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

Names and origin

Protein names

Recommended name:
    Eukaryotic translation initiation factor 4E transporter
      Short name=eIF4E transporter
      Short name=4E-T
Alternative name(s):
    Eukaryotic translation initiation factor 4E nuclear import factor 1

Gene names

Name:

EIF4ENIF1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner.
Tissue specificity	Widely expressed.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.1 Inferred from direct assay. Source: HPA
Molecular function	protein binding Ref.1 Inferred from physical interaction. Source: IntAct protein transporter activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4E	P06730	1	EBI-301024,EBI-73440
EIF4E2	O60573	2	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.12
	Modified residue	74	1	Phosphoserine Ref.8
	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	345	1	Phosphoserine Ref.9
	Modified residue	486	1	N6-acetyllysine Ref.13
	Modified residue	564	1	Phosphoserine Ref.9 Ref.11 Ref.12
	Modified residue	587	1	Phosphoserine Ref.12
	Modified residue	693	1	Phosphoserine Ref.12
	Modified residue	914	1	Phosphoserine Ref.7
	Modified residue	920	1	Phosphoserine Ref.7
	Modified residue	951	1	Phosphoserine Ref.9 Ref.12
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. 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: 10856257] [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: 15461802] [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: 14702039] [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: 10591208] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Testis.
[7]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-914 AND SER-920, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-136; SER-138; SER-345; SER-564 AND SER-951, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, MASS SPECTROMETRY.
[12]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-564; SER-587; SER-693 AND SER-951, MASS SPECTROMETRY. Tissue: T-cell.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, MASS SPECTROMETRY.
+	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. NP_001157974.1. NP_062817.2.
UniGene	Hs.517559
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRA8. 9 interactions.
STRING	Q9NRA8.
PTM databases
PhosphoSite	Q9NRA8.
Proteomic databases
PRIDE	Q9NRA8.
Genome annotation databases
Ensembl	ENST00000330125; ENSP00000328103; ENSG00000184708; Homo sapiens. [Genome view] ENST00000397525; ENSP00000380659; ENSG00000184708; Homo sapiens. [Genome view] ENST00000420671; ENSP00000409372; ENSG00000184708; Homo sapiens. [Genome view]
GeneID	56478.
KEGG	hsa:56478.
UCSC	uc003akx.1. human. uc003akz.1. human.
Organism-specific databases
CTD	56478.
GeneCards	GC22M030159.
HGNC	HGNC:16687. EIF4ENIF1.
HPA	HPA001619. HPA002078.
MIM	607445. gene.
PharmGKB	PA38410.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15714.
HOGENOM	HBG267574.
HOVERGEN	Q9NRA8.
InParanoid	Q9NRA8.
OMA	GRKTPTL.
OrthoDB	EOG9VQD7M.
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 Resources
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:	January 19, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.