

443 – 445

3

Helix

454 – 464

11

Helix

471 – 476

6

Helix

603 – 615

13

Beta strand

619 – 621

3

Helix

622 – 634

13

Helix

635 – 638

4

Helix

643 – 658

16

Helix

660 – 662

3

Helix

663 – 676

14

Helix

692 – 709

18

Helix

733 – 755

23

Helix

761 – 776

16

Helix

781 – 798

18

Helix

812 – 827

16

Helix

834 – 848

15

Sequences

	Sequence		Length	Mass (Da)
	P39935 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 391256802F86118E	FASTA	952	107,101
	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

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]	"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. , 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]	"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. , 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, MASS SPECTROMETRY. 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-881; SER-885; THR-888; SER-891; SER-892 AND SER-896, MASS SPECTROMETRY.
[15]	"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-276 AND SER-908, MASS SPECTROMETRY.
[16]	"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-163; SER-195; SER-293; SER-892; SER-896; SER-908; SER-916; SER-920 AND SER-948, MASS SPECTROMETRY.
[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.

PIR

S64473.

RefSeq

NP_011678.3. NM_001181291.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RF8	NMR	-	B	391-488	[»]
2VSO	X-ray	2.60	E/F	572-854	[»]
2VSX	X-ray	2.80	E/F	572-854	[»]

DisProt

DP00082.

ProteinModelPortal

P39935.

SMR

P39935. Positions 391-488, 577-853.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-985N.

IntAct

P39935. 70 interactions.

MINT

MINT-617040.

STRING

4932.YGR162W.

Proteomic databases

PaxDb

P39935.

PeptideAtlas

P39935.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR162W; YGR162W; YGR162W.

GeneID

853071.

KEGG

sce:YGR162W.
sce:YGR169C.

Organism-specific databases

CYGD

YGR162w.

SGD

S000003394. TIF4631.

Phylogenomic databases

eggNOG

NOG301289.

GeneTree

ENSGT00530000063038.

HOGENOM

HOG000065985.

KO

K03260.
K15453.

OMA

TIQQIHE.

OrthoDB

EOG4CRQ7C.

Gene expression databases

Genevestigator

P39935.

GermOnline

YGR162W. 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

EvolutionaryTrace

P39935.

NextBio

973024.

Entry information

Entry name

IF4F1_YEAST

Accession

Primary (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:	April 3, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program