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Protein

Protein mago nashi homolog

Gene

MAGOH

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

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

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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_387. Cleavage of Growing Transcript in the Termination Region.
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6815. MAGOH.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytosol Source: Reactome
  • exon-exon junction complex Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 172KF → EA: Impaired nonsense-mediated decay activity. 1 Publication
Mutagenesisi41 – 422KN → DA: Complete loss of nonsense-mediated decay activity. 1 Publication
Mutagenesisi66 – 683DSE → RSR: Slightly reduced nonsense-mediated decay activity. 1 Publication
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. 1 Publication
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. 1 Publication
Mutagenesisi136 – 1361L → R: Complete loss of nonsense-mediated decay activity. 1 Publication

Organism-specific databases

PharmGKBiPA30563.

Polymorphism and mutation databases

BioMutaiMAGOH.
DMDMi47117708.

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

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
GOLGA2Q083793EBI-299134,EBI-618309
IPO13O948294EBI-299134,EBI-747310
RBM8AQ9Y5S925EBI-299134,EBI-447231
TADA2AO754783EBI-299134,EBI-742268

Protein-protein interaction databases

BioGridi110290. 186 interactions.
DIPiDIP-33069N.
IntActiP61326. 131 interactions.
MINTiMINT-1574804.
STRINGi9606.ENSP00000360525.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000003156.
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. AlignAdd to basket

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

        10         20         30         40         50
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA
60 70 80 90 100
YVHKSVMEEL KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT
110 120 130 140
TSKIGSLIDV NQSKDPEGLR VFYYLVQDLK CLVFSLIGLH FKIKPI
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:
EMBLi
GenBanki
DDBJi
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. [P61326-1]
RefSeqiNP_002361.1. NM_002370.3. [P61326-1]
UniGeneiHs.421576.

Genome annotation databases

EnsembliENST00000371466; ENSP00000360521; ENSG00000162385. [P61326-2]
ENST00000371470; ENSP00000360525; ENSG00000162385. [P61326-1]
GeneIDi4116.
KEGGihsa:4116.
UCSCiuc001cvf.2. human. [P61326-1]
uc010ont.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P61326-1]
RefSeqiNP_002361.1. NM_002370.3. [P61326-1]
UniGeneiHs.421576.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110290. 186 interactions.
DIPiDIP-33069N.
IntActiP61326. 131 interactions.
MINTiMINT-1574804.
STRINGi9606.ENSP00000360525.

Protein family/group databases

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

PTM databases

PhosphoSiteiP61326.

Polymorphism and mutation databases

BioMutaiMAGOH.
DMDMi47117708.

Proteomic databases

MaxQBiP61326.
PaxDbiP61326.
PRIDEiP61326.

Protocols and materials databases

DNASUi4116.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371466; ENSP00000360521; ENSG00000162385. [P61326-2]
ENST00000371470; ENSP00000360525; ENSG00000162385. [P61326-1]
GeneIDi4116.
KEGGihsa:4116.
UCSCiuc001cvf.2. human. [P61326-1]
uc010ont.2. human.

Organism-specific databases

CTDi4116.
GeneCardsiGC01M053692.
HGNCiHGNC:6815. MAGOH.
HPAiCAB015425.
HPA043036.
HPA047754.
MIMi602603. gene.
neXtProtiNX_P61326.
PharmGKBiPA30563.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255527.
GeneTreeiENSGT00390000003156.
HOGENOMiHOG000207428.
HOVERGENiHBG004353.
InParanoidiP61326.
KOiK12877.
OMAiKEDDTNW.
OrthoDBiEOG7F24VD.
PhylomeDBiP61326.
TreeFamiTF300128.

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiMAGOH. human.
EvolutionaryTraceiP61326.
GeneWikiiMAGOH.
GenomeRNAii4116.
NextBioi16162.
PROiP61326.
SOURCEiSearch...

Gene expression databases

BgeeiP61326.
CleanExiHS_MAGOH.
GenevestigatoriP61326.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 132 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

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.