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MSN

Identity

Other namesmoesin (membrane-organising extension spike protein)
HGNC (Hugo) MSN
Location Xq11
Location_base_pair Starts at 64804236 and ends at 64878518 bp from pter ( according to hg18-Mar_2006)  [Mapping]

DNA/RNA

Transcription 3879 bp mRNA with a 1733 bp of coding sequence

Protein

Description 576 amino acids, 75 kDa; contains in N-term a globular membrane binding domain (band 4.1 like domain (amino acids 57 to 224), known also as the four-point-one/ezrin/radixin/moesin domai, an alpha helix domain, and in C-term a domain which interact with actin filaments
Expression wide; expressed differentially in microvilli and cell adhesion sites
Function cytoskeleton protein; binds to the plasma membrane and interacts with actin/myosin; role in cell-cell recognition and signaling
Homology Ezrin, radixin, moesin are called the ERM proteins; they are members ofthe band 4.1 superfamily

Implicated in

Entity t(X;2)(q11;p23) --> MSN- ALK
Disease found in a case of ALK+ anaplasic large cell lymphoma
Abnormal Protein 1005 amino acids, 125 kDa; membrane restricted; ;448 N-term amino acid from MSN, containing the band 4.1 like domain and most of the alpha helix domain, fused to the 557 (instead of the usual 562) C-term amino acids from ALK (i.e. the cytoplasmic portion of ALK with the tyrosine kinase domain).
Oncogenesis tyrosine kinase activity.
  

External links

Nomenclature
HGNC (Hugo)MSN   7373
Entrez_Gene (NCBI)MSN  4478  moesin
Cards
AtlasMSNID363
GeneCards (Weizmann)MSN
Ensembl (Hinxton)ENSG00000147065 [Gene_View]  MSN [Vega]
AceView (NCBI)MSN
Genatlas (Paris)MSN
euGene (Indiana)4478
SOURCE (Stanford)NM_002444
Genomic and cartography
GoldenPath (UCSC)MSN  -  Xq11   chrX:64804236-64878518 +  Xq11.1   [Description]    (hg18-Mar_2006)
EnsemblMSN - Xq11.1 [CytoView]
Mapping of homologs : NCBIMSN [Mapview]
OMIM309845   
Gene and transcription
Gene : Genbank (Entrez)AK297165 AK308486 AK309986 BC001112 BC011827
Reference sequence (RefSeq transcript) :SRSNM_002444
Reference transcript : EntrezNM_002444
RefSeq genomic : SRSAC_000066 AC_000155 NC_000023 NT_011669 NW_001842373 NW_927711
RefSeq genomic : EntrezAC_000066 AC_000155 NC_000023 NT_011669 NW_001842373 NW_927711
Consensus coding sequences : CCDS NCBIMSN
Cluster EST : UnigeneHs.87752 [ SRS ] Hs.87752 [ NCBI ]
Alternative Splicing : Fast-db (Paris)9640
Protein : pattern, domain, 3D structure
Protein : UniProt/SwissProtP26038 (SRS) P26038 (Expasy) P26038 (Uniprot)
With graphics : InterProP26038
Splice isoforms : VarSplice FASTAP26038(VarSplice FASTA)
Domaine pattern : Prosite (SRS)FERM_1 (PS00660)    FERM_2 (PS00661)    FERM_3 (PS50057)   
Domain pattern : Prosite (Expaxy)FERM_1 (PS00660)    FERM_2 (PS00661)    FERM_3 (PS50057)   
Domains : Interpro (SRS)Band_4.1_N    ERM    ERM_C    Ez/rad/moesin    FERM/acyl-CoA_bd_prot_3-hlx    PH_type   
Domains : Interpro (EBI)Band_4.1_N    ERM    ERM_C    Ez/rad/moesin    FERM/acyl-CoA_bd_prot_3-hlx    PH_type   
Related proteins : CluSTrP26038
Domain families : Pfam SRSBand_41 (PF00373)    ERM (PF00769)   
Domain families : Pfam SangerBand_41 (PF00373)    ERM (PF00769)   
Domain families : Pfam NCBIpfam00373    pfam00769   
Domain families : Smart EMBLB41 (SM00295)
Blocks (Seattle)P26038
Crystal structure of protein : PDB SRS1E5W    1EF1    1SGH   
Crystal structure of protein : PDBSum1E5W    1EF1    1SGH   
Crystal structure of protein : IMB1E5W    1EF1    1SGH   
Crystal structure of protein : PDB RSDB1E5W    1EF1    1SGH   
HPRD02399
Protein Interaction databases
DIP (DOE-UCLA)P26038
IntAct (EBI)P26038
Polymorphism : SNP, mutations, diseases
Single Nucleotide Polymorphism (SNP) : dbSNP NCBIMSN
SNP : GeneSNP UtahMSN
SNP : HGBaseMSN
Genetic variants : HAPMAPMSN
Somatic Mutations in Cancer : COSMICMSN 
Translocation Breakpoints in Cancer : TICdbMSN 
Mutations and Diseases : HGMDMSN
Hereditary diseases : OMIM309845   
Hereditary diseases : GENETests309845   
Diseases : Genetic AssociationMSN
General knowledge
Homologs : HomoloGeneMSN
Homology/Alignments : Family Browser UCSCMSN
Phylogenetic Trees/Animal Genes : TreeFamMSN
Chemical/Protein Interactions : CTD4478
Keywords Ontology : AmiGOuropod  receptor binding  structural constituent of cytoskeleton  cytoplasm  cytoskeleton  plasma membrane  microvillus  cell motion  leukocyte adhesion  cytoskeletal protein binding  basolateral plasma membrane  apical plasma membrane  extrinsic to membrane  membrane to membrane docking  filopodium  cell adhesion molecule binding  leukocyte migration  
Keywords Ontology : EGO-EBIuropod  receptor binding  structural constituent of cytoskeleton  cytoplasm  cytoskeleton  plasma membrane  microvillus  cell motion  leukocyte adhesion  cytoskeletal protein binding  basolateral plasma membrane  apical plasma membrane  extrinsic to membrane  membrane to membrane docking  filopodium  cell adhesion molecule binding  leukocyte migration  
Pathways : BIOCARTA
Pathways : KEGGLeukocyte transendothelial migrationRegulation of actin cytoskeleton
Other databases
Probes
Probes : ImagenesMSN Related clones (RZPD - Berlin)
Literature
PubMed73 Pubmed reference(s) in Entrez
PubGeneMSN

Bibliography

Moesin: a member of the protein 4.1-talin-ezrin family of proteins.
Lankes WT, Furthmayr H
Proceedings of the National Academy of Sciences of the United States of America. 1991 ; 88 (19) : 8297-8301.
PMID 1924289
 
Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells.
Berryman M, Franck Z, Bretscher A
Journal of cell science. 1993 ; 105 ( Pt 4) : 1025-1043.
PMID 8227193
 
The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.
Chishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, Chasis JA, Conboy JG, Gascard P, Takakuwa Y, Huang SC, Benz EJ Jr, Bretscher A, Fehon RG, Gusella JF, Ramesh V, Solomon F, Marchesi VT, Tsukita S, Tsukita S, Hoover KB
Trends in biochemical sciences. 1998 ; 23 (8) : 281-282.
PMID 9757824
 
Regulation of cortical structure by the ezrin-radixin-moesin protein family.
Bretscher A
Current opinion in cell biology. 1999 ; 11 (1) : 109-116.
PMID 10047517
 
ERM proteins in cell adhesion and membrane dynamics.
Mangeat P, Roy C, Martin M
Trends in cell biology. 1999 ; 9 (5) : 187-192.
PMID 10322453
 
Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins.
Tsukita S, Yonemura S
The Journal of biological chemistry. 1999 ; 274 (49) : 34507-34510.
PMID 10574907
 
Molecular characterization of a new ALK translocation involving moesin (MSN-ALK) in anaplastic large cell lymphoma.
Tort F, Pinyol M, Pulford K, Roncador G, Hernandez L, Nayach I, Kluin-Nelemans HC, Kluin P, Touriol C, Delsol G, Mason D, Campo E
Laboratory investigation; a journal of technical methods and pathology. 2001 ; 81 (3) : 419-426.
PMID 11310834
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written08-2001Jean-Loup Huret

Citation

This paper should be referenced as such :
Huret JL . MSN. Atlas Genet Cytogenet Oncol Haematol. August 2001 .
URL : http://AtlasGeneticsOncology.org/Genes/MSNID363.html

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indexed on : Sat Jun 27 16:41:43 CEST 2009

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