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P50402

- EMD_HUMAN

UniProt

P50402 - EMD_HUMAN

Protein

Emerin

Gene

EMD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C.5 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. beta-tubulin binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to growth factor stimulus Source: BHF-UCL
    2. mitotic cell cycle Source: Reactome
    3. mitotic nuclear envelope disassembly Source: Reactome
    4. mitotic nuclear envelope reassembly Source: Reactome
    5. muscle contraction Source: ProtInc
    6. muscle organ development Source: ProtInc
    7. negative regulation of catenin import into nucleus Source: BHF-UCL
    8. negative regulation of fibroblast proliferation Source: BHF-UCL
    9. positive regulation of protein export from nucleus Source: BHF-UCL
    10. regulation of canonical Wnt signaling pathway Source: BHF-UCL
    11. skeletal muscle cell differentiation Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_200828. Depolymerisation of the Nuclear Lamina.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Emerin
    Gene namesi
    Name:EMD
    Synonyms:EDMD, STA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3331. 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.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB
    4. microtubule Source: UniProtKB-KW
    5. nuclear envelope Source: BHF-UCL
    6. nuclear inner membrane Source: BHF-UCL
    7. nuclear membrane Source: HPA
    8. nuclear outer membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Microtubule, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1) [MIM:310300]: A form of Emery-Dreifuss muscular dystrophy, a degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1.
    VAR_005198
    Natural varianti133 – 1331Q → H in EDMD1; loss of binding to F-actin. 1 Publication
    VAR_016016
    Natural varianti183 – 1831P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. 1 Publication
    VAR_005199
    Natural varianti183 – 1831P → T in EDMD1. 1 Publication
    VAR_005200

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491S → A: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. 1 Publication
    Mutagenesisi49 – 491S → E: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. 1 Publication
    Mutagenesisi196 – 1961S → A: No loss of binding to F-actin; when associated with A-197. 1 Publication
    Mutagenesisi197 – 1971S → A: No loss of binding to F-actin; when associated with A-196. 1 Publication

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation, Emery-Dreifuss muscular dystrophy

    Organism-specific databases

    MIMi310300. phenotype.
    Orphaneti98863. X-linked Emery-Dreifuss muscular dystrophy.
    PharmGKBiPA27766.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 254254EmerinPRO_0000206140Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine7 Publications
    Modified residuei8 – 81Phosphoserine2 Publications
    Modified residuei49 – 491Phosphoserine; by PKA6 Publications
    Modified residuei54 – 541Phosphoserine2 Publications
    Modified residuei60 – 601Phosphoserine3 Publications
    Modified residuei87 – 871Phosphoserine2 Publications
    Modified residuei161 – 1611PhosphotyrosineBy similarity
    Modified residuei171 – 1711Phosphoserine2 Publications

    Post-translational modificationi

    Found in four different phosphorylated forms, three of which appear to be associated with the cell cycle.8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP50402.
    PaxDbiP50402.
    PeptideAtlasiP50402.
    PRIDEiP50402.

    PTM databases

    PhosphoSiteiP50402.

    Expressioni

    Tissue specificityi

    Skeletal muscle, heart, colon, testis, ovary and pancreas.

    Gene expression databases

    ArrayExpressiP50402.
    BgeeiP50402.
    CleanExiHS_EMD.
    GenevestigatoriP50402.

    Organism-specific databases

    HPAiCAB001545.
    CAB002029.
    CAB062552.
    HPA000609.

    Interactioni

    Subunit structurei

    Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in the nuclear inner membrane. Interacts with SUN1 and SUN2 By similarity. Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta-tubulin.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCLAF1Q9NYF83EBI-489887,EBI-437804
    CTNNB1P352223EBI-489887,EBI-491549
    SH3GL2Q999622EBI-489887,EBI-77938
    Sun1Q9D6664EBI-489887,EBI-6752574From a different organism.
    SUN2Q9UH993EBI-489887,EBI-1044964

    Protein-protein interaction databases

    BioGridi108325. 101 interactions.
    DIPiDIP-34638N.
    IntActiP50402. 26 interactions.
    MINTiMINT-266014.
    STRINGi9606.ENSP00000358857.

    Structurei

    Secondary structure

    1
    254
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Helixi9 – 168
    Beta strandi17 – 193
    Helixi29 – 313
    Helixi32 – 376
    Helixi40 – 423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEINMR-A2-54[»]
    2ODCNMR-I2-47[»]
    2ODGNMR-C2-47[»]
    ProteinModelPortaliP50402.
    SMRiP50402. Positions 2-54.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50402.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei223 – 24321HelicalSequence 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 – 222177Interaction with F-actinCuratedAdd
    BLAST
    Regioni168 – 18619Interaction with CTNNB1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi192 – 1998Poly-Ser

    Sequence similaritiesi

    Contains 1 LEM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG46326.
    HOGENOMiHOG000081509.
    HOVERGENiHBG001099.
    InParanoidiP50402.
    KOiK12569.
    OMAiSIAHYRP.
    PhylomeDBiP50402.
    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.

    P50402-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP    50
    PSSSAASSYS FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF 100
    TTRTYGEPES AGPSRAVRQS VTSFPDADAF HHQVHDDDLL SSSEEECKDR 150
    ERPMYGRDSA YQSITHYRPV SASRSSLDLS YYPTSSSTSF MSSSSSSSSW 200
    LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF FIYHFMQAEE 250
    GNPF 254
    Length:254
    Mass (Da):28,994
    Last modified:October 1, 1996 - v1
    Checksum:iEB62EDD59B7A044F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1.
    VAR_005198
    Natural varianti133 – 1331Q → H in EDMD1; loss of binding to F-actin. 1 Publication
    VAR_016016
    Natural varianti149 – 1491D → H.
    Corresponds to variant rs2070818 [ dbSNP | Ensembl ].
    VAR_038433
    Natural varianti183 – 1831P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. 1 Publication
    VAR_005199
    Natural varianti183 – 1831P → T in EDMD1. 1 Publication
    VAR_005200

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82434 mRNA. Translation: CAA57817.1.
    L44140 Genomic DNA. Translation: AAA92645.1.
    D64111 Genomic DNA. Translation: BAA10972.1.
    X86810 Genomic DNA. Translation: CAA60500.1.
    BT007401 mRNA. Translation: AAP36065.1.
    CR536536 mRNA. Translation: CAG38773.1.
    BX936346 Genomic DNA. Translation: CAI43228.1.
    CH471172 Genomic DNA. Translation: EAW72742.1.
    BC000738 mRNA. Translation: AAH00738.1.
    CCDSiCCDS14745.1.
    PIRiS50834.
    RefSeqiNP_000108.1. NM_000117.2.
    UniGeneiHs.522823.

    Genome annotation databases

    EnsembliENST00000369842; ENSP00000358857; ENSG00000102119.
    GeneIDi2010.
    KEGGihsa:2010.
    UCSCiuc004fkl.3. human.

    Polymorphism databases

    DMDMi1706639.

    Cross-referencesi

    Web resourcesi

    EMD db

    "EMD mutation database"

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82434 mRNA. Translation: CAA57817.1 .
    L44140 Genomic DNA. Translation: AAA92645.1 .
    D64111 Genomic DNA. Translation: BAA10972.1 .
    X86810 Genomic DNA. Translation: CAA60500.1 .
    BT007401 mRNA. Translation: AAP36065.1 .
    CR536536 mRNA. Translation: CAG38773.1 .
    BX936346 Genomic DNA. Translation: CAI43228.1 .
    CH471172 Genomic DNA. Translation: EAW72742.1 .
    BC000738 mRNA. Translation: AAH00738.1 .
    CCDSi CCDS14745.1.
    PIRi S50834.
    RefSeqi NP_000108.1. NM_000117.2.
    UniGenei Hs.522823.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JEI NMR - A 2-54 [» ]
    2ODC NMR - I 2-47 [» ]
    2ODG NMR - C 2-47 [» ]
    ProteinModelPortali P50402.
    SMRi P50402. Positions 2-54.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108325. 101 interactions.
    DIPi DIP-34638N.
    IntActi P50402. 26 interactions.
    MINTi MINT-266014.
    STRINGi 9606.ENSP00000358857.

    PTM databases

    PhosphoSitei P50402.

    Polymorphism databases

    DMDMi 1706639.

    Proteomic databases

    MaxQBi P50402.
    PaxDbi P50402.
    PeptideAtlasi P50402.
    PRIDEi P50402.

    Protocols and materials databases

    DNASUi 2010.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369842 ; ENSP00000358857 ; ENSG00000102119 .
    GeneIDi 2010.
    KEGGi hsa:2010.
    UCSCi uc004fkl.3. human.

    Organism-specific databases

    CTDi 2010.
    GeneCardsi GC0XP153607.
    GeneReviewsi EMD.
    HGNCi HGNC:3331. EMD.
    HPAi CAB001545.
    CAB002029.
    CAB062552.
    HPA000609.
    MIMi 300384. gene.
    310300. phenotype.
    neXtProti NX_P50402.
    Orphaneti 98863. X-linked Emery-Dreifuss muscular dystrophy.
    PharmGKBi PA27766.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46326.
    HOGENOMi HOG000081509.
    HOVERGENi HBG001099.
    InParanoidi P50402.
    KOi K12569.
    OMAi SIAHYRP.
    PhylomeDBi P50402.
    TreeFami TF337236.

    Enzyme and pathway databases

    Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_200828. Depolymerisation of the Nuclear Lamina.

    Miscellaneous databases

    EvolutionaryTracei P50402.
    GeneWikii Emerin.
    GenomeRNAii 2010.
    NextBioi 8137.
    PROi P50402.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50402.
    Bgeei P50402.
    CleanExi HS_EMD.
    Genevestigatori P50402.

    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. "Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy."
      Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G., Toniolo D.
      Nat. Genet. 8:323-327(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Teratocarcinoma.
    2. "Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."
      Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.
      Hum. Mol. Genet. 5:659-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "A novel emerin mutation in a Japanese patient with Emery-Dreifuss muscular dystrophy."
      Yamada T., Kobayashi T.
      Hum. Genet. 97:693-694(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Identification of new mutations in the Emery-Dreifuss muscular dystrophy gene and evidence for genetic heterogeneity of the disease."
      Bione S., Small K., Aksmanovic M.A., D'Urso M., Ciccodicola A., Merlini L., Morandi L., Kress W., Yates J.R.W., Warren S.T., Toniolo D.
      Hum. Mol. Genet. 4:1859-1863(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Placenta.
    10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-17.
      Tissue: Platelet.
    11. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-31; 37-45; 48-115 AND 158-203, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma and Embryonic kidney.
    12. Cited for: SUBCELLULAR LOCATION.
    13. "Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype."
      Ellis J.A., Craxton M., Yates J.R.W., Kendrick-Jones J.
      J. Cell Sci. 111:781-792(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    14. "BAF is required for emerin assembly into the reforming nuclear envelope."
      Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y., Yoneda Y., Wilson K.L., Hiraoka Y.
      J. Cell Sci. 114:4575-4585(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BANF1.
    15. Cited for: INTERACTION WITH YTHDC1.
    16. "Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro."
      Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L.
      J. Biol. Chem. 278:6969-6975(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GMCL.
    17. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy."
      Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N., Mori C., Wilson K.L., Hiraoka Y.
      Eur. J. Biochem. 271:1035-1045(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCLAF1, CHARACTERIZATION OF VARIANT EDMD1 PHE-54.
    19. "Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane."
      Holaska J.M., Kowalski A.K., Wilson K.L.
      PLoS Biol. 2:1354-1362(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN, MUTAGENESIS OF SER-196 AND SER-197, CHARACTERIZATION OF VARIANTS EDMD1 PHE-54; HIS-133 AND HIS-183.
    20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: FUNCTION, INTERACTION WITH CTNNB1.
    23. "The Emery-Dreifuss muscular dystrophy associated-protein emerin is phosphorylated on serine 49 by protein kinase A."
      Roberts R.C., Sutherland-Smith A.J., Wheeler M.A., Jensen O.N., Emerson L.J., Spiliotis I.I., Tate C.G., Kendrick-Jones J., Ellis J.A.
      FEBS J. 273:4562-4575(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-49, SUBCELLULAR LOCATION, INTERACTION WITH LMNA, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-49.
    24. "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity."
      Jacque J.-M., Stevenson M.
      Nature 441:641-645(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane."
      Salpingidou G., Smertenko A., Hausmanowa-Petrucewicz I., Hussey P.J., Hutchison C.J.
      J. Cell Biol. 178:897-904(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BETA-TUBULIN.
    26. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-54; SER-60 AND SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    33. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy."
      Wolff N., Gilquin B., Courchay K., Callebaut I., Worman H.J., Zinn-Justin S.
      FEBS Lett. 501:171-176(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-54.
    39. "Structural characterization of the LEM motif common to three human inner nuclear membrane proteins."
      Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I., Worman H.J., Zinn-Justin S.
      Structure 9:503-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-54.
    40. "Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy."
      Ellis J.A., Yates J.R.W., Kendrick-Jones J., Brown C.A.
      Hum. Genet. 104:262-268(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDMD1 HIS-183 AND THR-183.
    41. "How does a g993t mutation in the emerin gene cause Emery-Dreifuss muscular dystrophy?"
      Holt I., Clements L., Manilal S., Morris G.E.
      Biochem. Biophys. Res. Commun. 287:1129-1133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDMD1 HIS-133.

    Entry informationi

    Entry nameiEMD_HUMAN
    AccessioniPrimary (citable) accession number: P50402
    Secondary accession number(s): Q6FI02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 160 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3