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O08579

- EMD_MOUSE

UniProt

O08579 - EMD_MOUSE

Protein

Emerin

Gene

Emd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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. 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

    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

    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

    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

    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.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...

    Transmembrane

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

    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 115 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