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P50402 (EMD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Emerin
Gene names
Name:EMD
Synonyms:EDMD, STA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.19 Ref.22 Ref.24 Ref.25 Ref.30

Subunit structure

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. Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.22 Ref.23 Ref.25 Ref.30

Subcellular location

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. Ref.12 Ref.13 Ref.23 Ref.25 Ref.30

Tissue specificity

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

Post-translational modification

Found in four different phosphorylated forms, three of which appear to be associated with the cell cycle. Ref.13 Ref.23

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.40 Ref.41

Sequence similarities

Contains 1 LEM domain.

Ontologies

Keywords
   Cellular componentMembrane
Microtubule
Nucleus
   DiseaseCardiomyopathy
Disease mutation
Emery-Dreifuss muscular dystrophy
   DomainTransmembrane
Transmembrane helix
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to growth factor stimulus

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

mitotic nuclear envelope reassembly

Traceable author statement. Source: Reactome

muscle contraction

Traceable author statement Ref.1. Source: ProtInc

muscle organ development

Traceable author statement Ref.1PubMed 8589715. Source: ProtInc

negative regulation of catenin import into nucleus

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

positive regulation of protein export from nucleus

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum

Inferred from direct assay. Source: HPA

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear envelope

Inferred from direct assay Ref.22. Source: BHF-UCL

nuclear inner membrane

Non-traceable author statement Ref.22. Source: BHF-UCL

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear outer membrane

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionactin binding

Inferred from direct assay Ref.19. Source: UniProtKB

beta-tubulin binding

Inferred from direct assay Ref.25. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19PubMed 15671068Ref.22Ref.30. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Emerin
PRO_0000206140

Regions

Transmembrane223 – 24321Helical; Potential
Domain1 – 4545LEM
Region46 – 222177Interaction with F-actin Probable
Region168 – 18619Interaction with CTNNB1
Compositional bias192 – 1998Poly-Ser

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.29 Ref.31 Ref.33 Ref.35 Ref.36 Ref.37
Modified residue81Phosphoserine Ref.33
Modified residue491Phosphoserine; by PKA Ref.21 Ref.23 Ref.26 Ref.27 Ref.28
Modified residue541Phosphoserine Ref.28
Modified residue601Phosphoserine Ref.28 Ref.32
Modified residue871Phosphoserine Ref.28
Modified residue1611Phosphotyrosine By similarity
Modified residue1711Phosphoserine Ref.33

Natural variations

Natural variant541S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1. Ref.18 Ref.19
VAR_005198
Natural variant1331Q → H in EDMD1; loss of binding to F-actin. Ref.19 Ref.41
VAR_016016
Natural variant1491D → H.
Corresponds to variant rs2070818 [ dbSNP | Ensembl ].
VAR_038433
Natural variant1831P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. Ref.19 Ref.40
VAR_005199
Natural variant1831P → T in EDMD1. Ref.40
VAR_005200

Experimental info

Mutagenesis491S → A: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. Ref.23
Mutagenesis491S → E: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. Ref.23
Mutagenesis1961S → A: No loss of binding to F-actin; when associated with A-197. Ref.19
Mutagenesis1971S → A: No loss of binding to F-actin; when associated with A-196. Ref.19

Secondary structure

........... 254
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50402 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EB62EDD59B7A044F

FASTA25428,994
        10         20         30         40         50         60 
MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP PSSSAASSYS 

        70         80         90        100        110        120 
FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF TTRTYGEPES AGPSRAVRQS 

       130        140        150        160        170        180 
VTSFPDADAF HHQVHDDDLL SSSEEECKDR ERPMYGRDSA YQSITHYRPV SASRSSLDLS 

       190        200        210        220        230        240 
YYPTSSSTSF MSSSSSSSSW LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF 

       250 
FIYHFMQAEE GNPF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Immunocytochemical detection of emerin within the nuclear matrix."
Squarzoni S., Sabatelli P., Ognibene A., Toniolo D., Cartegni L., Cobianchi F., Petrini S., Merlini L., Maraldi N.M.
Neuromuscul. Disord. 8:338-344(1998) [PubMed] [Europe PMC] [Abstract]
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]"Emerin interacts in vitro with the splicing-associated factor, YT521-B."
Wilkinson F.L., Holaska J.M., Zhang Z., Sharma A., Manilal S., Holt I., Stamm S., Wilson K.L., Morris G.E.
Eur. J. Biochem. 270:2459-2466(2003) [PubMed] [Europe PMC] [Abstract]
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]"The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus."
Markiewicz E., Tilgner K., Barker N., van de Wetering M., Clevers H., Dorobek M., Hausmanowa-Petrusewicz I., Ramaekers F.C.S., Broers J.L.V., Blankesteijn W.M., Salpingidou G., Wilson R.G., Ellis J.A., Hutchison C.J.
EMBO J. 25:3275-3285(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Emerin-prelamin A interplay in human fibroblasts."
Capanni C., Del Coco R., Mattioli E., Camozzi D., Columbaro M., Schena E., Merlini L., Squarzoni S., Maraldi N.M., Lattanzi G.
Biol. Cell 101:541-554(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
[31]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

EMD db

"EMD mutation database"

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14745.1.
PIRS50834.
RefSeqNP_000108.1. NM_000117.2.
UniGeneHs.522823.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEINMR-A2-54[»]
2ODCNMR-I2-47[»]
2ODGNMR-C2-47[»]
ProteinModelPortalP50402.
SMRP50402. Positions 2-54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108325. 107 interactions.
DIPDIP-34638N.
IntActP50402. 26 interactions.
MINTMINT-266014.
STRING9606.ENSP00000358857.

PTM databases

PhosphoSiteP50402.

Polymorphism databases

DMDM1706639.

Proteomic databases

MaxQBP50402.
PaxDbP50402.
PeptideAtlasP50402.
PRIDEP50402.

Protocols and materials databases

DNASU2010.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369842; ENSP00000358857; ENSG00000102119.
ENST00000594177; ENSP00000468971; ENSG00000268557.
GeneID2010.
KEGGhsa:2010.
UCSCuc004fkl.3. human.

Organism-specific databases

CTD2010.
GeneCardsGC0XP153607.
GeneReviewsEMD.
HGNCHGNC:3331. EMD.
HPACAB001545.
CAB002029.
CAB062552.
HPA000609.
MIM300384. gene.
310300. phenotype.
neXtProtNX_P50402.
Orphanet98863. X-linked Emery-Dreifuss muscular dystrophy.
PharmGKBPA27766.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46326.
HOGENOMHOG000081509.
HOVERGENHBG001099.
InParanoidP50402.
KOK12569.
OMASIAHYRP.
PhylomeDBP50402.
TreeFamTF337236.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressP50402.
BgeeP50402.
CleanExHS_EMD.
GenevestigatorP50402.

Family and domain databases

Gene3D1.10.720.40. 1 hit.
InterProIPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamPF03020. LEM. 1 hit.
[Graphical view]
SMARTSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMSSF63451. SSF63451. 1 hit.
PROSITEPS50954. LEM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50402.
GeneWikiEmerin.
GenomeRNAi2010.
NextBio8137.
PROP50402.
SOURCESearch...

Entry information

Entry nameEMD_HUMAN
AccessionPrimary (citable) accession number: P50402
Secondary accession number(s): Q6FI02
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM