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]
End| 8,001,862 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 7 (mouse)[2]

Band| 7|7 E3| Start| 108,533,624 bp[2]
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

[edit]

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

## See also

[edit]

* Eukaryotic initiation factor 3 (eIF3)

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000175390 – Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031029 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ 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.
6. ^ "Entrez Gene: EIF3S5 eukaryotic translation initiation factor 3, subunit 5 epsilon, 47kDa".
7. ^ 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.
8. ^ 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.
9. ^ 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.
10. ^ 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.

## Further reading

[edit]

* 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 9746088.1–3&rft.pages=203-8&rft.date=2005&rft_id=https://api.semanticscholar.org/CorpusID:9746088#id-name=S2CID&rft_id=info:pmid/15862967&rft_id=info:doi/10.1016/j.jsbmb.2005.01.007&rft.aulast=Pope&rft.aufirst=SN&rft.au=Lee,+IR&rfr_id=info:sid/en.wikipedia.org:EIF3F" class="Z3988">
* 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.

* v
* t
* e

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins|

| Initiation factor|

| Bacterial|

* IF1
* IF2
* IF3

|

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

Other concepts|

* Aminoacyl tRNA synthetase
* Reading frame
* Start codon
* Stop codon
* Shine-Dalgarno sequence/Kozak consensus sequence

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