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(Top) 1 Interactions 2 See also 3 References 4 Further reading

EIF3I

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EIF3I

Identifiers

Aliases

EIF3I, EIF3S2, PRO2242, TRIP-1, TRIP1, eIF3-beta, eIF3-p36, eukaryotic translation initiation factor 3 subunit I

External IDs

OMIM: 603911; MGI: 1860763; HomoloGene: 2786; GeneCards: EIF3I; OMA:EIF3I - orthologs

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1p35.2	Start	32,221,077 bp^[1]
Band	1p35.2	End	32,245,397 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 D2.2\|4 63.26 cM	Start	129,485,753 bp^[2]
Band	4 D2.2\|4 63.26 cM	End	129,494,441 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

islet of Langerhans

ganglionic eminence

smooth muscle tissue

gastrocnemius muscle

rectum

left adrenal gland

right adrenal gland

ventricular zone

muscle of thigh

left adrenal cortex

Top expressed in

endocardial cushion

Paneth cell

Rostral migratory stream

internal carotid artery

condyle

atrioventricular valve

external carotid artery

vas deferens

fossa

human fetus

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding translation initiation factor activity
Cellular component	extracellular exosome cytosol cytoplasm eukaryotic translation initiation factor 3 complex eukaryotic translation initiation factor 3 complex, eIF3m eukaryotic 43S preinitiation complex eukaryotic 48S preinitiation complex
Biological process	translational initiation protein biosynthesis formation of cytoplasmic translation initiation complex cytoplasmic translational initiation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


8668


54709

Ensembl


ENSG00000084623


ENSMUSG00000028798

UniProt


Q13347


Q9QZD9

RefSeq (mRNA)


NM_003757 NM_001394168


NM_018799

RefSeq (protein)


NP_003748


NP_061269

Location (UCSC)

Chr 1: 32.22 – 32.25 Mb

Chr 4: 129.49 – 129.49 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Eukaryotic translation initiation factor 3 subunit I (eIF3i) is a protein that in humans is encoded by the EIF3I gene.^[5]^[6]^[7]

Interactions

[edit]

eIF3i has been shown to interact with TGF beta 1^[8] and eIF3a.^[6]^[9]^[10]

References

[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000084623 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028798 – 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.

^ Chen RH, Miettinen PJ, Maruoka EM, Choy L, Derynck R (Nov 1995). "A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor". Nature. 377 (6549): 548–52. Bibcode:1995Natur.377..548C. doi:10.1038/377548a0. PMID 7566156. S2CID 4341262.

^ ^a ^b Asano K, Kinzy TG, Merrick WC, Hershey JW (Feb 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.

^ "Entrez Gene: EIF3S2 eukaryotic translation initiation factor 3, subunit 2 beta, 36kDa".

^ Choy L, Derynck R (Nov 1998). "The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts as a modulator of the TGF-beta response". J. Biol. Chem. 273 (47): 31455–62. doi:10.1074/jbc.273.47.31455. PMID 9813058.

^ 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.

Galli-Stauber C, Raho G, Rossi D, Corona DF, Pirola B, Bonaglia MC, Zuffardi O, Sorrentino V (1998). "Genomic structure and chromosomal location of the human TGFbeta-receptor interacting protein-1 (TRIP-1) gene to 1p34.1". FEBS Lett. 426 (2): 279–82. doi:10.1016/S0014-5793(98)00361-5. PMID 9599024.

Choy L, Derynck R (1998). "The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts as a modulator of the TGF-beta response". J. Biol. Chem. 273 (47): 31455–62. doi:10.1074/jbc.273.47.31455. PMID 9813058.

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.

Poelzl G, Kasai Y, Mochizuki N, Shaul PW, Brown M, Mendelsohn ME (2000). "Specific association of estrogen receptor beta with the cell cycle spindle assembly checkpoint protein, MAD2". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2836–9. Bibcode:2000PNAS...97.2836P. doi:10.1073/pnas.050580997. PMC 16016. PMID 10706629.

McGonigle S, Beall MJ, Pearce EJ (2002). "Eukaryotic initiation factor 2 alpha subunit associates with TGF beta receptors and 14-3-3 epsilon and acts as a modulator of the TGF beta response". Biochemistry. 41 (2): 579–87. doi:10.1021/bi011407z. PMID 11781097.

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.

Fraser CS, Lee JY, Mayeur GL, Bushell M, Doudna JA, Hershey JW (2004). "The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro". J. Biol. Chem. 279 (10): 8946–56. doi:10.1074/jbc.M312745200. PMID 14688252.

Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.

Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.

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.

Guo D, Han J, Adam BL, Colburn NH, Wang MH, Dong Z, Eizirik DL, She JX, Wang CY (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.

Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, Kim JM, Song KS, Noh SM, Kim S, Yoo HS, Kim YS, Kim NS (2005). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674. S2CID 69278.

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins

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