EIF3F

Protein-coding gene in the species Homo sapiens

EIF3F

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3J8B, 3J8C

Identifiers

Aliases

EIF3F, EIF3S5, eIF3-p47, eukaryotic translation initiation factor 3 subunit F, MRT67

External IDs

OMIM: 603914; MGI: 1913335; HomoloGene: 2783; GeneCards: EIF3F; OMA:EIF3F - orthologs

EC number

3.4.19.12

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11p15.4	Start	7,970,251 bp^[1]
Band	11p15.4	End	8,001,862 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7\|7 E3	Start	108,533,624 bp^[2]
Band	7\|7 E3	End	108,542,158 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

gonad

ganglionic eminence

left ovary

skin of leg

skin of abdomen

body of pancreas

ventricular zone

right ovary

stromal cell of endometrium

body of uterus

Top expressed in

Paneth cell

transitional epithelium of urinary bladder

vas deferens

vestibular sensory epithelium

medial ganglionic eminence

hair follicle

utricle

endothelial cell of lymphatic vessel

internal carotid artery

fossa

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	cysteine-type peptidase activity translation initiation factor activity thiol-dependent deubiquitinase peptidase activity protein binding hydrolase activity translation initiation factor binding
Cellular component	cytoplasm cytosol eukaryotic translation initiation factor 3 complex membrane eukaryotic translation initiation factor 3 complex, eIF3m eukaryotic 43S preinitiation complex eukaryotic 48S preinitiation complex
Biological process	proteolysis translational initiation protein biosynthesis IRES-dependent viral translational initiation protein deubiquitination formation of cytoplasmic translation initiation complex cytoplasmic translational initiation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


8665


66085

Ensembl


ENSG00000175390


ENSMUSG00000031029

UniProt


O00303


Q9DCH4

RefSeq (mRNA)


NM_003754


NM_025344

RefSeq (protein)


NP_003745


NP_079620

Location (UCSC)

Chr 11: 7.97 – 8 Mb

Chr 7: 108.53 – 108.54 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Eukaryotic translation initiation factor 3 subunit F (eIF3f) is a protein that in humans is encoded by the EIF3F gene.^[5]^[6]

Interactions

EIF3F has been shown to interact with Mammalian target of rapamycin^[7] and EIF3A.^[8]^[9]^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000175390 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031029 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Asano K, Vornlocher HP, Richter-Cook NJ, Merrick WC, Hinnebusch AG, Hershey JW (Nov 1997). "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly". J. Biol. Chem. 272 (43): 27042–52. doi:10.1074/jbc.272.43.27042. PMID 9341143.
^ "Entrez Gene: EIF3S5 eukaryotic translation initiation factor 3, subunit 5 epsilon, 47kDa".
^ Harris TE, Chi A, Shabanowitz J, Hunt DF, Rhoads RE, Lawrence JC (Apr 2006). "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin". EMBO J. 25 (8): 1659–68. doi:10.1038/sj.emboj.7601047. PMC 1440840. PMID 16541103.
^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
^ Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (Oct 2003). "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3". Eur. J. Biochem. 270 (20): 4133–9. doi:10.1046/j.1432-1033.2003.03807.x. PMID 14519125.
^ Block KL, Vornlocher HP, Hershey JW (Nov 1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". J. Biol. Chem. 273 (48): 31901–8. doi:10.1074/jbc.273.48.31901. PMID 9822659.

Asano K, Kinzy TG, Merrick WC, Hershey JW (1997). "Conservation and diversity of eukaryotic translation initiation factor eIF3". J. Biol. Chem. 272 (2): 1101–9. doi:10.1074/jbc.272.2.1101. PMID 8995409.
Méthot N, Rom E, Olsen H, Sonenberg N (1997). "The human homologue of the yeast Prt1 protein is an integral part of the eukaryotic initiation factor 3 complex and interacts with p170". J. Biol. Chem. 272 (2): 1110–6. doi:10.1074/jbc.272.2.1110. PMID 8995410.
Block KL, Vornlocher HP, Hershey JW (1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". J. Biol. Chem. 273 (48): 31901–8. doi:10.1074/jbc.273.48.31901. PMID 9822659.
Shi J, Feng Y, Goulet AC, Vaillancourt RR, Sachs NA, Hershey JW, Nelson MA (2003). "The p34cdc2-related cyclin-dependent kinase 11 interacts with the p47 subunit of eukaryotic initiation factor 3 during apoptosis". J. Biol. Chem. 278 (7): 5062–71. doi:10.1074/jbc.M206427200. PMID 12446680.
Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (2003). "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor elF3". Eur. J. Biochem. 270 (20): 4133–9. doi:10.1046/j.1432-1033.2003.03807.x. PMID 14519125.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967. S2CID 9746088.
Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (2005). "A human protein–protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein–protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Sheffler DJ, Kroeze WK, Garcia BG, Deutch AY, Hufeisen SJ, Leahy P, Brüning JC, Roth BL (2006). "p90 ribosomal S6 kinase 2 exerts a tonic brake on G protein-coupled receptor signaling". Proc. Natl. Acad. Sci. U.S.A. 103 (12): 4717–22. Bibcode:2006PNAS..103.4717S. doi:10.1073/pnas.0600585103. PMC 1450237. PMID 16537434.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins

Initiation factor

Bacterial

Mitochondrial

MTIF1
MTIF2
MTIF3

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	eIF1 B SUI1 family eIF1A Y
eIF2	α kinase β γ eIF2A eIF2B 1 2 3 4 5 eIF2D
eIF3	A B C D E F G H I J K L M
eIF4	A 1 2 3 E1 2 3 G 1 2 3 B H
eIF5	EIF5 EIF5A 2 5B
eIF6	EIF6

Elongation factor

Bacterial/Mitochondrial	EF-Tu EF-Ts EF-G EF-4 EF-P TSFM GFM1 GFM2
Archaeal/Eukaryotic	a/eEF-1 A1 2 3 B P1 P2 P3 D E G a/eEF-2

Release factor

Class 1
- eRF1
Class 2/RF3
- GSPT1
- GSPT2

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL17 RPL18 RPL18A RPL19 RPL21 RPL22 RPL23 RPL23A RPL24 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 RRP15-like RSL24D1
40S subunit	RPSA RPS2 RPS3 RPS3A RPS4 (RPS4X, RPS4Y1, RPS4Y2) RPS5 RPS6 RPS7 RPS8 RPS9 RPS10 RPS11 RPS12 RPS13 RPS14 RPS15 RPS15A RPS16 RPS17 RPS18 RPS19 RPS20 RPS21 RPS23 RPS24 RPS25 RPS26 RPS27 RPS27A RPS28 RPS29 RPS30 RACK1

Mitochondrial

39S subunit	MRPL1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42
28S subunit	MRPS1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35