EMD_HUMAN
ID EMD_HUMAN Reviewed; 254 AA.
AC P50402; Q6FI02;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Emerin;
GN Name=EMD; Synonyms=EDMD, STA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=7894480; DOI=10.1038/ng1294-323;
RA Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G.,
RA Toniolo D.;
RT "Identification of a novel X-linked gene responsible for Emery-Dreifuss
RT muscular dystrophy.";
RL Nat. Genet. 8:323-327(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8655156; DOI=10.1007/bf02281886;
RA Yamada T., Kobayashi T.;
RT "A novel emerin mutation in a Japanese patient with Emery-Dreifuss muscular
RT dystrophy.";
RL Hum. Genet. 97:693-694(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8595407; DOI=10.1093/hmg/4.10.1859;
RA Bione S., Small K., Aksmanovic M.A., D'Urso M., Ciccodicola A., Merlini L.,
RA Morandi L., Kress W., Yates J.R.W., Warren S.T., Toniolo D.;
RT "Identification of new mutations in the Emery-Dreifuss muscular dystrophy
RT gene and evidence for genetic heterogeneity of the disease.";
RL Hum. Mol. Genet. 4:1859-1863(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 1-17.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP PROTEIN SEQUENCE OF 1-31; 37-45; 48-115 AND 158-203, ACETYLATION AT MET-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=9673989; DOI=10.1016/s0960-8966(98)00031-5;
RA Squarzoni S., Sabatelli P., Ognibene A., Toniolo D., Cartegni L.,
RA Cobianchi F., Petrini S., Merlini L., Maraldi N.M.;
RT "Immunocytochemical detection of emerin within the nuclear matrix.";
RL Neuromuscul. Disord. 8:338-344(1998).
RN [13]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=9472006; DOI=10.1242/jcs.111.6.781;
RA Ellis J.A., Craxton M., Yates J.R.W., Kendrick-Jones J.;
RT "Aberrant intracellular targeting and cell cycle-dependent phosphorylation
RT of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype.";
RL J. Cell Sci. 111:781-792(1998).
RN [14]
RP INTERACTION WITH BANF1.
RX PubMed=11792822; DOI=10.1242/jcs.114.24.4575;
RA Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y.,
RA Yoneda Y., Wilson K.L., Hiraoka Y.;
RT "BAF is required for emerin assembly into the reforming nuclear envelope.";
RL J. Cell Sci. 114:4575-4585(2001).
RN [15]
RP INTERACTION WITH YTHDC1.
RX PubMed=12755701; DOI=10.1046/j.1432-1033.2003.03617.x;
RA Wilkinson F.L., Holaska J.M., Zhang Z., Sharma A., Manilal S., Holt I.,
RA Stamm S., Wilson K.L., Morris G.E.;
RT "Emerin interacts in vitro with the splicing-associated factor, YT521-B.";
RL Eur. J. Biochem. 270:2459-2466(2003).
RN [16]
RP INTERACTION WITH GMCL.
RX PubMed=12493765; DOI=10.1074/jbc.m208811200;
RA Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L.;
RT "Transcriptional repressor germ cell-less (GCL) and barrier to
RT autointegration factor (BAF) compete for binding to emerin in vitro.";
RL J. Biol. Chem. 278:6969-6975(2003).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [18]
RP INTERACTION WITH BCLAF1, AND CHARACTERIZATION OF VARIANT EDMD1 PHE-54.
RX PubMed=15009215; DOI=10.1111/j.1432-1033.2004.04007.x;
RA Haraguchi T., Holaska J.M., Yamane M., Koujin T., Hashiguchi N., Mori C.,
RA Wilson K.L., Hiraoka Y.;
RT "Emerin binding to Btf, a death-promoting transcriptional repressor, is
RT disrupted by a missense mutation that causes Emery-Dreifuss muscular
RT dystrophy.";
RL Eur. J. Biochem. 271:1035-1045(2004).
RN [19]
RP FUNCTION, INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN, MUTAGENESIS OF SER-196
RP AND SER-197, AND CHARACTERIZATION OF VARIANTS EDMD1 PHE-54; HIS-133 AND
RP HIS-183.
RX PubMed=15328537; DOI=10.1371/journal.pbio.0020231;
RA Holaska J.M., Kowalski A.K., Wilson K.L.;
RT "Emerin caps the pointed end of actin filaments: evidence for an actin
RT cortical network at the nuclear inner membrane.";
RL PLoS Biol. 2:1354-1362(2004).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [22]
RP FUNCTION, AND INTERACTION WITH CTNNB1.
RX PubMed=16858403; DOI=10.1038/sj.emboj.7601230;
RA Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H.,
RA Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V.,
RA Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J.;
RT "The inner nuclear membrane protein emerin regulates beta-catenin activity
RT by restricting its accumulation in the nucleus.";
RL EMBO J. 25:3275-3285(2006).
RN [23]
RP PHOSPHORYLATION AT SER-49, SUBCELLULAR LOCATION, INTERACTION WITH LMNA,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-49.
RX PubMed=16972941; DOI=10.1111/j.1742-4658.2006.05464.x;
RA Roberts R.C., Sutherland-Smith A.J., Wheeler M.A., Jensen O.N.,
RA Emerson L.J., Spiliotis I.I., Tate C.G., Kendrick-Jones J., Ellis J.A.;
RT "The Emery-Dreifuss muscular dystrophy associated-protein emerin is
RT phosphorylated on serine 49 by protein kinase A.";
RL FEBS J. 273:4562-4575(2006).
RN [24]
RP FUNCTION.
RX PubMed=16680152; DOI=10.1038/nature04682;
RA Jacque J.-M., Stevenson M.;
RT "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity.";
RL Nature 441:641-645(2006).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BETA-TUBULIN.
RX PubMed=17785515; DOI=10.1083/jcb.200702026;
RA Salpingidou G., Smertenko A., Hausmanowa-Petrucewicz I., Hussey P.J.,
RA Hutchison C.J.;
RT "A novel role for the nuclear membrane protein emerin in association of the
RT centrosome to the outer nuclear membrane.";
RL J. Cell Biol. 178:897-904(2007).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-54; SER-60 AND
RP SER-87, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LMNA.
RX PubMed=19323649; DOI=10.1042/bc20080175;
RA Capanni C., Del Coco R., Mattioli E., Camozzi D., Columbaro M., Schena E.,
RA Merlini L., Squarzoni S., Maraldi N.M., Lattanzi G.;
RT "Emerin-prelamin A interplay in human fibroblasts.";
RL Biol. Cell 101:541-554(2009).
RN [31]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19167377; DOI=10.1016/j.ydbio.2008.12.038;
RA Mamada H., Takahashi N., Taira M.;
RT "Involvement of an inner nuclear membrane protein, Nemp1, in Xenopus neural
RT development through an interaction with the chromatin protein BAF.";
RL Dev. Biol. 327:497-507(2009).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-8 AND SER-171, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [36]
RP INTERACTION WITH TMEM201.
RX PubMed=21610090; DOI=10.1242/jcs.078923;
RA Gudise S., Figueroa R.A., Lindberg R., Larsson V., Hallberg E.;
RT "Samp1 is functionally associated with the LINC complex and A-type lamina
RT networks.";
RL J. Cell Sci. 124:2077-2085(2011).
RN [37]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-29; SER-49; SER-60;
RP SER-87; SER-98; SER-171 AND SER-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [43]
RP STRUCTURE BY NMR OF 2-54.
RX PubMed=11470279; DOI=10.1016/s0014-5793(01)02649-7;
RA Wolff N., Gilquin B., Courchay K., Callebaut I., Worman H.J.,
RA Zinn-Justin S.;
RT "Structural analysis of emerin, an inner nuclear membrane protein mutated
RT in X-linked Emery-Dreifuss muscular dystrophy.";
RL FEBS Lett. 501:171-176(2001).
RN [44]
RP STRUCTURE BY NMR OF 2-54.
RX PubMed=11435115; DOI=10.1016/s0969-2126(01)00611-6;
RA Laguri C., Gilquin B., Wolff N., Romi-Lebrun R., Courchay K., Callebaut I.,
RA Worman H.J., Zinn-Justin S.;
RT "Structural characterization of the LEM motif common to three human inner
RT nuclear membrane proteins.";
RL Structure 9:503-511(2001).
RN [45]
RP VARIANTS EDMD1 HIS-183 AND THR-183.
RX PubMed=10323252; DOI=10.1007/s004390050946;
RA Ellis J.A., Yates J.R.W., Kendrick-Jones J., Brown C.A.;
RT "Changes at P183 of emerin weaken its protein-protein interactions
RT resulting in X-linked Emery-Dreifuss muscular dystrophy.";
RL Hum. Genet. 104:262-268(1999).
RN [46]
RP VARIANT EDMD1 HIS-133.
RX PubMed=11587540; DOI=10.1006/bbrc.2001.5708;
RA Holt I., Clements L., Manilal S., Morris G.E.;
RT "How does a g993t mutation in the emerin gene cause Emery-Dreifuss muscular
RT dystrophy?";
RL Biochem. Biophys. Res. Commun. 287:1129-1133(2001).
CC -!- FUNCTION: Stabilizes and promotes the formation of a nuclear actin
CC cortical network. Stimulates actin polymerization in vitro by binding
CC and stabilizing the pointed end of growing filaments. Inhibits beta-
CC catenin activity by preventing its accumulation in the nucleus. Acts by
CC influencing the nuclear accumulation of beta-catenin through a CRM1-
CC dependent export pathway. Links centrosomes to the nuclear envelope via
CC a microtubule association. EMD and BAF are cooperative cofactors of
CC HIV-1 infection. Association of EMD with the viral DNA requires the
CC presence of BAF and viral integrase. The association of viral DNA with
CC chromatin requires the presence of BAF and EMD. Required for proper
CC localization of non-farnesylated prelamin-A/C.
CC {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152,
CC ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515,
CC ECO:0000269|PubMed:19323649}.
CC -!- SUBUNIT: Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and
CC YTHDC1/YT521. Interacts with TMEM43; the interaction retains emerin in
CC the nuclear inner membrane. Interacts with SUN1 and SUN2 (By
CC similarity). Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta-
CC tubulin. Interacts with TMEM201. {ECO:0000250,
CC ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12493765,
CC ECO:0000269|PubMed:12755701, ECO:0000269|PubMed:15009215,
CC ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16858403,
CC ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:17785515,
CC ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:21610090}.
CC -!- INTERACTION:
CC P50402; Q9ULW3: ABT1; NbExp=6; IntAct=EBI-489887, EBI-2602396;
CC P50402; P60709: ACTB; NbExp=2; IntAct=EBI-489887, EBI-353944;
CC P50402; Q8WTP8: AEN; NbExp=3; IntAct=EBI-489887, EBI-8637627;
CC P50402; P16157-17: ANK1; NbExp=3; IntAct=EBI-489887, EBI-941819;
CC P50402; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-489887, EBI-7054139;
CC P50402; Q5T686: AVPI1; NbExp=3; IntAct=EBI-489887, EBI-8640233;
CC P50402; O75531: BANF1; NbExp=13; IntAct=EBI-489887, EBI-1055977;
CC P50402; Q9NYF8: BCLAF1; NbExp=3; IntAct=EBI-489887, EBI-437804;
CC P50402; Q8N7W2-2: BEND7; NbExp=9; IntAct=EBI-489887, EBI-10181188;
CC P50402; Q13895: BYSL; NbExp=6; IntAct=EBI-489887, EBI-358049;
CC P50402; Q8NEC5: CATSPER1; NbExp=9; IntAct=EBI-489887, EBI-744545;
CC P50402; Q8N5R6: CCDC33; NbExp=3; IntAct=EBI-489887, EBI-740841;
CC P50402; Q96S94-5: CCNL2; NbExp=3; IntAct=EBI-489887, EBI-12024864;
CC P50402; P20138: CD33; NbExp=3; IntAct=EBI-489887, EBI-3906571;
CC P50402; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-489887, EBI-739624;
CC P50402; Q9HA82: CERS4; NbExp=3; IntAct=EBI-489887, EBI-2622997;
CC P50402; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-489887, EBI-1045797;
CC P50402; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-489887, EBI-17710733;
CC P50402; P21964: COMT; NbExp=3; IntAct=EBI-489887, EBI-372265;
CC P50402; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-489887, EBI-18013275;
CC P50402; O43889-2: CREB3; NbExp=3; IntAct=EBI-489887, EBI-625022;
CC P50402; P35222: CTNNB1; NbExp=3; IntAct=EBI-489887, EBI-491549;
CC P50402; Q5JRM2: CXorf66; NbExp=3; IntAct=EBI-489887, EBI-12823659;
CC P50402; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-489887, EBI-2349927;
CC P50402; Q96PL5: ERMAP; NbExp=3; IntAct=EBI-489887, EBI-13361852;
CC P50402; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-489887, EBI-18304435;
CC P50402; Q969F0: FATE1; NbExp=10; IntAct=EBI-489887, EBI-743099;
CC P50402; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-489887, EBI-3917143;
CC P50402; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-489887, EBI-13345167;
CC P50402; Q8IUY3: GRAMD2A; NbExp=3; IntAct=EBI-489887, EBI-11984319;
CC P50402; O75031: HSF2BP; NbExp=3; IntAct=EBI-489887, EBI-7116203;
CC P50402; Q0VD86: INCA1; NbExp=3; IntAct=EBI-489887, EBI-6509505;
CC P50402; Q8N6L0: KASH5; NbExp=8; IntAct=EBI-489887, EBI-749265;
CC P50402; Q14500: KCNJ12; NbExp=3; IntAct=EBI-489887, EBI-11794596;
CC P50402; B7U540: KCNJ18; NbExp=3; IntAct=EBI-489887, EBI-19949648;
CC P50402; Q15842: KCNJ8; NbExp=3; IntAct=EBI-489887, EBI-17440235;
CC P50402; Q9UGI6-2: KCNN3; NbExp=3; IntAct=EBI-489887, EBI-17888181;
CC P50402; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-489887, EBI-8472129;
CC P50402; P43628: KIR2DL3; NbExp=3; IntAct=EBI-489887, EBI-8632435;
CC P50402; Q9H400: LIME1; NbExp=3; IntAct=EBI-489887, EBI-2830566;
CC P50402; P02545: LMNA; NbExp=7; IntAct=EBI-489887, EBI-351935;
CC P50402; P02545-1: LMNA; NbExp=4; IntAct=EBI-489887, EBI-351949;
CC P50402; Q9P127: LUZP4; NbExp=9; IntAct=EBI-489887, EBI-10198848;
CC P50402; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-489887, EBI-10268010;
CC P50402; P50221: MEOX1; NbExp=3; IntAct=EBI-489887, EBI-2864512;
CC P50402; P50222: MEOX2; NbExp=3; IntAct=EBI-489887, EBI-748397;
CC P50402; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-489887, EBI-16439278;
CC P50402; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-489887, EBI-6163737;
CC P50402; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-489887, EBI-2514313;
CC P50402; Q7Z6M4: MTERF4; NbExp=3; IntAct=EBI-489887, EBI-948435;
CC P50402; Q6IBW4-4: NCAPH2; NbExp=3; IntAct=EBI-489887, EBI-10247000;
CC P50402; P35240-4: NF2; NbExp=3; IntAct=EBI-489887, EBI-1014514;
CC P50402; Q9NQX5: NPDC1; NbExp=3; IntAct=EBI-489887, EBI-748927;
CC P50402; Q9P286: PAK5; NbExp=3; IntAct=EBI-489887, EBI-741896;
CC P50402; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-489887, EBI-2568609;
CC P50402; Q04864-2: REL; NbExp=3; IntAct=EBI-489887, EBI-10829018;
CC P50402; O60930: RNASEH1; NbExp=3; IntAct=EBI-489887, EBI-2372399;
CC P50402; Q99962: SH3GL2; NbExp=2; IntAct=EBI-489887, EBI-77938;
CC P50402; A6NEL2: SOWAHB; NbExp=3; IntAct=EBI-489887, EBI-23696033;
CC P50402; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-489887, EBI-17280858;
CC P50402; Q16623: STX1A; NbExp=3; IntAct=EBI-489887, EBI-712466;
CC P50402; Q12846: STX4; NbExp=3; IntAct=EBI-489887, EBI-744942;
CC P50402; Q9UH99: SUN2; NbExp=4; IntAct=EBI-489887, EBI-1044964;
CC P50402; Q8NF91-3: SYNE1; NbExp=5; IntAct=EBI-489887, EBI-10760352;
CC P50402; Q8NF91-11: SYNE1; NbExp=3; IntAct=EBI-489887, EBI-10758913;
CC P50402; Q8WXH0-3: SYNE2; NbExp=5; IntAct=EBI-489887, EBI-10760388;
CC P50402; Q7RTU1: TCF23; NbExp=3; IntAct=EBI-489887, EBI-12127592;
CC P50402; Q8WUU8: TMEM174; NbExp=3; IntAct=EBI-489887, EBI-10276729;
CC P50402; Q86VY9: TMEM200A; NbExp=3; IntAct=EBI-489887, EBI-11732844;
CC P50402; Q5SNT2-2: TMEM201; NbExp=4; IntAct=EBI-489887, EBI-11994282;
CC P50402; Q9BTV4: TMEM43; NbExp=5; IntAct=EBI-489887, EBI-721293;
CC P50402; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-489887, EBI-18178701;
CC P50402; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-489887, EBI-11742770;
CC P50402; Q9Y320: TMX2; NbExp=3; IntAct=EBI-489887, EBI-6447886;
CC P50402; Q9Y228: TRAF3IP3; NbExp=9; IntAct=EBI-489887, EBI-765817;
CC P50402; Q8IWZ5: TRIM42; NbExp=6; IntAct=EBI-489887, EBI-5235829;
CC P50402; O95292: VAPB; NbExp=3; IntAct=EBI-489887, EBI-1188298;
CC P50402; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-489887, EBI-2555749;
CC P50402; Q9NU63-3: ZFP57; NbExp=3; IntAct=EBI-489887, EBI-12879708;
CC P50402; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-489887, EBI-711679;
CC P50402; P49910: ZNF165; NbExp=3; IntAct=EBI-489887, EBI-741694;
CC P50402; Q53Z40: ZNF165; NbExp=3; IntAct=EBI-489887, EBI-10186058;
CC P50402; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-489887, EBI-749023;
CC P50402; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-489887, EBI-7233259;
CC P50402; Q9BYN7: ZNF341; NbExp=3; IntAct=EBI-489887, EBI-9089622;
CC P50402; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-489887, EBI-8643207;
CC P50402; Q6P9A3: ZNF549; NbExp=3; IntAct=EBI-489887, EBI-13046342;
CC P50402; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-489887, EBI-10251462;
CC P50402; P68135: ACTA1; Xeno; NbExp=3; IntAct=EBI-489887, EBI-367540;
CC P50402; Q9D666: Sun1; Xeno; NbExp=4; IntAct=EBI-489887, EBI-6752574;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:19167377}; Single-pass membrane protein;
CC Nucleoplasmic side {ECO:0000269|PubMed:19167377}. Nucleus outer
CC membrane. Note=Colocalized with BANF1 at the central region of the
CC assembling nuclear rim, near spindle-attachment sites. The accumulation
CC of different intermediates of prelamin-A/C (non-farnesylated or
CC carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its
CC localization in the nucleus.
CC -!- TISSUE SPECIFICITY: Skeletal muscle, heart, colon, testis, ovary and
CC pancreas.
CC -!- PTM: Found in four different phosphorylated forms, three of which
CC appear to be associated with the cell cycle.
CC {ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:9472006}.
CC -!- DISEASE: Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1)
CC [MIM:310300]: A form of Emery-Dreifuss muscular dystrophy, a
CC degenerative myopathy characterized by weakness and atrophy of muscle
CC without involvement of the nervous system, early contractures of the
CC elbows, Achilles tendons and spine, and cardiomyopathy associated with
CC cardiac conduction defects. {ECO:0000269|PubMed:10323252,
CC ECO:0000269|PubMed:11587540, ECO:0000269|PubMed:15009215,
CC ECO:0000269|PubMed:15328537}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=EMD db; Note=EMD mutation database;
CC URL="https://databases.lovd.nl/shared/genes/EMD";
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DR EMBL; X82434; CAA57817.1; -; mRNA.
DR EMBL; L44140; AAA92645.1; -; Genomic_DNA.
DR EMBL; D64111; BAA10972.1; -; Genomic_DNA.
DR EMBL; X86810; CAA60500.1; -; Genomic_DNA.
DR EMBL; BT007401; AAP36065.1; -; mRNA.
DR EMBL; CR536536; CAG38773.1; -; mRNA.
DR EMBL; BX936346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72742.1; -; Genomic_DNA.
DR EMBL; BC000738; AAH00738.1; -; mRNA.
DR CCDS; CCDS14745.1; -.
DR PIR; S50834; S50834.
DR RefSeq; NP_000108.1; NM_000117.2.
DR PDB; 1JEI; NMR; -; A=2-54.
DR PDB; 2ODC; NMR; -; I=2-47.
DR PDB; 2ODG; NMR; -; C=2-47.
DR PDB; 6GHD; X-ray; 2.10 A; G/H=2-45.
DR PDB; 6RPR; X-ray; 2.26 A; G=2-44.
DR PDB; 7NDY; X-ray; 1.44 A; G=2-187.
DR PDBsum; 1JEI; -.
DR PDBsum; 2ODC; -.
DR PDBsum; 2ODG; -.
DR PDBsum; 6GHD; -.
DR PDBsum; 6RPR; -.
DR PDBsum; 7NDY; -.
DR AlphaFoldDB; P50402; -.
DR BMRB; P50402; -.
DR SMR; P50402; -.
DR BioGRID; 108325; 711.
DR CORUM; P50402; -.
DR DIP; DIP-34638N; -.
DR IntAct; P50402; 236.
DR MINT; P50402; -.
DR STRING; 9606.ENSP00000358857; -.
DR GlyGen; P50402; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; P50402; -.
DR MetOSite; P50402; -.
DR PhosphoSitePlus; P50402; -.
DR SwissPalm; P50402; -.
DR BioMuta; EMD; -.
DR DMDM; 1706639; -.
DR EPD; P50402; -.
DR jPOST; P50402; -.
DR MassIVE; P50402; -.
DR PaxDb; P50402; -.
DR PeptideAtlas; P50402; -.
DR PRIDE; P50402; -.
DR ProteomicsDB; 56218; -.
DR TopDownProteomics; P50402; -.
DR Antibodypedia; 371; 493 antibodies from 40 providers.
DR DNASU; 2010; -.
DR Ensembl; ENST00000369842.9; ENSP00000358857.4; ENSG00000102119.12.
DR Ensembl; ENST00000683627.1; ENSP00000507533.1; ENSG00000102119.12.
DR GeneID; 2010; -.
DR KEGG; hsa:2010; -.
DR MANE-Select; ENST00000369842.9; ENSP00000358857.4; NM_000117.3; NP_000108.1.
DR UCSC; uc004fkl.4; human.
DR CTD; 2010; -.
DR DisGeNET; 2010; -.
DR GeneCards; EMD; -.
DR GeneReviews; EMD; -.
DR HGNC; HGNC:3331; EMD.
DR HPA; ENSG00000102119; Low tissue specificity.
DR MalaCards; EMD; -.
DR MIM; 300384; gene.
DR MIM; 310300; phenotype.
DR neXtProt; NX_P50402; -.
DR OpenTargets; ENSG00000102119; -.
DR Orphanet; 98863; X-linked Emery-Dreifuss muscular dystrophy.
DR PharmGKB; PA27766; -.
DR VEuPathDB; HostDB:ENSG00000102119; -.
DR eggNOG; ENOG502S5SJ; Eukaryota.
DR GeneTree; ENSGT00390000002034; -.
DR HOGENOM; CLU_095531_0_0_1; -.
DR InParanoid; P50402; -.
DR OMA; DRERPIY; -.
DR OrthoDB; 1219474at2759; -.
DR PhylomeDB; P50402; -.
DR TreeFam; TF337236; -.
DR PathwayCommons; P50402; -.
DR Reactome; R-HSA-2980766; Nuclear Envelope Breakdown.
DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; P50402; -.
DR SIGNOR; P50402; -.
DR BioGRID-ORCS; 2010; 10 hits in 709 CRISPR screens.
DR ChiTaRS; EMD; human.
DR EvolutionaryTrace; P50402; -.
DR GeneWiki; Emerin; -.
DR GenomeRNAi; 2010; -.
DR Pharos; P50402; Tbio.
DR PRO; PR:P50402; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P50402; protein.
DR Bgee; ENSG00000102119; Expressed in left ovary and 202 other tissues.
DR ExpressionAtlas; P50402; baseline and differential.
DR Genevisible; P50402; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:LIFEdb.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:FlyBase.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR CDD; cd12939; LEM_emerin; 1.
DR DisProt; DP01770; -.
DR Gene3D; 1.10.720.40; -; 1.
DR InterPro; IPR035004; Emerin.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR InterPro; IPR034989; LEM_emerin.
DR PANTHER; PTHR15171; PTHR15171; 1.
DR Pfam; PF03020; LEM; 1.
DR SMART; SM00540; LEM; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cardiomyopathy;
KW Direct protein sequencing; Disease variant;
KW Emery-Dreifuss muscular dystrophy; Membrane; Microtubule; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Emerin"
FT /id="PRO_0000206140"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..45
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 46..222
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000305"
FT REGION 168..186
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000269|PubMed:16858403"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 49
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:16972941,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63190"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63190"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63190"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08579"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08579"
FT VARIANT 54
FT /note="S -> F (in EDMD1; no loss of binding to F-actin,
FT enhanced rate of actin polymerization and loss of binding
FT to BCLAF1)"
FT /evidence="ECO:0000269|PubMed:15009215,
FT ECO:0000269|PubMed:15328537"
FT /id="VAR_005198"
FT VARIANT 133
FT /note="Q -> H (in EDMD1; loss of binding to F-actin)"
FT /evidence="ECO:0000269|PubMed:11587540,
FT ECO:0000269|PubMed:15328537"
FT /id="VAR_016016"
FT VARIANT 149
FT /note="D -> H (in dbSNP:rs2070818)"
FT /id="VAR_038433"
FT VARIANT 183
FT /note="P -> H (in EDMD1; no loss of binding to F-actin and
FT enhanced rate of actin polymerization; dbSNP:rs104894805)"
FT /evidence="ECO:0000269|PubMed:10323252,
FT ECO:0000269|PubMed:15328537"
FT /id="VAR_005199"
FT VARIANT 183
FT /note="P -> T (in EDMD1; dbSNP:rs104894806)"
FT /evidence="ECO:0000269|PubMed:10323252"
FT /id="VAR_005200"
FT MUTAGEN 49
FT /note="S->A: Abolishes phosphorylation. No effect on
FT targeting to nuclear envelope nor on interaction with
FT LMNA."
FT /evidence="ECO:0000269|PubMed:16972941"
FT MUTAGEN 49
FT /note="S->E: Mimics phosphorylation. No effect on targeting
FT to nuclear envelope nor on interaction with LMNA."
FT /evidence="ECO:0000269|PubMed:16972941"
FT MUTAGEN 196
FT /note="S->A: No loss of binding to F-actin; when associated
FT with A-197."
FT /evidence="ECO:0000269|PubMed:15328537"
FT MUTAGEN 197
FT /note="S->A: No loss of binding to F-actin; when associated
FT with A-196."
FT /evidence="ECO:0000269|PubMed:15328537"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:7NDY"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:7NDY"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:7NDY"
SQ SEQUENCE 254 AA; 28994 MW; EB62EDD59B7A044F CRC64;
MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP PSSSAASSYS
FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF TTRTYGEPES AGPSRAVRQS
VTSFPDADAF HHQVHDDDLL SSSEEECKDR ERPMYGRDSA YQSITHYRPV SASRSSLDLS
YYPTSSSTSF MSSSSSSSSW LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF
FIYHFMQAEE GNPF
