Emerin (EMD)
The protein contains 254 amino acids for an estimated molecular weight of 28994 Da.
Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is predicted to be membranous by TOPCONS.
(right-click above to access to more options from the contextual menu)
Biological Process
Cellular response to growth factor stimulus
Mitotic cell cycle
Mitotic nuclear membrane disassembly
Mitotic nuclear membrane reassembly
Muscle contraction
Muscle organ development
Negative regulation of canonical Wnt signaling pathway
Negative regulation of catenin import into nucleus
Negative regulation of fibroblast proliferation
Nuclear membrane organization
Positive regulation of protein export from nucleus
Protein insertion into ER membrane
Regulation of canonical Wnt signaling pathway
Skeletal muscle cell differentiation
The reference OMIM entry for this protein is 300384
Emerin; emd
Sta
DESCRIPTION
The EMD gene encodes a ubiquitous protein, emerin, that is found along the nuclear rim of many cell types and is a member of the nuclear lamina-associated protein family. Mutation in the EMD gene has been found to cause the Emery-Dreifuss type of muscular dystrophy (EDMD; 310300).CLONING
Bione et al. (1993) constructed a transcriptional map of the 2-Mb region of Xq28 to which the Emery-Dreifuss muscular dystrophy locus had been mapped by linkage studies. Within this region, they identified the STA gene. Bione et al. (1994) determined that STA (EMD) encodes a 254-amino acid protein, termed emerin, which lacks a signal peptide, contains a long N-terminal domain, and is hydrophilic except for a highly hydrophobic 20-amino acid sequence at the C-terminal region. It has several putative phosphorylation sites and 1 potential glycosylation site. Northern blot analysis demonstrated ubiquitous expression of a major, approximately 1-kb transcript, with highest expression in skeletal muscle and heart and abundant expression in other tissues, including colon, testis, ovary, and placenta. Bione et al. (1994) suggested that emerin belongs to a class of tail-anchored membrane proteins of the secretory pathway involved in vesicular transport. Manilal et al. (1996) developed a panel of 12 monoclonal antibodies to a large fragment of emerin cDNA prepared by PCR and expressed as a recombinant protein in E. coli. These antibodies detected 4 different epitopes on emerin. All monoclonal antibodies recognized a 34-kD protein in all tissues tested. Immunofluorescence and cell fractionation studies confirmed that emerin is located in the nuclear membrane. Amino acid sequence similarities and cellular localization suggested that emerin is a member of the nuclear lamina-associated protein family. Small et al. (1997) isolated and characterized the complete mouse emerin gene. The 2.9-kb mouse emerin gene comprises 6 exons and encodes a protein 73% identical to that of the human protein. As in the human, the gene encodes a serine-rich protein similar to lamina-associated protein-2 (LAP2; 188380) and shows critical LAP2 phosphorylation sites.GENE FUNCTION
Cartegni et al. (1997) reported that emerin localizes to the inner nuclear membrane via its hydrophobic C-terminal domain, but that in heart and cultured cardiomyocytes, it is also associated with the intercalated discs. They proposed a general role for emerin in membrane anchorage to the cytoskeleton. In the nuclear envelope, emerin plays a ubiquitous and indispensable role in association of the nuclear membrane with the lamina. In heart, it is specifically located to desmosomes and fasciae adherentes. Desmosomes and fasciae adherentes anchor desmin-containing intermediate filaments and the bundles of sarcomeric myofilaments, respectively. They consist of transmembrane adhesive glycoproteins, members of the cadherin superfamily, and of cytoplasmic proteins such as vinculin (193065), catenins, and actin-binding proteins. Different assortments of the same or similar proteins in desmosomes, fasciae adherentes, focal adhesions, and other adhesive junctions seem to confer specific functions to ensure cell-cell communication and tight adhesion between cells and to the extracellular matrix. The role of this complex assortment of proteins is best demonstrated by the existence of many genetic diseases that perturb adhesion and in the heart by the dramatic consequences of plakog ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300384 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed