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Protein

Emerin

Gene

Emd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. actin binding Source: MGI
  2. beta-tubulin binding Source: MGI

GO - Biological processi

  1. cellular response to growth factor stimulus Source: MGI
  2. negative regulation of catenin import into nucleus Source: MGI
  3. negative regulation of fibroblast proliferation Source: MGI
  4. positive regulation of protein export from nucleus Source: MGI
  5. regulation of canonical Wnt signaling pathway Source: MGI
  6. skeletal muscle cell differentiation Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.

Names & Taxonomyi

Protein namesi
Recommended name:
Emerin
Gene namesi
Name:Emd
Synonyms:Sta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:108117. Emd.

Subcellular locationi

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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei224 – 24421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
  4. microtubule Source: UniProtKB-KW
  5. nuclear envelope Source: UniProtKB
  6. nuclear inner membrane Source: MGI
  7. nuclear lamina Source: MGI
  8. nuclear membrane Source: MGI
  9. nuclear outer membrane Source: MGI
  10. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259EmerinPRO_0000206141Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei88 – 881PhosphoserineBy similarity
Modified residuei161 – 1611Phosphotyrosine1 Publication
Modified residuei171 – 1711PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO08579.
PaxDbiO08579.
PRIDEiO08579.

PTM databases

PhosphoSiteiO08579.

Miscellaneous databases

PMAP-CutDBO08579.

Expressioni

Tissue specificityi

Detected in embryonic fibroblasts, skeletal muscle, heart muscle and tongue epithelium (at protein level). Widely expressed.2 Publications

Gene expression databases

BgeeiO08579.
CleanExiMM_EMD.
ExpressionAtlasiO08579. baseline and differential.
GenevestigatoriO08579.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi199436. 3 interactions.
IntActiO08579. 2 interactions.
MINTiMINT-4094379.
STRINGi10090.ENSMUSP00000002029.

Structurei

3D structure databases

ProteinModelPortaliO08579.
SMRiO08579. Positions 2-47.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4545LEMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 223178Interaction with F-actinBy similarityAdd
BLAST
Regioni168 – 18720Interaction with CTNNB1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi53 – 597Poly-Ser
Compositional biasi186 – 20015Poly-SerAdd
BLAST

Sequence similaritiesi

Contains 1 LEM domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46326.
GeneTreeiENSGT00390000002034.
HOGENOMiHOG000081509.
HOVERGENiHBG001099.
InParanoidiO08579.
KOiK12569.
OMAiNIXLDSG.
OrthoDBiEOG7DFXDP.
PhylomeDBiO08579.
TreeFamiTF337236.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
InterProiIPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamiPF03020. LEM. 1 hit.
[Graphical view]
SMARTiSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMiSSF63451. SSF63451. 1 hit.
PROSITEiPS50954. LEM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08579-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDDYAVLSDT ELAAVLRQYN IPHGPIVGST RKLYEKKIFE YETQRRRLLP
60 70 80 90 100
PNSSSSSFSY QFSDLDSAAV DSDMYDLPKK EDALLYQSKD YNDDYYEESY
110 120 130 140 150
LTTKTYGEPE SVGMSKSFRQ PGTSLVDADT FHHQVRDDIF SSLEEEGKDR
160 170 180 190 200
ERLIYGQDSA YQSIAHYRPI SNVSRSSLGL SYYPTSSTSS VSSSSSSPSS
210 220 230 240 250
WLTRRAIRPE KQAPAAALGQ DRQVPLWGQL LLFLVFAAFL LFVYYSIQAE

EGNPFWMDP
Length:259
Mass (Da):29,436
Last modified:July 1, 1997 - v1
Checksum:i645B021541063502
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961Y → C in BAE39870. (PubMed:16141072)Curated
Sequence conflicti254 – 2541P → H in BAE39870. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79753 Genomic DNA. Translation: AAB51239.1.
U73902 mRNA. Translation: AAD00238.1.
AK146361 mRNA. Translation: BAE27112.1.
AK167852 mRNA. Translation: BAE39870.1.
CH466650 Genomic DNA. Translation: EDL29837.1.
BC132131 mRNA. Translation: AAI32132.1.
BC132133 mRNA. Translation: AAI32134.1.
CCDSiCCDS30222.1.
RefSeqiNP_031953.1. NM_007927.3.
UniGeneiMm.18892.

Genome annotation databases

EnsembliENSMUST00000002029; ENSMUSP00000002029; ENSMUSG00000001964.
GeneIDi13726.
KEGGimmu:13726.
UCSCiuc009toa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79753 Genomic DNA. Translation: AAB51239.1.
U73902 mRNA. Translation: AAD00238.1.
AK146361 mRNA. Translation: BAE27112.1.
AK167852 mRNA. Translation: BAE39870.1.
CH466650 Genomic DNA. Translation: EDL29837.1.
BC132131 mRNA. Translation: AAI32132.1.
BC132133 mRNA. Translation: AAI32134.1.
CCDSiCCDS30222.1.
RefSeqiNP_031953.1. NM_007927.3.
UniGeneiMm.18892.

3D structure databases

ProteinModelPortaliO08579.
SMRiO08579. Positions 2-47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199436. 3 interactions.
IntActiO08579. 2 interactions.
MINTiMINT-4094379.
STRINGi10090.ENSMUSP00000002029.

PTM databases

PhosphoSiteiO08579.

Proteomic databases

MaxQBiO08579.
PaxDbiO08579.
PRIDEiO08579.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002029; ENSMUSP00000002029; ENSMUSG00000001964.
GeneIDi13726.
KEGGimmu:13726.
UCSCiuc009toa.1. mouse.

Organism-specific databases

CTDi2010.
MGIiMGI:108117. Emd.

Phylogenomic databases

eggNOGiNOG46326.
GeneTreeiENSGT00390000002034.
HOGENOMiHOG000081509.
HOVERGENiHBG001099.
InParanoidiO08579.
KOiK12569.
OMAiNIXLDSG.
OrthoDBiEOG7DFXDP.
PhylomeDBiO08579.
TreeFamiTF337236.

Enzyme and pathway databases

ReactomeiREACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.

Miscellaneous databases

ChiTaRSiEmd. mouse.
NextBioi284512.
PMAP-CutDBO08579.
PROiO08579.
SOURCEiSearch...

Gene expression databases

BgeeiO08579.
CleanExiMM_EMD.
ExpressionAtlasiO08579. baseline and differential.
GenevestigatoriO08579.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
InterProiIPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamiPF03020. LEM. 1 hit.
[Graphical view]
SMARTiSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMiSSF63451. SSF63451. 1 hit.
PROSITEiPS50954. LEM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], TISSUE SPECIFICITY.
    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.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: DBA/2.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy."
    Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K., Stewart C.L., Burke B.
    J. Cell Biol. 147:913-920(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "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.
  8. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "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.

Entry informationi

Entry nameiEMD_MOUSE
AccessioniPrimary (citable) accession number: O08579
Secondary accession number(s): Q3TIH6, Q3UJP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 1, 1997
Last modified: February 4, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.