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MSN (moesin)

Identity

Other namesmoesin (membrane-organising extension spike protein)
HGNC (Hugo) MSN
LocusID (NCBI) 4478
Location Xq12
Location_base_pair Starts at 64887511 and ends at 64961793 bp from pter ( according to hg19-Feb_2009)  [Mapping]
 
  Probe(s) - Courtesy Mariano Rocchi, Resources for Molecular Cytogenetics

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.
  

Other Leukemias implicated (Data extracted from papers in the Atlas)

Leukemias 11q23ChildAMLID1615

External links

Nomenclature
HGNC (Hugo)MSN   7373
Cards
AtlasMSNID363
Entrez_Gene (NCBI)MSN  4478  moesin
GeneCards (Weizmann)MSN
Ensembl (Hinxton)ENSG00000147065 [Gene_View]  chrX:64887511-64961793 [Contig_View]  MSN [Vega]
ICGC DataPortalENSG00000147065
cBioPortalMSN
AceView (NCBI)MSN
Genatlas (Paris)MSN
WikiGenes4478
SOURCE (Princeton)NM_002444
Genomic and cartography
GoldenPath (UCSC)MSN  -  Xq12   chrX:64887511-64961793 +  Xq11.1   [Description]    (hg19-Feb_2009)
EnsemblMSN - Xq11.1 [CytoView]
Mapping of homologs : NCBIMSN [Mapview]
OMIM309845   
Gene and transcription
Genbank (Entrez)AK297165 AK308486 AK309986 BC001112 BC011827
RefSeq transcript (Entrez)NM_002444
RefSeq genomic (Entrez)AC_000155 NC_000023 NC_018934 NG_012516 NT_011651 NW_001842373 NW_004929443
Consensus coding sequences : CCDS (NCBI)MSN
Cluster EST : UnigeneHs.87752 [ NCBI ]
CGAP (NCI)Hs.87752
Alternative Splicing : Fast-db (Paris)GSHG0031582
Alternative Splicing GalleryENSG00000147065
Gene ExpressionMSN [ NCBI-GEO ]     MSN [ SEEK ]   MSN [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP26038 (Uniprot)
NextProtP26038  [Medical]
With graphics : InterProP26038
Splice isoforms : SwissVarP26038 (Swissvar)
Domaine pattern : Prosite (Expaxy)FERM_1 (PS00660)    FERM_2 (PS00661)    FERM_3 (PS50057)   
Domains : Interpro (EBI)Band_41_domain [organisation]   Band_41_fam [organisation]   ERM [organisation]   ERM_C_dom [organisation]   Ez/rad/moesin_like [organisation]   FERM/acyl-CoA-bd_prot_3-hlx [organisation]   FERM_central [organisation]   FERM_CS [organisation]   FERM_domain [organisation]   FERM_N [organisation]   FERM_PH-like_C [organisation]   Moesin_tail [organisation]   PH_like_dom [organisation]   Ubiquitin-rel_dom [organisation]  
Related proteins : CluSTrP26038
Domain families : Pfam (Sanger)ERM (PF00769)    FERM_C (PF09380)    FERM_M (PF00373)    FERM_N (PF09379)   
Domain families : Pfam (NCBI)pfam00769    pfam09380    pfam00373    pfam09379   
Domain families : Smart (EMBL)B41 (SM00295)  
DMDM Disease mutations4478
Blocks (Seattle)P26038
PDB (SRS)1E5W    1EF1    1SGH   
PDB (PDBSum)1E5W    1EF1    1SGH   
PDB (IMB)1E5W    1EF1    1SGH   
PDB (RSDB)1E5W    1EF1    1SGH   
Human Protein AtlasENSG00000147065 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasP26038
HPRD02399
IPIIPI00219365   
Protein Interaction databases
DIP (DOE-UCLA)P26038
IntAct (EBI)P26038
FunCoupENSG00000147065
BioGRIDMSN
InParanoidP26038
Interologous Interaction database P26038
IntegromeDBMSN
STRING (EMBL)MSN
Ontologies - Pathways
Ontology : AmiGOuropod  double-stranded RNA binding  actin binding  receptor binding  structural constituent of cytoskeleton  protein binding  extracellular space  cytoplasm  cytoskeleton  plasma membrane  microvillus  focal adhesion  cellular component movement  leukocyte cell-cell adhesion  positive regulation of gene expression  basolateral plasma membrane  apical plasma membrane  extrinsic component of membrane  protein kinase binding  membrane to membrane docking  filopodium  microvillus membrane  apical part of cell  cell adhesion molecule binding  leukocyte migration  establishment of endothelial barrier  extracellular vesicular exosome  blood microparticle  regulation of lymphocyte migration  
Ontology : EGO-EBIuropod  double-stranded RNA binding  actin binding  receptor binding  structural constituent of cytoskeleton  protein binding  extracellular space  cytoplasm  cytoskeleton  plasma membrane  microvillus  focal adhesion  cellular component movement  leukocyte cell-cell adhesion  positive regulation of gene expression  basolateral plasma membrane  apical plasma membrane  extrinsic component of membrane  protein kinase binding  membrane to membrane docking  filopodium  microvillus membrane  apical part of cell  cell adhesion molecule binding  leukocyte migration  establishment of endothelial barrier  extracellular vesicular exosome  blood microparticle  regulation of lymphocyte migration  
Pathways : KEGGLeukocyte transendothelial migration    Regulation of actin cytoskeleton    Measles    Proteoglycans in cancer   
Protein Interaction DatabaseMSN
Wikipedia pathwaysMSN
Gene fusion - rearrangments
Rearrangement : COSMICALK [2p23.2]  -  MSN [Xq12]  
  [COSF423] [COSF468] 
Rearrangement : COSMICMSN [Xq12]  -  ALK [2p23.2]  
  [COSF421] [COSF422] [COSF467] 
Rearrangement : TICdbMSN [Xq12]  -  ALK [10q25.1]
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)MSN
snp3D : Map Gene to Disease4478
SNP (GeneSNP Utah)MSN
SNP : HGBaseMSN
Genetic variants : HAPMAPMSN
Exome VariantMSN
1000_GenomesMSN 
ICGC programENSG00000147065 
Cancer Gene: CensusMSN 
Somatic Mutations in Cancer : COSMICMSN 
CONAN: Copy Number AnalysisMSN 
Mutations and Diseases : HGMDMSN
Genomic VariantsMSN  MSN [DGVbeta]
dbVarMSN
ClinVarMSN
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM309845   
MedgenMSN
GENETestsMSN
Disease Genetic AssociationMSN
Huge Navigator MSN [HugePedia]  MSN [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneMSN
Homology/Alignments : Family Browser (UCSC)MSN
Phylogenetic Trees/Animal Genes : TreeFamMSN
Chemical/Protein Interactions : CTD4478
Chemical/Pharm GKB GenePA31178
Clinical trialMSN
Cancer Resource (Charite)ENSG00000147065
Other databases
Probes
Litterature
PubMed151 Pubmed reference(s) in Entrez
CoreMineMSN
iHOPMSN
OncoSearchMSN

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 (moesin)
Atlas Genet Cytogenet Oncol Haematol. 2001;5(4):263-264.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/MSNID363.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Wed Jul 30 16:57:36 CEST 2014

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