SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00002496 
UniProt Accession
Theoretical PI
4.85  
Molecular Weight
29436 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Emd 
Gene Synonyms/Alias
Sta 
Protein Name
Emerin 
Protein Synonyms/Alias
 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:X;71500026-71506887;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.973743348 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. Emery-Dreifuss muscular dystrophy (EMD) is an X-linked recessive disorder associated with muscle wasting, contractures, and cardiomyopathy. The responsible emerin gene has recently been identified and found to encode a serine-rich protein similar to lamina-associated protein 2 (LAP2), although the disease mechanism remains obscure. In order to pursue the pathophysiology of this disorder, we report here the isolation and characterization of the complete mouse emerin gene. The emerin cDNA was isolated from murine strain BALB/c, and the emerin gene was isolated from strain 129. The 2.9-kb mouse emerin gene was completely sequenced and found to be composed of 6 exons and encode a protein 73% identical to that of the human protein. Key similarities with LAP2 were found to be conserved, including critical LAP2 phosphorylation sites. Examination of the murine promoter revealed three previously unrecognized cAMP response elements (CRE) conserved between human and mouse. While Northern analysis shows emerin to be widely expressed in the mouse, as it is in humans, these promoter elements may indicate cAMP responsiveness. These data provide the necessary elements to further investigate EMD in a murine system. PMID: [9107678] 

2. We present here a first characterization of LUMA, an unique integral inner nuclear membrane (INM) protein. LUMA is a highly conserved protein even in some bacteria and shares a PFAM domain of unknown function with orthologs from many species. Assessing LUMA topology by using protease protection of membrane-inserted LUMA and antibody epitope accessibility assays reveals that LUMA contains four transmembrane domains and a large hydrophilic domain located between membrane spans 1 and 2. The large hydrophilic domain is exposed to the perinuclear space whereas both LUMA termini reside cyto- or nucleoplasmically. Nuclear envelope targeting of LUMA mainly depends on the membrane spans. LUMA's transmembrane domains also promote homooligomerization. LUMA binds A- and B-type lamins and depends on A-type lamins for its INM localization. Furthermore, it interacts with emerin. Both downregulation of LUMA and overexpression of dominant-negative acting LUMA fragments causes redistribution of emerin. We propose that LUMA functions as a tetraspanin-like membrane organizer and has the potential to contribute to the pathomechanism of dystrophic diseases, such as Emery-Dreifuss muscular dystrophy. PMID: [18230648] 

3. We used on-line electron capture dissociation (ECD) for the large scale identification and localization of sites of phosphorylation. Each FT-ICR ECD event was paired with a linear ion trap collision-induced dissociation (CID) event, allowing a direct comparison of the relative merits of ECD and CID for phosphopeptide identification and site localization. Linear ion trap CID was shown to be most efficient for phosphopeptide identification, whereas FT-ICR ECD was superior for localization of sites of phosphorylation. The combination of confident CID and ECD identification and confident CID and ECD localization is particularly valuable in cases where a phosphopeptide is identified just once within a phosphoproteomics experiment. PMID: [19131326] 

4. The nuclear envelope (NE) LINC complex, in mammals comprised of SUN domain and nesprin proteins, provides a direct connection between the nuclear lamina and the cytoskeleton, which contributes to nuclear positioning and cellular rigidity. SUN1 and SUN2 interact with lamin A, but lamin A is only required for NE localization of SUN2, and it remains unclear how SUN1 is anchored. Here, we identify emerin and short nesprin-2 isoforms as novel nucleoplasmic binding partners of SUN1/2. These have overlapping binding sites distinct from the lamin A binding site. However, we demonstrate that tight association of SUN1 with the nuclear lamina depends upon a short motif within residues 209-228, a region that does not interact significantly with known SUN1 binding partners. Moreover, SUN1 localizes correctly in cells lacking emerin. Importantly then, the major determinant of SUN1 NE localization has yet to be identified. We further find that a subset of lamin A mutations, associated with laminopathies Emery-Dreifuss muscular dystrophy (EDMD) and Hutchinson-Gilford progeria syndrome (HGPS), disrupt lamin A interaction with SUN1 and SUN2. Despite this, NE localization of SUN1 and SUN2 is not impaired in cell lines from either class of patients. Intriguingly, SUN1 expression at the NE is instead enhanced in a significant proportion of HGPS but not EDMD cells and strongly correlates with pre-lamin A accumulation due to preferential interaction of SUN1 with pre-lamin A. We propose that these different perturbations in lamin A-SUN protein interactions may underlie the opposing effects of EDMD and HGPS mutations on nuclear and cellular mechanics. PMID: [19933576] 

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Function
Stabilizes and promotes the formation of a nuclear actincortical network. Stimulates actin polymerization in vitro bybinding and stabilizing the pointed end of growing filaments.Inhibits beta-catenin activity by preventing its accumulation inthe nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomesto the nuclear envelope via a microtubule association. Requiredfor proper localization of non-farnesylated prelamin-A/C (Bysimilarity). 
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Subcellular Location
Nucleus inner membrane; Single-pass membraneprotein; Nucleoplasmic side. Nucleus outer membrane.Note=Colocalized with BANF1 at the central region of theassembling nuclear rim, near spindle-attachment sites. Theaccumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) infibroblasts modify its localization in the nucleus (Bysimilarity). 
Tissue Specificity
Widely expressed. 
Gene Ontology
GO IDGO termEvidence
GO:0005783 C:endoplasmic reticulum IEA:Compara.
GO:0016021 C:integral to membrane IEA:UniProtKB-KW.
GO:0005874 C:microtubule IEA:UniProtKB-KW.
GO:0005637 C:nuclear inner membrane TAS:MGI.
GO:0005652 C:nuclear lamina TAS:MGI.
GO:0005640 C:nuclear outer membrane IEA:UniProtKB-SubCell.
GO:0005819 C:spindle IEA:Compara.
GO:0071363 P:cellular response to growth factor stimulus IEA:Compara.
GO:0035414 P:negative regulation of catenin import into nucleus IEA:Compara.
GO:0048147 P:negative regulation of fibroblast proliferation IEA:Compara.
GO:0031468 P:nuclear envelope reassembly IEA:Compara.
GO:0046827 P:positive regulation of protein export from nucleus IEA:Compara.
GO:0060828 P:regulation of canonical Wnt receptor signaling pathway IEA:Compara.
GO:0035914 P:skeletal muscle cell differentiation IMP:MGI.
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Interpro
IPR003887;    LEM.
IPR011015;    LEM-like_dom.
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Pfam
PF03020;    LEM;    1.
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SMART
SM00540;    LEM;    1.
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PROSITE
PS50954;    LEM;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    259       Emerin.
                             /FTId=PRO_0000206141.
TRANSMEM    224    244       Helical; (Potential).
DOMAIN        1     45       LEM.
REGION       46    223       Interaction with F-actin (By similarity).
REGION      168    187       Interaction with CTNNB1 (By similarity).
COMPBIAS     53     59       Poly-Ser.
COMPBIAS    186    200       Poly-Ser.
MOD_RES       1      1       N-acetylmethionine (By similarity).
MOD_RES       8      8       Phosphoserine (By similarity).
MOD_RES      29     29       Phosphoserine (By similarity).
MOD_RES      54     54       Phosphoserine (By similarity).
MOD_RES      60     60       Phosphotyrosine (By similarity).
MOD_RES      67     67       Phosphoserine (By similarity).
MOD_RES      75     75       Phosphotyrosine (By similarity).
MOD_RES      86     86       Phosphotyrosine (By similarity).
MOD_RES      88     88       Phosphoserine (By similarity).
MOD_RES      96     96       Phosphotyrosine (By similarity).
MOD_RES     100    100       Phosphotyrosine (By similarity).
MOD_RES     106    106       Phosphotyrosine (By similarity).
MOD_RES     161    161       Phosphotyrosine.
MOD_RES     163    163       Phosphoserine (By similarity).
MOD_RES     167    167       Phosphotyrosine (By similarity).
MOD_RES     171    171       Phosphoserine (By similarity).
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Nucleotide Sequence
Length: 3938 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 259 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
CdiptString 
CdiptString 
Pou5f1BioGRID 
Other Protein-Protein interaction resources
String database  
View Microarray data
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