Q9NRA8 (4ET_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 4E transporter
Short name=4E-T
Short name=eIF4E transporter

Alternative name(s):
Eukaryotic translation initiation factor 4E nuclear import factor 1

Gene names

Name:

EIF4ENIF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	985 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Nucleoplasmic shuttling protein. Mediates the nuclear import of EIF4E by a piggy-back mechanism.
Subunit structure	Interacts with EIF4E. Interacts with importin beta only in the presence of importin alpha, suggesting a direct interaction with importin alpha. Interacts with APOBEC3G in an RNA-dependent manner. Ref.7
Subcellular location	Cytoplasm. Nucleus. Nucleus › PML body. Nucleus speckle. Note: Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localization to nuclear foci and speckles requires active transcription. Ref.15
Tissue specificity	Widely expressed.
Sequence caution	The sequence BAB15092.1 differs from that shown. Reason: Erroneous initiation. The sequence BAC11194.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Traceable author statement Ref.1. Source: ProtInc cytosol Inferred from electronic annotation. Source: Compara nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	protein transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4E	P06730	5	EBI-301024,EBI-73440
EIF4E2	O60573	3	EBI-301024,EBI-398610

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NRA8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NRA8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-262: Missing.
     493-504: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 985	985	Eukaryotic translation initiation factor 4E transporter		PRO_0000064381
Regions
	Region	30 – 36	7	EIF4E-binding
	Motif	195 – 211	17	Nuclear localization signal
	Motif	438 – 447	10	Nuclear export signal
	Motif	613 – 638	26	Nuclear export signal
	Compositional bias	148 – 210	63	Arg-rich
Amino acid modifications
	Modified residue	5	1	Phosphoserine Ref.10 Ref.12
	Modified residue	78	1	Phosphoserine By similarity
	Modified residue	120	1	Phosphoserine Ref.9
	Modified residue	136	1	Phosphoserine Ref.9
	Modified residue	138	1	Phosphoserine Ref.9
	Modified residue	301	1	Phosphoserine Ref.12
	Modified residue	345	1	Phosphoserine Ref.9
	Modified residue	486	1	N6-acetyllysine Ref.11
	Modified residue	513	1	Phosphoserine Ref.12
	Modified residue	564	1	Phosphoserine Ref.9 Ref.10 Ref.12
	Modified residue	587	1	Phosphoserine Ref.10
	Modified residue	693	1	Phosphoserine Ref.10
	Modified residue	920	1	Phosphoserine Ref.8
	Modified residue	951	1	Phosphoserine Ref.9 Ref.12 Ref.14
Natural variations
	Alternative sequence	100 – 262	163	Missing in isoform 2.		VSP_003783
	Alternative sequence	493 – 504	12	Missing in isoform 2.		VSP_003784
Experimental info
	Mutagenesis	30	1	Y → A: Abolishes interaction with EIF4E. Ref.1
	Mutagenesis	195 – 196	2	RR → NS: Abolishes the nuclear localization.
	Sequence conflict	114	1	L → F in AAF81693. Ref.1
	Sequence conflict	616	1	Q → QQ in BAB15092. Ref.3
	Sequence conflict	616	1	Q → QQ in AAH32941. Ref.6
	Sequence conflict	825	1	Q → R in AAH33028. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 2, 2002. Version 2. Checksum: 4C898E0488903C04	FASTA	985	108,201
	10 20 30 40 50 60 MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC LSEKYDSDGV 70 80 90 100 110 120 WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVD PRERVKEDDL DVVLSPQRRS 130 140 150 160 170 180 FGGGCHVTAA VSSRRSGSPL EKDSDGLRLL GGRRIGSGRI ISARTFEKDH RLSDKDLRDL 190 200 210 220 230 240 RDRDRERDFK DKRFRREFGD SKRVFGERRR NDSYTEEEPE WFSAGPTSQS ETIELTGFDD 250 260 270 280 290 300 KILEEDHKGR KRTRRRTASV KEGIVECNGG VAEEDEVEVI LAQEPAADQE VPRDAVLPEQ 310 320 330 340 350 360 SPGDFDFNEF FNLDKVPCLA SMIEDVLGEG SVSASRFSRW FSNPSRSGSR SSSLGSTPHE 370 380 390 400 410 420 ELERLAGLEQ AILSPGQNSG NYFAPIPLED HAENKVDILE MLQKAKVDLK PLLSSLSANK 430 440 450 460 470 480 EKLKESSHSG VVLSVEEVEA GLKGLKVDQQ VKNSTPFMAE HLEETLSAVT NNRQLKKDGD 490 500 510 520 530 540 MTAFNKLVST MKASGTLPSQ PKVSRNLESH LMSPAEIPGQ PVPKNILQEL LGQPVQRPAS 550 560 570 580 590 600 SNLLSGLMGS LEPTTSLLGQ RAPSPPLSQV FQTRAASADY LRPRIPSPIG FTPGPQQLLG 610 620 630 640 650 660 DPFQGMRKPM SPITAQMSQL ELQQAALEGL ALPHDLAVQA ANFYQPGFGK PQVDRTRDGF 670 680 690 700 710 720 RNRQQRVTKS PAPVHRGNSS SPAPAASITS MLSPSFTPTS VIRKMYESKE KSKEEPASGK 730 740 750 760 770 780 AALGDSKEDT QKASEENLLS SSSVPSADRD SSPTTNSKLS ALQRSSCSTP LSQANRYTKE 790 800 810 820 830 840 QDYRPKATGR KTPTLASPVP TTPFLRPVHQ VPLVPHVPMV RPAHQLHPGL VQRMLAQGVH 850 860 870 880 890 900 PQHLPSLLQT GVLPPGMDLS HLQGISGPIL GQPFYPLPAA SHPLLNPRPG TPLHLAMVQQ 910 920 930 940 950 960 QLQRSVLHPP GSGSHAAAVS VQTTPQNVPS RSGLPHMHSQ LEHRPSQRSS SPVGLAKWFG 970 980 SDVLQQPLPS MPAKVISVDE LEYRQ
	Isoform 2 [UniParc]. Checksum: 3CDFA55990053C52	FASTA	810	88,098
	10 20 30 40 50 60 MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC LSEKYDSDGV 70 80 90 100 110 120 WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVG IVECNGGVAE EDEVEVILAQ 130 140 150 160 170 180 EPAADQEVPR DAVLPEQSPG DFDFNEFFNL DKVPCLASMI EDVLGEGSVS ASRFSRWFSN 190 200 210 220 230 240 PSRSGSRSSS LGSTPHEELE RLAGLEQAIL SPGQNSGNYF APIPLEDHAE NKVDILEMLQ 250 260 270 280 290 300 KAKVDLKPLL SSLSANKEKL KESSHSGVVL SVEEVEAGLK GLKVDQQVKN STPFMAEHLE 310 320 330 340 350 360 ETLSAVTNNR QLKKDGDMTA FNKLVSTMKR NLESHLMSPA EIPGQPVPKN ILQELLGQPV 370 380 390 400 410 420 QRPASSNLLS GLMGSLEPTT SLLGQRAPSP PLSQVFQTRA ASADYLRPRI PSPIGFTPGP 430 440 450 460 470 480 QQLLGDPFQG MRKPMSPITA QMSQLELQQA ALEGLALPHD LAVQAANFYQ PGFGKPQVDR 490 500 510 520 530 540 TRDGFRNRQQ RVTKSPAPVH RGNSSSPAPA ASITSMLSPS FTPTSVIRKM YESKEKSKEE 550 560 570 580 590 600 PASGKAALGD SKEDTQKASE ENLLSSSSVP SADRDSSPTT NSKLSALQRS SCSTPLSQAN 610 620 630 640 650 660 RYTKEQDYRP KATGRKTPTL ASPVPTTPFL RPVHQVPLVP HVPMVRPAHQ LHPGLVQRML 670 680 690 700 710 720 AQGVHPQHLP SLLQTGVLPP GMDLSHLQGI SGPILGQPFY PLPAASHPLL NPRPGTPLHL 730 740 750 760 770 780 AMVQQQLQRS VLHPPGSGSH AAAVSVQTTP QNVPSRSGLP HMHSQLEHRP SQRSSSPVGL 790 800 810 AKWFGSDVLQ QPLPSMPAKV ISVDELEYRQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E." Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N. EMBO J. 19:3142-3156(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, PHOSPHORYLATION, MUTAGENESIS OF TYR-30 AND 195-ARG-ARG-196. Tissue: Fetal brain.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Placenta and Teratocarcinoma.
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Testis.
[7]	"Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies." Wichroski M.J., Robb G.B., Rana T.M. PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APOBEC3G.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, MASS SPECTROMETRY. Tissue: Platelet.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-136; SER-138; SER-345; SER-564 AND SER-951, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-564; SER-587 AND SER-693, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, MASS SPECTROMETRY.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-301; SER-513; SER-564 AND SER-951, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-951, MASS SPECTROMETRY.
[15]	"RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor." Marnef A., Weil D., Standart N. Mol. Biol. Cell 23:213-224(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF240775 mRNA. Translation: AAF81693.1. CR456386 mRNA. Translation: CAG30272.1. AK025254 mRNA. Translation: BAB15092.1. Different initiation. AK074768 mRNA. Translation: BAC11194.1. Different initiation. AK314636 mRNA. Translation: BAG37198.1. AL096701 Genomic DNA. Translation: CAI12878.1. CH471095 Genomic DNA. Translation: EAW59977.1. BC032941 mRNA. Translation: AAH32941.1. BC033028 mRNA. Translation: AAH33028.1.
IPI	IPI00291800. IPI00550518.
RefSeq	NP_001157973.1. NM_001164501.1. NP_001157974.1. NM_001164502.1. NP_062817.2. NM_019843.3.
UniGene	Hs.517559.
3D structure databases
ProteinModelPortal	Q9NRA8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRA8. 10 interactions.
MINT	MINT-1956064.
STRING	9606.ENSP00000328103.
PTM databases
PhosphoSite	Q9NRA8.
Polymorphism databases
DMDM	22095430.
Proteomic databases
PaxDb	Q9NRA8.
PRIDE	Q9NRA8.
Protocols and materials databases
DNASU	56478.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330125; ENSP00000328103; ENSG00000184708. ENST00000397525; ENSP00000380659; ENSG00000184708.
GeneID	56478.
KEGG	hsa:56478.
UCSC	uc003aky.2. human.
Organism-specific databases
CTD	56478.
GeneCards	GC22M031835.
H-InvDB	HIX0016395.
HGNC	HGNC:16687. EIF4ENIF1.
HPA	HPA001619. HPA002078.
MIM	607445. gene.
neXtProt	NX_Q9NRA8.
PharmGKB	PA38410.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG43453.
HOGENOM	HOG000232370.
HOVERGEN	HBG023298.
InParanoid	Q9NRA8.
OMA	PRIPSPI.
PhylomeDB	Q9NRA8.
Gene expression databases
ArrayExpress	Q9NRA8.
Bgee	Q9NRA8.
CleanEx	HS_EIF4ENIF1.
Genevestigator	Q9NRA8.
GermOnline	ENSG00000184708. Homo sapiens.
Family and domain databases
InterPro	IPR018862. eIF4E_transporter. [Graphical view]
Pfam	PF10477. EIF4E-T. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EIF4ENIF1. human.
GenomeRNAi	56478.
NextBio	62017.
SOURCE	Search...

Entry information

Entry name

4ET_HUMAN

Accession

Primary (citable) accession number: Q9NRA8
Secondary accession number(s): B1AKL2 , B2RBF1, Q8NCF2, Q9H708

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	August 2, 2002
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.