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P61326 (MGN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein mago nashi homolog
Gene names
Name:MAGOH
Synonyms:MAGOHA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.18

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm. 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. Ref.17

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the mago nashi family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
mRNA transport
Nonsense-mediated mRNA decay
Translation regulation
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   LigandRNA-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.8. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

exon-exon junction complex

Inferred from direct assay PubMed 16601204Ref.14Ref.16. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Protein mago nashi homolog
PRO_0000174145

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15 Ref.19 Ref.20

Experimental info

Mutagenesis16 – 172KF → EA: Impaired nonsense-mediated decay activity.
Mutagenesis41 – 422KN → DA: Complete loss of nonsense-mediated decay activity.
Mutagenesis66 – 683DSE → RSR: Slightly reduced nonsense-mediated decay activity. Ref.11 Ref.16
Mutagenesis681E → R: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-72; K-73 and R-117. Ref.16
Mutagenesis72 – 732ED → RK: Fully active. Ref.16
Mutagenesis721E → R: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-68; K-73 and R-117. Ref.16
Mutagenesis731D → K: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-68; R-72 and R-117. Ref.16
Mutagenesis85 – 873RQE → EQR: Fully active. Ref.11
Mutagenesis1171E → R: Abolishes interaction with WIBG/PYM leading to increase EJC association with splices mRNAs; when associated with R-68; R-72 and K-73. Ref.16
Mutagenesis130 – 1345KCLVF → ECLVA: Complete loss of nonsense-mediated decay activity. Ref.11
Mutagenesis1361L → R: Complete loss of nonsense-mediated decay activity. Ref.11

Secondary structure

.......................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61326 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: FFAD0B075E045875

FASTA14617,164
        10         20         30         40         50         60 
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL 

        70         80         90        100        110        120 
KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT TSKIGSLIDV NQSKDPEGLR 

       130        140 
VFYYLVQDLK CLVFSLIGLH FKIKPI 

« Hide

References

« Hide 'large scale' references
[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].
[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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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. expand/collapse author list , 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].
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mechanism of ATP turnover inhibition in the EJC."
Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K., Le Hir H., Andersen G.R.
RNA 15:67-75(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; EIF4A3; RBM8A AND TRANSITION STATE ANALOG ADP-ALF3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035940 mRNA. Translation: AAC39606.1.
AF067173 mRNA. Translation: AAD32457.1.
AK312113 mRNA. Translation: BAG35049.1.
AL606760 Genomic DNA. Translation: CAI18914.1.
CH471059 Genomic DNA. Translation: EAX06748.1.
BC018211 mRNA. Translation: AAH18211.1.
RefSeqNP_002361.1. NM_002370.3.
UniGeneHs.421576.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP61326.
SMRP61326. Positions 2-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110290. 172 interactions.
DIPDIP-33069N.
IntActP61326. 129 interactions.
MINTMINT-1574804.
STRING9606.ENSP00000360525.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteP61326.

Polymorphism databases

DMDM47117708.

Proteomic databases

PaxDbP61326.
PRIDEP61326.

Protocols and materials databases

DNASU4116.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371470; ENSP00000360525; ENSG00000162385.
GeneID4116.
KEGGhsa:4116.
UCSCuc001cvf.2. human.

Organism-specific databases

CTD4116.
GeneCardsGC01M053692.
HGNCHGNC:6815. MAGOH.
HPACAB015425.
HPA043036.
HPA047754.
MIM602603. gene.
neXtProtNX_P61326.
PharmGKBPA30563.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255527.
HOGENOMHOG000207428.
HOVERGENHBG004353.
InParanoidP61326.
KOK12877.
OMAKEDDTNW.
OrthoDBEOG7F24VD.
PhylomeDBP61326.
TreeFamTF300128.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressP61326.
BgeeP61326.
CleanExHS_MAGOH.
GenevestigatorP61326.

Family and domain databases

Gene3D3.30.1560.10. 1 hit.
InterProIPR004023. Mago_nashi.
[Graphical view]
PANTHERPTHR12638. PTHR12638. 1 hit.
PfamPF02792. Mago_nashi. 1 hit.
[Graphical view]
SUPFAMSSF89817. SSF89817. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAGOH. human.
EvolutionaryTraceP61326.
GeneWikiMAGOH.
GenomeRNAi4116.
NextBio16162.
PROP61326.
SOURCESearch...

Entry information

Entry nameMGN_HUMAN
AccessionPrimary (citable) accession number: P61326
Secondary accession number(s): B2R5A2 expand/collapse secondary AC list , O35169, P50606, Q5SW69
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM