Reviewed, UniProtKB/Swiss-Prot O00303 (EIF3F_HUMAN)

Names and origin

Protein names

Recommended name:
    Eukaryotic translation initiation factor 3 subunit F
      Short name=eIF3f
Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 5
    eIF-3-epsilon
    eIF3 p47

Gene names

Name:	EIF3F
Synonyms:	EIF3S5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.
Subunit structure	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of FRAP1 and RAPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Ref.6 Ref.12
Subcellular location	Cytoplasm Probable.
Post-translational modification	Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.10 Ref.11
Sequence similarities	Belongs to the eIF-3 subunit F family. Contains 1 MPN (JAB/Mov34) domain.
Mass spectrometry	Molecular mass is 37554.8 Da from positions 1 - 357. Ref.10 Molecular mass is 37475.6±0.2 Da from positions 1 - 357. Determined by MALDI. Ref.12

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	translational initiation Ref.12 Inferred by curator. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome eukaryotic translation initiation factor 3 complex Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	protein binding Ref.12 Inferred from physical interaction. Source: UniProtKB translation initiation factor activity Ref.1 Ref.12 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF1B	O60739	1	EBI-711990,EBI-1043343
EIF3A	Q14152	1	EBI-711990,EBI-366617
GLE1	Q53GS7	1	EBI-711990,EBI-1955541

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.10
	Chain	2 – 357	356	Eukaryotic translation initiation factor 3 subunit F		PRO_0000213964
Regions
	Domain	87 – 196	110	MPN
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.10
	Modified residue	258	1	Phosphoserine Ref.10 Ref.11
Natural variations
	Natural variant	39	1	P → L: dbSNP rs1043738.		VAR_029267
	Natural variant	172	1	W → L: dbSNP rs1044058.		VAR_014452
Experimental info
	Sequence conflict	50 – 56	7	Missing in BAC04577. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O00303-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 8A70FC6E2BF07737	FASTA	357	37,564
	10 20 30 40 50 60 MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA AAAAATAAPG 70 80 90 100 110 120 QTPASAQAPA QTPAPALPGP ALPGPFPGGR VVRLHPVILA SIVDSYERRN EGAARVIGTL 130 140 150 160 170 180 LGTVDKHSVE VTNCFSVPHN ESEDEVAVDM EFAKNMYELH KKVSPNELIL GWYATGHDIT 190 200 210 220 230 240 EHSVLIHEYY SREAPNPIHL TVDTSLQNGR MSIKAYVSTL MGVPGRTMGV MFTPLTVKYA 250 260 270 280 290 300 YYDTERIGVD LIMKTCFSPN RVIGLSSDLQ QVGGASARIQ DALSTVLQYA EDVLSGKVSA 310 320 330 340 350 DNTVGRFLMS LVNQVPKIVP DDFETMLNSN INDLLMVTYL ANLTQSQIAL NEKLVNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly." Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C., Hinnebusch A.G., Hershey J.W.B. J. Biol. Chem. 272:27042-27052(1997) [PubMed: 9341143] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala and Brain.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	"mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events." Holz M.K., Ballif B.A., Gygi S.P., Blenis J. Cell 123:569-580(2005) [PubMed: 16286006] [Abstract] Cited for: INTERACTION WITH RPS6KB1, IDENTIFICATION BY MASS SPECTROMETRY.
[7]	"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association." Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V. RNA 11:470-486(2005) [PubMed: 15703437] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[8]	"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit." LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E. J. Biol. Chem. 281:22917-22932(2006) [PubMed: 16766523] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"Reconstitution reveals the functional core of mammalian eIF3." Masutani M., Sonenberg N., Yokoyama S., Imataka H. EMBO J. 26:3373-3383(2007) [PubMed: 17581632] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[10]	"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry." Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A. Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed: 17322308] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-258, MASS SPECTROMETRY.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, MASS SPECTROMETRY.
[12]	"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3." Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V. Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed: 18599441] [Abstract] Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY, INTERACTION WITH EIF3B; EIF3H AND EIF3M.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Structural roles for human translation factor eIF3 in initiation of protein synthesis." Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E. Science 310:1513-1515(2005) [PubMed: 16322461] [Abstract] Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U94855 mRNA. Translation: AAD03467.1. AK095574 mRNA. Translation: BAC04577.1. AK289637 mRNA. Translation: BAF82326.1. AK291354 mRNA. Translation: BAF84043.1. BT006894 mRNA. Translation: AAP35540.1. CR456959 mRNA. Translation: CAG33240.1. BC000490 mRNA. Translation: AAH00490.1.
IPI	IPI00654777.
RefSeq	NP_003745.1.
UniGene	Hs.516023
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O00303. 18 interactions.
Protein family/group databases
MEROPS	M67.974.
PTM databases
PhosphoSite	O00303.
Proteomic databases
PRIDE	O00303.
Genome annotation databases
Ensembl	ENSG00000175390. Homo sapiens. [Contig view]
GeneID	8665.
KEGG	hsa:8665.
NMPDR	fig|9606.3.peg.5217.
Organism-specific databases
GeneCards	GC11P007966. GC12M005013.
H-InvDB	HIX0009420. HIX0037238. HIX0037638.
HGNC	HGNC:3275. EIF3F.
MIM	603914. gene.
PharmGKB	PA27703.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O00303.
HOVERGEN	O00303.
OMA	O00303. PEDFETM.
Enzyme and pathway databases
Reactome	REACT_1762. 3' -UTR-mediated translational regulation. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	O00303.
Bgee	O00303.
CleanEx	HS_EIF3F.
GermOnline	ENSG00000175390. Homo sapiens.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
ProDom	PD363422. Mov34-1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	32503.
SOURCE	Search...

Entry information

Entry name

EIF3F_HUMAN

Accession

Primary (citable) accession number: O00303
Secondary accession number(s): A8K0S2, Q6IB45, Q8N978

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)