Emerin - Mus musculus (Mouse)

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O08579 (EMD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Emerin

Gene names

Name:	Emd
Synonyms:	Sta

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Required for proper localization of non-farnesylated prelamin-A/C By similarity.
Subunit structure	Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in the inner nuclear membrane. Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta-tubulin By similarity. Interacts with SUN1 and SUN2. Ref.3 Ref.5
Subcellular location	Nucleus inner membrane; Single-pass membrane protein; Nucleoplasmic side. Nucleus outer membrane. Note: Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus By similarity. Ref.3
Tissue specificity	Widely expressed.
Sequence similarities	Contains 1 LEM domain.

Ontologies

Keywords
Cellular component	Membrane Microtubule Nucleus
Domain	Transmembrane Transmembrane helix
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara negative regulation of catenin import into nucleus Inferred from electronic annotation. Source: Compara negative regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of protein export from nucleus Inferred from electronic annotation. Source: Compara regulation of canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara skeletal muscle cell differentiation Inferred from mutant phenotype PubMed 19720741. Source: MGI
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW nuclear inner membrane Traceable author statement PubMed 11591818. Source: MGI nuclear lamina Traceable author statement PubMed 11591818. Source: MGI nuclear outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 259

259

Emerin

PRO_0000206141

Regions

Transmembrane

224 – 244

Helical; Potential

Domain

1 – 45

LEM

Region

46 – 223

178

Interaction with F-actin By similarity

Region

168 – 187

Interaction with CTNNB1 By similarity

Compositional bias

53 – 59

Poly-Ser

Compositional bias

186 – 200

Poly-Ser

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

161

Phosphotyrosine Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

O08579 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 645B021541063502
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FASTA

259

29,436

        10         20         30         40         50         60 
MDDYAVLSDT ELAAVLRQYN IPHGPIVGST RKLYEKKIFE YETQRRRLLP PNSSSSSFSY 

        70         80         90        100        110        120 
QFSDLDSAAV DSDMYDLPKK EDALLYQSKD YNDDYYEESY LTTKTYGEPE SVGMSKSFRQ 

       130        140        150        160        170        180 
PGTSLVDADT FHHQVRDDIF SSLEEEGKDR ERLIYGQDSA YQSIAHYRPI SNVSRSSLGL 

       190        200        210        220        230        240 
SYYPTSSTSS VSSSSSSPSS WLTRRAIRPE KQAPAAALGQ DRQVPLWGQL LLFLVFAAFL 

       250 
LFVYYSIQAE EGNPFWMDP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the complete mouse emerin gene." Small K., Wagener M., Warren S.T. Mamm. Genome 8:337-341(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[2]	"cDNA sequence and analysis of the murine Emery-Dreifuss muscular dystrophy gene." Hawkes S.L.J., Neville L.A., Kennedy M.A.K., Love D.R. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR.
[3]	"LUMA interacts with emerin and influences its distribution at the inner nuclear membrane." Bengtsson L., Otto H. J. Cell Sci. 121:536-548(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TMEM43, SUBCELLULAR LOCATION.
[4]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[5]	"Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes." Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S. J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUN1 AND SUN2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U79753 Genomic DNA. Translation: AAB51239.1. U73902 mRNA. Translation: AAD00238.1.
IPI	IPI00114401.
RefSeq	NP_031953.1. NM_007927.2.
UniGene	Mm.18892.
3D structure databases
ProteinModelPortal	O08579.
SMR	O08579. Positions 2-47.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08579. 1 interaction.
STRING	10090.ENSMUSP00000002029.
PTM databases
PhosphoSite	O08579.
Proteomic databases
PaxDb	O08579.
PRIDE	O08579.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002029; ENSMUSP00000002029; ENSMUSG00000001964.
GeneID	13726.
KEGG	mmu:13726.
Organism-specific databases
CTD	2010.
MGI	MGI:108117. Emd.
Phylogenomic databases
eggNOG	NOG46326.
HOGENOM	HOG000081509.
HOVERGEN	HBG001099.
InParanoid	O08579.
KO	K12569.
OrthoDB	EOG4Z62PK.
Gene expression databases
ArrayExpress	O08579.
Bgee	O08579.
CleanEx	MM_EMD.
Genevestigator	O08579.
GermOnline	ENSMUSG00000001964. Mus musculus.
Family and domain databases
Gene3D	1.10.720.40. 1 hit.
InterPro	IPR011015. LEM/LEM-like_dom. IPR003887. LEM_dom. [Graphical view]
Pfam	PF03020. LEM. 1 hit. [Graphical view]
SMART	SM00540. LEM. 1 hit. [Graphical view]
SUPFAM	SSF63451. LEM_like. 1 hit.
PROSITE	PS50954. LEM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EMD. mouse.
NextBio	284512.
PMAP-CutDB	O08579.
SOURCE	Search...

Entry information

Entry name

EMD_MOUSE

Accession

Primary (citable) accession number: O08579

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents