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Protein EMD PDB 1jei.png
PDB rendering based on 1jei.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols EMD ; EDMD; LEMD5; STA
External IDs OMIM300384 MGI108117 HomoloGene91 GeneCards: EMD Gene
RNA expression pattern
PBB GE EMD 209477 at tn.png
More reference expression data
Species Human Mouse
Entrez 2010 13726
Ensembl ENSG00000102119 ENSMUSG00000001964
UniProt P50402 O08579
RefSeq (mRNA) NM_000117 NM_007927
RefSeq (protein) NP_000108 NP_031953
Location (UCSC) Chr X:
154.38 – 154.38 Mb
Chr X:
74.25 – 74.26 Mb
PubMed search [1] [2]

Emerin, together with MAN1, is a LEM domain-containing integral protein of the inner nuclear membrane in vertebrates. The function of MAN1 is not extensively known, but emerin is known to interact with nuclear lamins, barrier-to-autointegration factor (BAF), nesprin-1α, and a transcription repressor.


Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene.[1]

Clinical significance[edit]

Mutations in emerin cause X-linked recessive Emery-Dreifuss muscular dystrophy.

Moreover, recent research have found that the absence of functional emerin may decrease the infectivity of HIV-1. Thus, it is speculated that patients suffering from Emery-Dreifuss muscular dystrophy may have immunity to or show an irregular infection pattern to HIV-1.[2]


Emerin has been shown to interact with:


  1. ^ "Entrez Gene: EMD emerin (Emery-Dreifuss muscular dystrophy)". 
  2. ^ Li M, Craigie R (June 2006). "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity". Nature 441 (7093): 581–2. doi:10.1038/441581a. PMID 16738646. 
  3. ^ a b Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L et al. (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. 303 (3): 764–70. doi:10.1016/s0006-291x(03)00415-7. PMID 12670476. 
  4. ^ a b c Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I et al. (June 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". Eur. J. Biochem. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701. 
  5. ^ Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K et al. (February 2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535. 
  6. ^ Clements L, Manilal S, Love DR, Morris GE (January 2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356. 

Further reading[edit]

External links[edit]