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Protein

Eukaryotic translation initiation factor 4E transporter

Gene

EIF4ENIF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Nucleoplasmic shuttling protein. Mediates the nuclear import of EIF4E by a piggy-back mechanism.

GO - Molecular functioni

  • mRNA binding Source: Ensembl
  • poly(A) RNA binding Source: UniProtKB
  • protein transporter activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
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 namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:16687. EIF4ENIF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytoplasmic mRNA processing body Source: Ensembl
  • cytosol Source: Ensembl
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: ProtInc
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301Y → A: Abolishes interaction with EIF4E. 1 Publication
Mutagenesisi195 – 1962RR → NS: Abolishes the nuclear localization. 1 Publication

Organism-specific databases

Orphaneti619. Primary ovarian failure.
PharmGKBiPA38410.

Polymorphism and mutation databases

BioMutaiEIF4ENIF1.
DMDMi22095430.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 985985Eukaryotic translation initiation factor 4E transporterPRO_0000064381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine2 Publications
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei136 – 1361Phosphoserine1 Publication
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei301 – 3011Phosphoserine1 Publication
Modified residuei345 – 3451Phosphoserine1 Publication
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei486 – 4861N6-acetyllysine1 Publication
Modified residuei513 – 5131Phosphoserine1 Publication
Modified residuei564 – 5641Phosphoserine3 Publications
Modified residuei587 – 5871Phosphoserine1 Publication
Modified residuei693 – 6931Phosphoserine1 Publication
Modified residuei920 – 9201Phosphoserine1 Publication
Modified residuei951 – 9511Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NRA8.
PaxDbiQ9NRA8.
PRIDEiQ9NRA8.

PTM databases

PhosphoSiteiQ9NRA8.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ9NRA8.
CleanExiHS_EIF4ENIF1.
ExpressionAtlasiQ9NRA8. baseline and differential.
GenevisibleiQ9NRA8. HS.

Organism-specific databases

HPAiHPA001619.
HPA002078.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX23EBI-301024,EBI-6863741From a different organism.
DDX6P261963EBI-301024,EBI-351257
DEF6Q9H4E73EBI-301024,EBI-745369
DTX2Q4ZH493EBI-301024,EBI-10192429
DTX2Q86UW94EBI-301024,EBI-740376
EFHC1Q5JVL46EBI-301024,EBI-743105
EIF4EP067309EBI-301024,EBI-73440
EIF4E2O605733EBI-301024,EBI-398610
FANCLQ9NW383EBI-301024,EBI-2339898
HNRNPFP525973EBI-301024,EBI-352986
KRT19P087273EBI-301024,EBI-742756
OIP5O434823EBI-301024,EBI-536879
TTC19Q6DKK23EBI-301024,EBI-948354
TXLNAP402223EBI-301024,EBI-359793

Protein-protein interaction databases

BioGridi121148. 23 interactions.
IntActiQ9NRA8. 25 interactions.
MINTiMINT-1956064.
STRINGi9606.ENSP00000328103.

Structurei

3D structure databases

ProteinModelPortaliQ9NRA8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 367EIF4E-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi195 – 21117Nuclear localization signalAdd
BLAST
Motifi438 – 44710Nuclear export signal
Motifi613 – 63826Nuclear export signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi148 – 21063Arg-richAdd
BLAST

Phylogenomic databases

eggNOGiNOG43453.
GeneTreeiENSGT00390000012071.
HOGENOMiHOG000232370.
HOVERGENiHBG023298.
InParanoidiQ9NRA8.
KOiK18728.
OMAiHQVPLVP.
OrthoDBiEOG7GFB42.
PhylomeDBiQ9NRA8.
TreeFamiTF101531.

Family and domain databases

InterProiIPR018862. eIF4E_transporter.
[Graphical view]
PfamiPF10477. EIF4E-T. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRA8-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC
60 70 80 90 100
LSEKYDSDGV WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVD
110 120 130 140 150
PRERVKEDDL DVVLSPQRRS FGGGCHVTAA VSSRRSGSPL EKDSDGLRLL
160 170 180 190 200
GGRRIGSGRI ISARTFEKDH RLSDKDLRDL RDRDRERDFK DKRFRREFGD
210 220 230 240 250
SKRVFGERRR NDSYTEEEPE WFSAGPTSQS ETIELTGFDD KILEEDHKGR
260 270 280 290 300
KRTRRRTASV KEGIVECNGG VAEEDEVEVI LAQEPAADQE VPRDAVLPEQ
310 320 330 340 350
SPGDFDFNEF FNLDKVPCLA SMIEDVLGEG SVSASRFSRW FSNPSRSGSR
360 370 380 390 400
SSSLGSTPHE ELERLAGLEQ AILSPGQNSG NYFAPIPLED HAENKVDILE
410 420 430 440 450
MLQKAKVDLK PLLSSLSANK EKLKESSHSG VVLSVEEVEA GLKGLKVDQQ
460 470 480 490 500
VKNSTPFMAE HLEETLSAVT NNRQLKKDGD MTAFNKLVST MKASGTLPSQ
510 520 530 540 550
PKVSRNLESH LMSPAEIPGQ PVPKNILQEL LGQPVQRPAS SNLLSGLMGS
560 570 580 590 600
LEPTTSLLGQ RAPSPPLSQV FQTRAASADY LRPRIPSPIG FTPGPQQLLG
610 620 630 640 650
DPFQGMRKPM SPITAQMSQL ELQQAALEGL ALPHDLAVQA ANFYQPGFGK
660 670 680 690 700
PQVDRTRDGF RNRQQRVTKS PAPVHRGNSS SPAPAASITS MLSPSFTPTS
710 720 730 740 750
VIRKMYESKE KSKEEPASGK AALGDSKEDT QKASEENLLS SSSVPSADRD
760 770 780 790 800
SSPTTNSKLS ALQRSSCSTP LSQANRYTKE QDYRPKATGR KTPTLASPVP
810 820 830 840 850
TTPFLRPVHQ VPLVPHVPMV RPAHQLHPGL VQRMLAQGVH PQHLPSLLQT
860 870 880 890 900
GVLPPGMDLS HLQGISGPIL GQPFYPLPAA SHPLLNPRPG TPLHLAMVQQ
910 920 930 940 950
QLQRSVLHPP GSGSHAAAVS VQTTPQNVPS RSGLPHMHSQ LEHRPSQRSS
960 970 980
SPVGLAKWFG SDVLQQPLPS MPAKVISVDE LEYRQ
Length:985
Mass (Da):108,201
Last modified:August 2, 2002 - v2
Checksum:i4C898E0488903C04
GO
Isoform 2 (identifier: Q9NRA8-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:811
Mass (Da):88,226
Checksum:iB93D3AE24B15E7C0
GO
Isoform 3 (identifier: Q9NRA8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     616-616: Q → QQ

Note: No experimental confirmation available.
Show »
Length:986
Mass (Da):108,329
Checksum:iCBED6CC9160D72C0
GO

Sequence cautioni

The sequence BAB15092.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC11194.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141L → F in AAF81693 (PubMed:10856257).Curated
Sequence conflicti825 – 8251Q → R in AAH33028 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei100 – 262163Missing in isoform 2. 1 PublicationVSP_003783Add
BLAST
Alternative sequencei493 – 50412Missing in isoform 2. 1 PublicationVSP_003784Add
BLAST
Alternative sequencei616 – 6161Q → QQ in isoform 2 and isoform 3. 2 PublicationsVSP_047042

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13898.1. [Q9NRA8-1]
CCDS54520.1. [Q9NRA8-2]
RefSeqiNP_001157973.1. NM_001164501.1. [Q9NRA8-1]
NP_001157974.1. NM_001164502.1. [Q9NRA8-2]
NP_062817.2. NM_019843.3. [Q9NRA8-1]
XP_005261743.1. XM_005261686.1. [Q9NRA8-3]
XP_005261744.1. XM_005261687.1. [Q9NRA8-3]
XP_005261745.1. XM_005261688.1. [Q9NRA8-3]
XP_006724344.2. XM_006724281.2. [Q9NRA8-3]
XP_011528582.1. XM_011530280.1. [Q9NRA8-1]
XP_011528583.1. XM_011530281.1. [Q9NRA8-3]
UniGeneiHs.517559.

Genome annotation databases

EnsembliENST00000330125; ENSP00000328103; ENSG00000184708.
ENST00000344710; ENSP00000342927; ENSG00000184708. [Q9NRA8-2]
ENST00000397525; ENSP00000380659; ENSG00000184708.
GeneIDi56478.
KEGGihsa:56478.
UCSCiuc003aky.2. human. [Q9NRA8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13898.1. [Q9NRA8-1]
CCDS54520.1. [Q9NRA8-2]
RefSeqiNP_001157973.1. NM_001164501.1. [Q9NRA8-1]
NP_001157974.1. NM_001164502.1. [Q9NRA8-2]
NP_062817.2. NM_019843.3. [Q9NRA8-1]
XP_005261743.1. XM_005261686.1. [Q9NRA8-3]
XP_005261744.1. XM_005261687.1. [Q9NRA8-3]
XP_005261745.1. XM_005261688.1. [Q9NRA8-3]
XP_006724344.2. XM_006724281.2. [Q9NRA8-3]
XP_011528582.1. XM_011530280.1. [Q9NRA8-1]
XP_011528583.1. XM_011530281.1. [Q9NRA8-3]
UniGeneiHs.517559.

3D structure databases

ProteinModelPortaliQ9NRA8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121148. 23 interactions.
IntActiQ9NRA8. 25 interactions.
MINTiMINT-1956064.
STRINGi9606.ENSP00000328103.

PTM databases

PhosphoSiteiQ9NRA8.

Polymorphism and mutation databases

BioMutaiEIF4ENIF1.
DMDMi22095430.

Proteomic databases

MaxQBiQ9NRA8.
PaxDbiQ9NRA8.
PRIDEiQ9NRA8.

Protocols and materials databases

DNASUi56478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330125; ENSP00000328103; ENSG00000184708.
ENST00000344710; ENSP00000342927; ENSG00000184708. [Q9NRA8-2]
ENST00000397525; ENSP00000380659; ENSG00000184708.
GeneIDi56478.
KEGGihsa:56478.
UCSCiuc003aky.2. human. [Q9NRA8-1]

Organism-specific databases

CTDi56478.
GeneCardsiGC22M031835.
H-InvDBHIX0016395.
HGNCiHGNC:16687. EIF4ENIF1.
HPAiHPA001619.
HPA002078.
MIMi607445. gene.
neXtProtiNX_Q9NRA8.
Orphaneti619. Primary ovarian failure.
PharmGKBiPA38410.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43453.
GeneTreeiENSGT00390000012071.
HOGENOMiHOG000232370.
HOVERGENiHBG023298.
InParanoidiQ9NRA8.
KOiK18728.
OMAiHQVPLVP.
OrthoDBiEOG7GFB42.
PhylomeDBiQ9NRA8.
TreeFamiTF101531.

Miscellaneous databases

GeneWikiiEIF4ENIF1.
GenomeRNAii56478.
NextBioi62017.
PROiQ9NRA8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRA8.
CleanExiHS_EIF4ENIF1.
ExpressionAtlasiQ9NRA8. baseline and differential.
GenevisibleiQ9NRA8. HS.

Family and domain databases

InterProiIPR018862. eIF4E_transporter.
[Graphical view]
PfamiPF10477. EIF4E-T. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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] (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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. 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. 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.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-951, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry namei4ET_HUMAN
AccessioniPrimary (citable) accession number: Q9NRA8
Secondary accession number(s): B1AKL2
, B1AKL3, B2RBF1, Q8NCF2, Q9H708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: July 22, 2015
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.