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P61326

- MGN_HUMAN

UniProt

P61326 - MGN_HUMAN

Protein

Protein mago nashi homolog

Gene

MAGOH

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

    Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator WIBG/PYM leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly.3 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-end processing Source: Reactome
    3. mRNA export from nucleus Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. mRNA splicing, via spliceosome Source: UniProtKB
    6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    7. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
    8. regulation of translation Source: UniProtKB-KW
    9. RNA metabolic process Source: Reactome
    10. RNA splicing Source: Reactome
    11. termination of RNA polymerase II transcription Source: Reactome
    12. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Biological processi

    mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, Translation regulation, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Protein family/group databases

    TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein mago nashi homolog
    Gene namesi
    Name:MAGOH
    Synonyms:MAGOHA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6815. MAGOH.

    Subcellular locationi

    Nucleus 1 Publication. Nucleus speckle 1 Publication. Cytoplasm 1 Publication
    Note: Detected in granule-like structures in the dendroplasm By similarity. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.By similarity

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytosol Source: Reactome
    3. exon-exon junction complex Source: UniProtKB
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 172KF → EA: Impaired nonsense-mediated decay activity.
    Mutagenesisi41 – 422KN → DA: Complete loss of nonsense-mediated decay activity.
    Mutagenesisi66 – 683DSE → RSR: Slightly reduced nonsense-mediated decay activity.
    Mutagenesisi68 – 681E → R: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-72; K-73 and R-117. 1 Publication
    Mutagenesisi72 – 732ED → RK: Fully active. 1 Publication
    Mutagenesisi72 – 721E → R: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-68; K-73 and R-117. 1 Publication
    Mutagenesisi73 – 731D → K: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-68; R-72 and R-117. 1 Publication
    Mutagenesisi85 – 873RQE → EQR: Fully active.
    Mutagenesisi117 – 1171E → R: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-68; R-72 and K-73. 1 Publication
    Mutagenesisi130 – 1345KCLVF → ECLVA: Complete loss of nonsense-mediated decay activity.
    Mutagenesisi136 – 1361L → R: Complete loss of nonsense-mediated decay activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA30563.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 146146Protein mago nashi homologPRO_0000174145Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP61326.
    PaxDbiP61326.
    PRIDEiP61326.

    PTM databases

    PhosphoSiteiP61326.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP61326.
    BgeeiP61326.
    CleanExiHS_MAGOH.
    GenevestigatoriP61326.

    Organism-specific databases

    HPAiCAB015425.
    HPA043036.
    HPA047754.

    Interactioni

    Subunit structurei

    Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with WIBG/PYM; the interaction is direct and dissociates the EJC from spliced mRNAs. Identified in the spliceosome C complex.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASC3O152345EBI-299134,EBI-299118
    EIF4A3P3891920EBI-299134,EBI-299104
    IPO13O948294EBI-299134,EBI-747310
    RBM8AQ9Y5S922EBI-299134,EBI-447231

    Protein-protein interaction databases

    BioGridi110290. 176 interactions.
    DIPiDIP-33069N.
    IntActiP61326. 129 interactions.
    MINTiMINT-1574804.
    STRINGi9606.ENSP00000360525.

    Structurei

    Secondary structure

    1
    146
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1511
    Beta strandi18 – 269
    Beta strandi30 – 389
    Turni40 – 423
    Beta strandi44 – 529
    Helixi54 – 6714
    Helixi69 – 713
    Beta strandi74 – 774
    Beta strandi85 – 928
    Beta strandi95 – 1017
    Helixi107 – 1104
    Beta strandi113 – 1153
    Helixi116 – 14126

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P27X-ray2.00A/C2-145[»]
    2HYIX-ray2.30A/G1-146[»]
    2J0QX-ray3.20C/F1-146[»]
    2J0SX-ray2.21C1-146[»]
    2XB2X-ray3.40C/Y1-146[»]
    3EX7X-ray2.30A/E1-146[»]
    ProteinModelPortaliP61326.
    SMRiP61326. Positions 2-145.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61326.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the mago nashi family.Curated

    Phylogenomic databases

    eggNOGiNOG255527.
    HOGENOMiHOG000207428.
    HOVERGENiHBG004353.
    InParanoidiP61326.
    KOiK12877.
    OMAiKEDDTNW.
    OrthoDBiEOG7F24VD.
    PhylomeDBiP61326.
    TreeFamiTF300128.

    Family and domain databases

    Gene3Di3.30.1560.10. 1 hit.
    InterProiIPR004023. Mago_nashi.
    [Graphical view]
    PANTHERiPTHR12638. PTHR12638. 1 hit.
    PfamiPF02792. Mago_nashi. 1 hit.
    [Graphical view]
    SUPFAMiSSF89817. SSF89817. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61326-1) [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

    MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA    50
    YVHKSVMEEL KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT 100
    TSKIGSLIDV NQSKDPEGLR VFYYLVQDLK CLVFSLIGLH FKIKPI 146
    Length:146
    Mass (Da):17,164
    Last modified:May 10, 2004 - v1
    Checksum:iFFAD0B075E045875
    GO
    Isoform 2 (identifier: P61326-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-86: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:109
    Mass (Da):12,844
    Checksum:iD232443C8370F0CF
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 8637Missing in isoform 2. 1 PublicationVSP_056246Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035940 mRNA. Translation: AAC39606.1.
    AF067173 mRNA. Translation: AAD32457.1.
    AK297895 mRNA. Translation: BAG60216.1.
    AK312113 mRNA. Translation: BAG35049.1.
    AL606760 Genomic DNA. Translation: CAI18914.1.
    CH471059 Genomic DNA. Translation: EAX06747.1.
    CH471059 Genomic DNA. Translation: EAX06748.1.
    BC018211 mRNA. Translation: AAH18211.1.
    CCDSiCCDS577.1.
    RefSeqiNP_002361.1. NM_002370.3.
    UniGeneiHs.421576.

    Genome annotation databases

    EnsembliENST00000371466; ENSP00000360521; ENSG00000162385.
    ENST00000371470; ENSP00000360525; ENSG00000162385.
    GeneIDi4116.
    KEGGihsa:4116.
    UCSCiuc001cvf.2. human.

    Polymorphism databases

    DMDMi47117708.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035940 mRNA. Translation: AAC39606.1 .
    AF067173 mRNA. Translation: AAD32457.1 .
    AK297895 mRNA. Translation: BAG60216.1 .
    AK312113 mRNA. Translation: BAG35049.1 .
    AL606760 Genomic DNA. Translation: CAI18914.1 .
    CH471059 Genomic DNA. Translation: EAX06747.1 .
    CH471059 Genomic DNA. Translation: EAX06748.1 .
    BC018211 mRNA. Translation: AAH18211.1 .
    CCDSi CCDS577.1.
    RefSeqi NP_002361.1. NM_002370.3.
    UniGenei Hs.421576.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P27 X-ray 2.00 A/C 2-145 [» ]
    2HYI X-ray 2.30 A/G 1-146 [» ]
    2J0Q X-ray 3.20 C/F 1-146 [» ]
    2J0S X-ray 2.21 C 1-146 [» ]
    2XB2 X-ray 3.40 C/Y 1-146 [» ]
    3EX7 X-ray 2.30 A/E 1-146 [» ]
    ProteinModelPortali P61326.
    SMRi P61326. Positions 2-145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110290. 176 interactions.
    DIPi DIP-33069N.
    IntActi P61326. 129 interactions.
    MINTi MINT-1574804.
    STRINGi 9606.ENSP00000360525.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei P61326.

    Polymorphism databases

    DMDMi 47117708.

    Proteomic databases

    MaxQBi P61326.
    PaxDbi P61326.
    PRIDEi P61326.

    Protocols and materials databases

    DNASUi 4116.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371466 ; ENSP00000360521 ; ENSG00000162385 .
    ENST00000371470 ; ENSP00000360525 ; ENSG00000162385 .
    GeneIDi 4116.
    KEGGi hsa:4116.
    UCSCi uc001cvf.2. human.

    Organism-specific databases

    CTDi 4116.
    GeneCardsi GC01M053692.
    HGNCi HGNC:6815. MAGOH.
    HPAi CAB015425.
    HPA043036.
    HPA047754.
    MIMi 602603. gene.
    neXtProti NX_P61326.
    PharmGKBi PA30563.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255527.
    HOGENOMi HOG000207428.
    HOVERGENi HBG004353.
    InParanoidi P61326.
    KOi K12877.
    OMAi KEDDTNW.
    OrthoDBi EOG7F24VD.
    PhylomeDBi P61326.
    TreeFami TF300128.

    Enzyme and pathway databases

    Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    ChiTaRSi MAGOH. human.
    EvolutionaryTracei P61326.
    GeneWikii MAGOH.
    GenomeRNAii 4116.
    NextBioi 16162.
    PROi P61326.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61326.
    Bgeei P61326.
    CleanExi HS_MAGOH.
    Genevestigatori P61326.

    Family and domain databases

    Gene3Di 3.30.1560.10. 1 hit.
    InterProi IPR004023. Mago_nashi.
    [Graphical view ]
    PANTHERi PTHR12638. PTHR12638. 1 hit.
    Pfami PF02792. Mago_nashi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF89817. SSF89817. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The mammalian homologue of mago nashi encodes a serum-inducible protein."
      Zhao X.F., Colaizzo-Anas T., Nowak N.J., Shows T.B., Elliott R.W., Aplan P.D.
      Genomics 47:319-322(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    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] (ISOFORMS 1 AND 2).
      Tissue: Thymus.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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] (ISOFORM 1).
      Tissue: Ovary.
    7. "MAGOH interacts with a novel RNA-binding protein."
      Zhao X.F., Nowak N.J., Shows T.B., Aplan P.D.
      Genomics 63:145-148(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM8A.
    8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    9. "A novel mode of RBD-protein recognition in the Y14-Mago complex."
      Fribourg S., Gatfield D., Izaurralde E., Conti E.
      Nat. Struct. Biol. 10:433-439(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBM8A.
    10. "Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex."
      Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.
      EMBO Rep. 5:304-310(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WIBG.
    11. "Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
      Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
      Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 16-LYS-GLU-17; 41-LYS-ASN-42; 66-ASP--GLU-68; 72-GLU-ASP-73; 85-ARG--GLU-87; 130-LYS--PHE-134 AND LEU-136.
    12. "The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity."
      Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.
      Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX.
    13. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
      Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
      RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs."
      Diem M.D., Chan C.C., Younis I., Dreyfuss G.
      Nat. Struct. Mol. Biol. 14:1173-1179(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WIBG.
    15. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Disassembly of exon junction complexes by PYM."
      Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.
      Cell 137:536-548(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WIBG, MUTAGENESIS OF GLU-68; GLU-72; ASP-73 AND GLU-117.
    17. "Assembly and mobility of exon-exon junction complexes in living cells."
      Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
      RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
      Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
      Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structure of the Y14-Magoh core of the exon junction complex."
      Lau C.K., Diem M.D., Dreyfuss G., Van Duyne G.D.
      Curr. Biol. 13:933-941(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RBM8A.
    22. "The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA."
      Bono F., Ebert J., Lorentzen E., Conti E.
      Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; EIF4A3; RBM8A AND AMP-PNP.
    23. "Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA."
      Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.
      Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; EIF4A3; RBM8A AND ADP-NP.
    24. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; EIF4A3; RBM8A AND TRANSITION STATE ANALOG ADP-ALF3.

    Entry informationi

    Entry nameiMGN_HUMAN
    AccessioniPrimary (citable) accession number: P61326
    Secondary accession number(s): B1ARP8
    , B2R5A2, O35169, P50606, Q5SW69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3