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Q9NRA8

- 4ET_HUMAN

UniProt

Q9NRA8 - 4ET_HUMAN

Protein

Eukaryotic translation initiation factor 4E transporter

Gene

EIF4ENIF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (02 Aug 2002)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein transporter activity Source: ProtInc

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:16687. EIF4ENIF1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. NucleusPML body 1 Publication. Nucleus speckle 1 Publication
    Note: Predominantly cytoplasmic. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Localization to nuclear foci and speckles requires active transcription.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Ensembl
    3. intracellular membrane-bounded organelle Source: HPA
    4. membrane Source: UniProtKB
    5. nuclear speck Source: UniProtKB-SubCell
    6. nucleus Source: ProtInc
    7. PML body Source: UniProtKB-SubCell

    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.

    Organism-specific databases

    Orphaneti619. Primary ovarian failure.
    PharmGKBiPA38410.

    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 – 51Phosphoserine3 Publications
    Modified residuei120 – 1201Phosphoserine2 Publications
    Modified residuei136 – 1361Phosphoserine2 Publications
    Modified residuei138 – 1381Phosphoserine2 Publications
    Modified residuei301 – 3011Phosphoserine2 Publications
    Modified residuei345 – 3451Phosphoserine2 Publications
    Modified residuei486 – 4861N6-acetyllysine1 Publication
    Modified residuei513 – 5131Phosphoserine2 Publications
    Modified residuei564 – 5641Phosphoserine4 Publications
    Modified residuei587 – 5871Phosphoserine2 Publications
    Modified residuei693 – 6931Phosphoserine2 Publications
    Modified residuei920 – 9201Phosphoserine2 Publications
    Modified residuei951 – 9511Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRA8.
    PaxDbiQ9NRA8.
    PRIDEiQ9NRA8.

    PTM databases

    PhosphoSiteiQ9NRA8.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ9NRA8.
    BgeeiQ9NRA8.
    CleanExiHS_EIF4ENIF1.
    GenevestigatoriQ9NRA8.

    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.
    EIF4EP067306EBI-301024,EBI-73440
    EIF4E2O605733EBI-301024,EBI-398610

    Protein-protein interaction databases

    BioGridi121148. 10 interactions.
    IntActiQ9NRA8. 15 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.
    HOGENOMiHOG000232370.
    HOVERGENiHBG023298.
    InParanoidiQ9NRA8.
    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. Align

    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

    MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC    50
    LSEKYDSDGV WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVD 100
    PRERVKEDDL DVVLSPQRRS FGGGCHVTAA VSSRRSGSPL EKDSDGLRLL 150
    GGRRIGSGRI ISARTFEKDH RLSDKDLRDL RDRDRERDFK DKRFRREFGD 200
    SKRVFGERRR NDSYTEEEPE WFSAGPTSQS ETIELTGFDD KILEEDHKGR 250
    KRTRRRTASV KEGIVECNGG VAEEDEVEVI LAQEPAADQE VPRDAVLPEQ 300
    SPGDFDFNEF FNLDKVPCLA SMIEDVLGEG SVSASRFSRW FSNPSRSGSR 350
    SSSLGSTPHE ELERLAGLEQ AILSPGQNSG NYFAPIPLED HAENKVDILE 400
    MLQKAKVDLK PLLSSLSANK EKLKESSHSG VVLSVEEVEA GLKGLKVDQQ 450
    VKNSTPFMAE HLEETLSAVT NNRQLKKDGD MTAFNKLVST MKASGTLPSQ 500
    PKVSRNLESH LMSPAEIPGQ PVPKNILQEL LGQPVQRPAS SNLLSGLMGS 550
    LEPTTSLLGQ RAPSPPLSQV FQTRAASADY LRPRIPSPIG FTPGPQQLLG 600
    DPFQGMRKPM SPITAQMSQL ELQQAALEGL ALPHDLAVQA ANFYQPGFGK 650
    PQVDRTRDGF RNRQQRVTKS PAPVHRGNSS SPAPAASITS MLSPSFTPTS 700
    VIRKMYESKE KSKEEPASGK AALGDSKEDT QKASEENLLS SSSVPSADRD 750
    SSPTTNSKLS ALQRSSCSTP LSQANRYTKE QDYRPKATGR KTPTLASPVP 800
    TTPFLRPVHQ VPLVPHVPMV RPAHQLHPGL VQRMLAQGVH PQHLPSLLQT 850
    GVLPPGMDLS HLQGISGPIL GQPFYPLPAA SHPLLNPRPG TPLHLAMVQQ 900
    QLQRSVLHPP GSGSHAAAVS VQTTPQNVPS RSGLPHMHSQ LEHRPSQRSS 950
    SPVGLAKWFG SDVLQQPLPS MPAKVISVDE LEYRQ 985
    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.
    The sequence BAC11194.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.517559.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi22095430.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13898.1. [Q9NRA8-1 ]
    CCDS54520.1. [Q9NRA8-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.517559.

    3D structure databases

    ProteinModelPortali Q9NRA8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121148. 10 interactions.
    IntActi Q9NRA8. 15 interactions.
    MINTi MINT-1956064.
    STRINGi 9606.ENSP00000328103.

    PTM databases

    PhosphoSitei Q9NRA8.

    Polymorphism databases

    DMDMi 22095430.

    Proteomic databases

    MaxQBi Q9NRA8.
    PaxDbi Q9NRA8.
    PRIDEi Q9NRA8.

    Protocols and materials databases

    DNASUi 56478.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330125 ; ENSP00000328103 ; ENSG00000184708 . [Q9NRA8-1 ]
    ENST00000344710 ; ENSP00000342927 ; ENSG00000184708 . [Q9NRA8-2 ]
    ENST00000397525 ; ENSP00000380659 ; ENSG00000184708 . [Q9NRA8-1 ]
    GeneIDi 56478.
    KEGGi hsa:56478.
    UCSCi uc003aky.2. human. [Q9NRA8-1 ]

    Organism-specific databases

    CTDi 56478.
    GeneCardsi GC22M031835.
    H-InvDB HIX0016395.
    HGNCi HGNC:16687. EIF4ENIF1.
    HPAi HPA001619.
    HPA002078.
    MIMi 607445. gene.
    neXtProti NX_Q9NRA8.
    Orphaneti 619. Primary ovarian failure.
    PharmGKBi PA38410.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43453.
    HOGENOMi HOG000232370.
    HOVERGENi HBG023298.
    InParanoidi Q9NRA8.
    OMAi HQVPLVP.
    OrthoDBi EOG7GFB42.
    PhylomeDBi Q9NRA8.
    TreeFami TF101531.

    Miscellaneous databases

    ChiTaRSi EIF4ENIF1. human.
    GeneWikii EIF4ENIF1.
    GenomeRNAii 56478.
    NextBioi 62017.
    PROi Q9NRA8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRA8.
    Bgeei Q9NRA8.
    CleanExi HS_EIF4ENIF1.
    Genevestigatori Q9NRA8.

    Family and domain databases

    InterProi IPR018862. eIF4E_transporter.
    [Graphical view ]
    Pfami PF10477. EIF4E-T. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 122 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