Reviewed, UniProtKB/Swiss-Prot P61326 (MGN_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein mago nashi homolog

Gene names

Name:	MAGOH
Synonyms:	MAGOHA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Remains associated with the mRNA after its export to the cytoplasm and require translation of the mRNA for removal. The heterodimer MAGOH-RBM8A interacts with PYM that function to enhance the translation of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Ref.9 Ref.11
Subunit structure	Heterodimer with RBM8A. Part of the EJC core complex that contains CASC3, EIF4A3, MAGOH and RBM8A. Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, NCBP1, NCBP2, PNN, RBM8A, RNPS1, SRRM1, NXF1, SAP18, UPF3B, UPF2 and THOC4. Interacts with WIBG/PYM; the interaction is direct and leads to dissociate the EJC from spliced mRNAs. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Ref.9 Ref.7 Ref.10 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, THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the mago nashi family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Translation regulation Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus Spliceosome
Ligand	RNA-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell exon-exon junction complex Ref.14 Ref.16 Inferred from direct assay. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.7 Ref.14 Ref.16 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASC3	O15234	1	EBI-299134,EBI-299118
EIF4A3	P38919	2	EBI-299134,EBI-299104
RBM8A	Q9Y5S9	7	EBI-299134,EBI-447231
YWHAQ	P27348	1	EBI-299134,EBI-359854

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 146

146

Protein mago nashi homolog

PRO_0000174145

Amino acid modifications

Modified residue

1

1

N-acetylmethionine

Modified residue

114

1

N6-acetyllysine Ref.18

Experimental info

Mutagenesis

16 – 17

2

KF → EA: Impaired nonsense-mediated decay activity.

Mutagenesis

41 – 42

2

KN → DA: Complete loss of nonsense-mediated decay activity.

Mutagenesis

66 – 68

3

DSE → RSR: Slightly reduced nonsense-mediated decay activity. Ref.16

Mutagenesis

68

1

E → 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

Mutagenesis

72 – 73

2

ED → RK: Fully active. Ref.16

Mutagenesis

72

1

E → 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

Mutagenesis

73

1

D → 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

Mutagenesis

85 – 87

3

RQE → EQR: Fully active.

Mutagenesis

117

1

E → 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

Mutagenesis

130 – 134

5

KCLVF → ECLVA: Complete loss of nonsense-mediated decay activity.

Mutagenesis

136

1

L → R: Complete loss of nonsense-mediated decay activity. Ref.11

Secondary structure

1

.

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.

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146

Helix Strand Turn

Details...

Beta strand

5 – 15

11

Beta strand

18 – 26

9

Beta strand

30 – 38

9

Turn

40 – 42

3

Beta strand

44 – 52

9

Helix

54 – 67

14

Helix

69 – 71

3

Beta strand

85 – 92

8

Beta strand

95 – 101

7

Helix

107 – 110

4

Helix

116 – 141

26

Sequences

	Sequence		Length	Mass (Da)
	P61326-1 [UniParc]. Last modified May 10, 2004. Version 1. Checksum: FFAD0B075E045875	FASTA	146	17,164
	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

References

	« Hide 'large scale' referencesShow '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: 9479507] [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. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [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. , 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: 14702039] [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. , 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: 16710414] [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. , 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: 15489334] [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: 10662555] [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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL 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: 12730685] [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: 14968132] [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: 16209946] [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: 16170325] [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: 16314458] [Abstract] Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, 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: 18026120] [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[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: 19410547] [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: 19324961] [Abstract] Cited for: SUBCELLULAR LOCATION.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, MASS SPECTROMETRY.
[19]	"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: 12781131] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RBM8A.
[20]	"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: 16923391] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; EIF4A3; RBM8A AND AMP-PNP.
[21]	"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: 16931718] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3; EIF4A3; RBM8A AND ADP-NP.
[22]	"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: 19033377] [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

EMBLGenBankDDBJ

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.

IPI

IPI00219306.

RefSeq

NP_002361.1.

UniGene

Hs.421576

3D structure databases

PDBPDBe

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	[»]
3EX7	X-ray	2.30	A/E	1-146	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P61326. 17 interactions.

STRING

P61326.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

P61326.

Proteomic databases

PRIDE

P61326.

Genome annotation databases

Ensembl

ENST00000371470; ENSP00000360525; ENSG00000162385; Homo sapiens. [Genome view]

GeneID

4116.

KEGG

hsa:4116.

UCSC

uc001cvf.1. human.

Organism-specific databases

CTD

4116.

GeneCards

GC01M053404.

H-InvDB

HIX0000596.

HGNC

HGNC:6815. MAGOH.

HPA

CAB015425.

MIM

602603. gene.

PharmGKB

PA30563.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P61326.

HOVERGEN

P61326.

OMA

VIGEHIS

Enzyme and pathway databases

Reactome

REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P61326.

Bgee

P61326.

CleanEx

HS_MAGOH.

Genevestigator

P61326.

GermOnline

ENSG00000162385. Homo sapiens.

Family and domain databases

InterPro

IPR004023. Mago_nashi.
[Graphical view]

Gene3D

G3DSA:3.30.1560.10. Mago_nashi. 1 hit.

PANTHER

PTHR12638. Mago_nashi. 1 hit.

Pfam

PF02792. Mago_nashi. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16162.

SOURCE

Search...

Entry information

Entry name

MGN_HUMAN

Accession

Primary (citable) accession number: P61326
Secondary accession number(s): B2R5A2 , O35169, P50606, Q5SW69

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	November 24, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.