Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

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

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length985 AA.
Sequence statusComplete.
Protein existenceEvidence 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. NucleusPML 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.16

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9WMX23EBI-301024,EBI-6863741From a different organism.
EIF4EP067306EBI-301024,EBI-73440
EIF4E2O605733EBI-301024,EBI-398610

Alternative products

This entry describes 3 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.
     616-616: Q → QQ
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NRA8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     616-616: Q → QQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 985985Eukaryotic translation initiation factor 4E transporter
PRO_0000064381

Regions

Region30 – 367EIF4E-binding
Motif195 – 21117Nuclear localization signal
Motif438 – 44710Nuclear export signal
Motif613 – 63826Nuclear export signal
Compositional bias148 – 21063Arg-rich

Amino acid modifications

Modified residue51Phosphoserine Ref.11 Ref.13
Modified residue1201Phosphoserine Ref.9
Modified residue1361Phosphoserine Ref.9
Modified residue1381Phosphoserine Ref.9
Modified residue3011Phosphoserine Ref.13
Modified residue3451Phosphoserine Ref.9
Modified residue4861N6-acetyllysine Ref.12
Modified residue5131Phosphoserine Ref.13
Modified residue5641Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue5871Phosphoserine Ref.11
Modified residue6931Phosphoserine Ref.11
Modified residue9201Phosphoserine Ref.8
Modified residue9511Phosphoserine Ref.9 Ref.13 Ref.15

Natural variations

Alternative sequence100 – 262163Missing in isoform 2.
VSP_003783
Alternative sequence493 – 50412Missing in isoform 2.
VSP_003784
Alternative sequence6161Q → QQ in isoform 2 and isoform 3.
VSP_047042

Experimental info

Mutagenesis301Y → A: Abolishes interaction with EIF4E. Ref.1
Mutagenesis195 – 1962RR → NS: Abolishes the nuclear localization.
Sequence conflict1141L → F in AAF81693. Ref.1
Sequence conflict8251Q → R in AAH33028. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: 4C898E0488903C04

FASTA985108,201
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B93D3AE24B15E7C0
Show »

FASTA81188,226
Isoform 3 [UniParc].

Checksum: CBED6CC9160D72C0
Show »

FASTA986108,329

References

« Hide '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. expand/collapse author list , 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] (ISOFORM 3).
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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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. No translation available.
CH471095 Genomic DNA. Translation: EAW59977.1.
BC032941 mRNA. Translation: AAH32941.1.
BC033028 mRNA. Translation: AAH33028.1.
RefSeqNP_001157973.1. NM_001164501.1.
NP_001157974.1. NM_001164502.1.
NP_062817.2. NM_019843.3.
XP_005261743.1. XM_005261686.1.
XP_005261744.1. XM_005261687.1.
XP_005261745.1. XM_005261688.1.
UniGeneHs.517559.

3D structure databases

ProteinModelPortalQ9NRA8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121148. 10 interactions.
IntActQ9NRA8. 15 interactions.
MINTMINT-1956064.
STRING9606.ENSP00000328103.

PTM databases

PhosphoSiteQ9NRA8.

Polymorphism databases

DMDM22095430.

Proteomic databases

PaxDbQ9NRA8.
PRIDEQ9NRA8.

Protocols and materials databases

DNASU56478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330125; ENSP00000328103; ENSG00000184708. [Q9NRA8-1]
ENST00000344710; ENSP00000342927; ENSG00000184708. [Q9NRA8-2]
ENST00000397525; ENSP00000380659; ENSG00000184708. [Q9NRA8-1]
GeneID56478.
KEGGhsa:56478.
UCSCuc003aky.2. human. [Q9NRA8-1]

Organism-specific databases

CTD56478.
GeneCardsGC22M031835.
H-InvDBHIX0016395.
HGNCHGNC:16687. EIF4ENIF1.
HPAHPA001619.
HPA002078.
MIM607445. gene.
neXtProtNX_Q9NRA8.
Orphanet619. Primary ovarian failure.
PharmGKBPA38410.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43453.
HOGENOMHOG000232370.
HOVERGENHBG023298.
InParanoidQ9NRA8.
OMASMPAKVI.
OrthoDBEOG7GFB42.
PhylomeDBQ9NRA8.
TreeFamTF101531.

Gene expression databases

ArrayExpressQ9NRA8.
BgeeQ9NRA8.
CleanExHS_EIF4ENIF1.
GenevestigatorQ9NRA8.

Family and domain databases

InterProIPR018862. eIF4E_transporter.
[Graphical view]
PfamPF10477. EIF4E-T. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4ENIF1. human.
GeneWikiEIF4ENIF1.
GenomeRNAi56478.
NextBio62017.
PROQ9NRA8.
SOURCESearch...

Entry information

Entry name4ET_HUMAN
AccessionPrimary (citable) accession number: Q9NRA8
Secondary accession number(s): B1AKL2 expand/collapse secondary AC list , B1AKL3, B2RBF1, Q8NCF2, Q9H708
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM