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O08579

- EMD_MOUSE

UniProt

O08579 - EMD_MOUSE

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Protein

Emerin

Gene
Emd, Sta
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular response to growth factor stimulus Source: Ensembl
  2. negative regulation of catenin import into nucleus Source: Ensembl
  3. negative regulation of fibroblast proliferation Source: Ensembl
  4. positive regulation of protein export from nucleus Source: Ensembl
  5. regulation of canonical Wnt signaling pathway Source: Ensembl
  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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei224 – 24421Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. microtubule Source: UniProtKB-KW
  4. nuclear envelope Source: UniProtKB
  5. nuclear inner membrane Source: MGI
  6. nuclear lamina Source: MGI
  7. nuclear outer membrane Source: UniProtKB-SubCell
  8. 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-acetylmethionine By similarity
Modified residuei8 – 81Phosphoserine By similarity
Modified residuei54 – 541Phosphoserine By similarity
Modified residuei88 – 881Phosphoserine By similarity
Modified residuei161 – 1611Phosphotyrosine1 Publication
Modified residuei171 – 1711Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

ArrayExpressiO08579.
BgeeiO08579.
CleanExiMM_EMD.
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 SUN2.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliO08579.
SMRiO08579. Positions 2-47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4545LEMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 223178Interaction with F-actin By similarityAdd
BLAST
Regioni168 – 18720Interaction with CTNNB1 By 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.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46326.
GeneTreeiENSGT00390000002034.
HOGENOMiHOG000081509.
HOVERGENiHBG001099.
InParanoidiO08579.
KOiK12569.
OMAiSIAHYRP.
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

MDDYAVLSDT ELAAVLRQYN IPHGPIVGST RKLYEKKIFE YETQRRRLLP    50
PNSSSSSFSY QFSDLDSAAV DSDMYDLPKK EDALLYQSKD YNDDYYEESY 100
LTTKTYGEPE SVGMSKSFRQ PGTSLVDADT FHHQVRDDIF SSLEEEGKDR 150
ERLIYGQDSA YQSIAHYRPI SNVSRSSLGL SYYPTSSTSS VSSSSSSPSS 200
WLTRRAIRPE KQAPAAALGQ DRQVPLWGQL LLFLVFAAFL LFVYYSIQAE 250
EGNPFWMDP 259
Length:259
Mass (Da):29,436
Last modified:July 1, 1997 - v1
Checksum:i645B021541063502
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961Y → C in BAE39870. 1 Publication
Sequence conflicti254 – 2541P → H in BAE39870. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS30222.1.
RefSeqi NP_031953.1. NM_007927.3.
UniGenei Mm.18892.

3D structure databases

ProteinModelPortali O08579.
SMRi O08579. Positions 2-47.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199436. 3 interactions.
IntActi O08579. 2 interactions.
MINTi MINT-4094379.
STRINGi 10090.ENSMUSP00000002029.

PTM databases

PhosphoSitei O08579.

Proteomic databases

PaxDbi O08579.
PRIDEi O08579.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002029 ; ENSMUSP00000002029 ; ENSMUSG00000001964 .
GeneIDi 13726.
KEGGi mmu:13726.
UCSCi uc009toa.1. mouse.

Organism-specific databases

CTDi 2010.
MGIi MGI:108117. Emd.

Phylogenomic databases

eggNOGi NOG46326.
GeneTreei ENSGT00390000002034.
HOGENOMi HOG000081509.
HOVERGENi HBG001099.
InParanoidi O08579.
KOi K12569.
OMAi SIAHYRP.
OrthoDBi EOG7DFXDP.
PhylomeDBi O08579.
TreeFami TF337236.

Enzyme and pathway databases

Reactomei REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.

Miscellaneous databases

ChiTaRSi EMD. mouse.
NextBioi 284512.
PMAP-CutDB O08579.
PROi O08579.
SOURCEi Search...

Gene expression databases

ArrayExpressi O08579.
Bgeei O08579.
CleanExi MM_EMD.
Genevestigatori O08579.

Family and domain databases

Gene3Di 1.10.720.40. 1 hit.
InterProi IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view ]
Pfami PF03020. LEM. 1 hit.
[Graphical view ]
SMARTi SM00540. LEM. 1 hit.
[Graphical view ]
SUPFAMi SSF63451. SSF63451. 1 hit.
PROSITEi PS50954. LEM. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 114 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