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 11-NOV-2015, entry version 172. DE RecName: Full=Emerin; GN Name=EMD; Synonyms=EDMD, STA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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- RT Dreifuss 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., RA Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., RA D'Urso M.; RT "Long-range sequence analysis in Xq28: thirteen known and six RT candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and RT 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 RT muscular 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., RA Merlini L., Morandi L., Kress W., Yates J.R.W., Warren S.T., RA Toniolo D.; RT "Identification of new mutations in the Emery-Dreifuss muscular RT dystrophy gene and evidence for genetic heterogeneity of the RT 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 RT 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., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA 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., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA 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., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA 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., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA 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., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric 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 RP MET-1, 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; RA Ellis J.A., Craxton M., Yates J.R.W., Kendrick-Jones J.; RT "Aberrant intracellular targeting and cell cycle-dependent RT phosphorylation of emerin contribute to the Emery-Dreifuss muscular RT dystrophy phenotype."; RL J. Cell Sci. 111:781-792(1998). RN [14] RP INTERACTION WITH BANF1. RX PubMed=11792822; 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 RT 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., RA Holt I., Stamm S., Wilson K.L., Morris G.E.; RT "Emerin interacts in vitro with the splicing-associated factor, YT521- RT 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 RT from human T cells using immobilized metal affinity chromatography and RT tandem 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., RA Mori C., Wilson K.L., Hiraoka Y.; RT "Emerin binding to Btf, a death-promoting transcriptional repressor, RT is disrupted by a missense mutation that causes Emery-Dreifuss RT muscular dystrophy."; RL Eur. J. Biochem. 271:1035-1045(2004). RN [19] RP FUNCTION, INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN, MUTAGENESIS OF RP SER-196 AND SER-197, AND CHARACTERIZATION OF VARIANTS EDMD1 PHE-54; RP HIS-133 AND 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 RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION RP BY 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling 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., RA Broers J.L.V., Blankesteijn W.M., Salpingidou G., Wilson R.G., RA Ellis J.A., Hutchison C.J.; RT "The inner nuclear membrane protein emerin regulates beta-catenin RT activity 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 RP LMNA, 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., RA 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 RT 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 RT of the 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 RP BY 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., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION RP BY 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 RT the 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 RP 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 RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a 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., RA Schena E., 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 RT neural development through an interaction with the chromatin protein RT BAF."; RL Dev. Biol. 327:497-507(2009). RN [32] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS 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 RP BY 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 RP SCALE ANALYSIS] AT SER-8 AND SER-171, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS 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., RA Meinnel T., 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 [38] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS 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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [40] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., 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 [41] 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 RT mutated in X-linked Emery-Dreifuss muscular dystrophy."; RL FEBS Lett. 501:171-176(2001). RN [42] 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., RA Callebaut I., Worman H.J., Zinn-Justin S.; RT "Structural characterization of the LEM motif common to three human RT inner nuclear membrane proteins."; RL Structure 9:503-511(2001). RN [43] 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 [44] 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 RT muscular 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 CC binding and stabilizing the pointed end of growing filaments. CC Inhibits beta-catenin activity by preventing its accumulation in CC the nucleus. Acts by influencing the nuclear accumulation of beta- CC catenin through a CRM1-dependent export pathway. Links centrosomes CC to the nuclear envelope via a microtubule association. EMD and BAF CC are cooperative cofactors of HIV-1 infection. Association of EMD CC with the viral DNA requires the presence of BAF and viral CC integrase. The association of viral DNA with chromatin requires CC the presence of BAF and EMD. Required for proper localization of CC non-farnesylated prelamin-A/C. {ECO:0000269|PubMed:15328537, CC ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, CC ECO:0000269|PubMed:17785515, 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 CC emerin in the nuclear inner membrane. Interacts with SUN1 and SUN2 CC (By similarity). Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and CC beta-tubulin. {ECO:0000250, ECO:0000269|PubMed:11792822, CC ECO:0000269|PubMed:12493765, ECO:0000269|PubMed:12755701, CC ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:15328537, CC ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:16972941, CC ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649}. CC -!- INTERACTION: CC Q9ULW3:ABT1; NbExp=3; IntAct=EBI-489887, EBI-2602396; CC Q8WTP8:AEN; NbExp=3; IntAct=EBI-489887, EBI-8637627; CC Q9NYF8:BCLAF1; NbExp=3; IntAct=EBI-489887, EBI-437804; CC Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-489887, EBI-10181188; CC Q13895:BYSL; NbExp=3; IntAct=EBI-489887, EBI-358049; CC Q8NEC5:CATSPER1; NbExp=3; IntAct=EBI-489887, EBI-744545; CC Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-489887, EBI-739624; CC P35222:CTNNB1; NbExp=3; IntAct=EBI-489887, EBI-491549; CC Q5JST6:EFHC2; NbExp=3; IntAct=EBI-489887, EBI-2349927; CC Q969F0:FATE1; NbExp=4; IntAct=EBI-489887, EBI-743099; CC Q9P127:LUZP4; NbExp=3; IntAct=EBI-489887, EBI-10198848; CC Q8N8X9:MAB21L3; NbExp=3; IntAct=EBI-489887, EBI-10268010; CC Q8TB93:PAK7; NbExp=3; IntAct=EBI-489887, EBI-741896; CC Q99962:SH3GL2; NbExp=2; IntAct=EBI-489887, EBI-77938; CC Q9D666:Sun1 (xeno); NbExp=4; IntAct=EBI-489887, EBI-6752574; CC Q9UH99:SUN2; NbExp=3; IntAct=EBI-489887, EBI-1044964; CC Q8NF91-11:SYNE1; NbExp=3; IntAct=EBI-489887, EBI-10758913; CC Q8NF91-3:SYNE1; NbExp=5; IntAct=EBI-489887, EBI-10760352; CC Q8WXH0-3:SYNE2; NbExp=5; IntAct=EBI-489887, EBI-10760388; CC Q9Y228:TRAF3IP3; NbExp=3; IntAct=EBI-489887, EBI-765817; CC A1L4B6:TRIM42; NbExp=3; IntAct=EBI-489887, EBI-10172216; CC Q53Z40:ZNF165; NbExp=3; IntAct=EBI-489887, EBI-10186058; CC Q9UNY5:ZNF232; NbExp=3; IntAct=EBI-489887, EBI-749023; 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 CC accumulation of different intermediates of prelamin-A/C (non- CC farnesylated or carboxymethylated farnesylated prelamin-A/C) in CC fibroblasts modify its localization in the nucleus. CC -!- TISSUE SPECIFICITY: Skeletal muscle, heart, colon, testis, ovary CC and 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 CC muscle without involvement of the nervous system, early CC contractures of the elbows, Achilles tendons and spine, and CC cardiomyopathy associated with cardiac conduction defects. CC {ECO:0000269|PubMed:10323252, ECO:0000269|PubMed:11587540}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Contains 1 LEM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00313}. CC -!- WEB RESOURCE: Name=EMD db; Note="EMD mutation database"; CC URL="http://www.dmd.nl/nmdb/index.php?select_db=EMD"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CAI43228.1; -; 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 UniGene; Hs.522823; -. DR PDB; 1JEI; NMR; -; A=2-54. DR PDB; 2ODC; NMR; -; I=2-47. DR PDB; 2ODG; NMR; -; C=2-47. DR PDBsum; 1JEI; -. DR PDBsum; 2ODC; -. DR PDBsum; 2ODG; -. DR ProteinModelPortal; P50402; -. DR SMR; P50402; 2-54. DR BioGrid; 108325; 149. DR DIP; DIP-34638N; -. DR IntAct; P50402; 50. DR MINT; MINT-266014; -. DR STRING; 9606.ENSP00000358857; -. DR PhosphoSite; P50402; -. DR BioMuta; EMD; -. DR DMDM; 1706639; -. DR MaxQB; P50402; -. DR PaxDb; P50402; -. DR PeptideAtlas; P50402; -. DR PRIDE; P50402; -. DR DNASU; 2010; -. DR Ensembl; ENST00000369842; ENSP00000358857; ENSG00000102119. DR GeneID; 2010; -. DR KEGG; hsa:2010; -. DR UCSC; uc004fkl.3; human. DR CTD; 2010; -. DR GeneCards; EMD; -. DR GeneReviews; EMD; -. DR HGNC; HGNC:3331; EMD. DR HPA; CAB001545; -. DR HPA; CAB002029; -. DR HPA; CAB062552; -. DR HPA; HPA000609; -. DR MIM; 300384; gene. DR MIM; 310300; phenotype. DR neXtProt; NX_P50402; -. DR Orphanet; 98863; X-linked Emery-Dreifuss muscular dystrophy. DR PharmGKB; PA27766; -. DR eggNOG; ENOG410IJ10; Eukaryota. DR eggNOG; ENOG410ZEWX; LUCA. DR GeneTree; ENSGT00390000002034; -. DR HOGENOM; HOG000081509; -. DR HOVERGEN; HBG001099; -. DR InParanoid; P50402; -. DR KO; K12569; -. DR OMA; SVDSDMY; -. DR PhylomeDB; P50402; -. DR TreeFam; TF337236; -. DR Reactome; R-HSA-2993913; Clearance of Nuclear Envelope Membranes from Chromatin. DR Reactome; R-HSA-2995383; Initiation of Nuclear Envelope Reformation. DR Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina. DR EvolutionaryTrace; P50402; -. DR GeneWiki; Emerin; -. DR GenomeRNAi; 2010; -. DR NextBio; 8137; -. DR PRO; PR:P50402; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; P50402; -. DR CleanEx; HS_EMD; -. DR ExpressionAtlas; P50402; baseline and differential. DR Genevisible; P50402; HS. 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; IDA: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:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome. DR GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc. DR GO; GO:0035414; P:negative regulation of catenin import into nucleus; IMP:BHF-UCL. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL. 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 Gene3D; 1.10.720.40; -; 1. DR InterPro; IPR011015; LEM/LEM-like_dom. DR InterPro; IPR003887; LEM_dom. 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 Complete proteome; Direct protein sequencing; Disease mutation; KW Emery-Dreifuss muscular dystrophy; Membrane; Microtubule; Nucleus; KW Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 254 Emerin. FT /FTId=PRO_0000206140. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT DOMAIN 1 45 LEM. {ECO:0000255|PROSITE- FT ProRule:PRU00313}. FT REGION 46 222 Interaction with F-actin. {ECO:0000305}. FT REGION 168 186 Interaction with CTNNB1. FT COMPBIAS 192 199 Poly-Ser. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:19369195, FT ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000244|PubMed:25944712, FT ECO:0000269|Ref.11}. FT MOD_RES 8 8 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 29 29 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 49 49 Phosphoserine; by PKA. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000269|PubMed:16972941}. FT MOD_RES 54 54 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 60 60 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332}. FT MOD_RES 87 87 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 141 141 Phosphoserine. FT {ECO:0000250|UniProtKB:Q63190}. FT MOD_RES 142 142 Phosphoserine. FT {ECO:0000250|UniProtKB:Q63190}. FT MOD_RES 143 143 Phosphoserine. FT {ECO:0000250|UniProtKB:Q63190}. FT MOD_RES 161 161 Phosphotyrosine. FT {ECO:0000250|UniProtKB:O08579}. FT MOD_RES 171 171 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 175 175 Phosphoserine. FT {ECO:0000250|UniProtKB:O08579}. FT VARIANT 54 54 S -> F (in EDMD1; no loss of binding to FT F-actin, enhanced rate of actin FT polymerization and loss of binding to FT BCLAF1). {ECO:0000269|PubMed:15009215, FT ECO:0000269|PubMed:15328537}. FT /FTId=VAR_005198. FT VARIANT 133 133 Q -> H (in EDMD1; loss of binding to F- FT actin). {ECO:0000269|PubMed:11587540, FT ECO:0000269|PubMed:15328537}. FT /FTId=VAR_016016. FT VARIANT 149 149 D -> H (in dbSNP:rs2070818). FT /FTId=VAR_038433. FT VARIANT 183 183 P -> H (in EDMD1; no loss of binding to FT F-actin and enhanced rate of actin FT polymerization). FT {ECO:0000269|PubMed:10323252, FT ECO:0000269|PubMed:15328537}. FT /FTId=VAR_005199. FT VARIANT 183 183 P -> T (in EDMD1). FT {ECO:0000269|PubMed:10323252}. FT /FTId=VAR_005200. FT MUTAGEN 49 49 S->A: Abolishes phosphorylation. No FT effect on targeting to nuclear envelope FT nor on interaction with LMNA. FT {ECO:0000269|PubMed:16972941}. FT MUTAGEN 49 49 S->E: Mimics phosphorylation. No effect FT on targeting to nuclear envelope nor on FT interaction with LMNA. FT {ECO:0000269|PubMed:16972941}. FT MUTAGEN 196 196 S->A: No loss of binding to F-actin; when FT associated with A-197. FT {ECO:0000269|PubMed:15328537}. FT MUTAGEN 197 197 S->A: No loss of binding to F-actin; when FT associated with A-196. FT {ECO:0000269|PubMed:15328537}. FT TURN 4 6 {ECO:0000244|PDB:1JEI}. FT HELIX 9 16 {ECO:0000244|PDB:1JEI}. FT STRAND 17 19 {ECO:0000244|PDB:1JEI}. FT HELIX 29 31 {ECO:0000244|PDB:1JEI}. FT HELIX 32 37 {ECO:0000244|PDB:1JEI}. FT HELIX 40 42 {ECO:0000244|PDB:1JEI}. 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 //