Reviewed,
UniProtKB/Swiss-Prot P50402 (EMD_HUMAN)
Last modified
November 24, 2009.
Version 109.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Emerin | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 254 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. Ref.16 Ref.21 Ref.23 Ref.24 |
| 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 By similarity. Interacts with ACTB, SPTAN1, F-actin, CTNNB1 and beta-tubulin. |
| 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. Ref.24 Ref.9 Ref.10 Ref.22 |
| 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.10 Ref.22 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.25 Ref.26 Ref.27 |
| Involvement in disease | Defects in EMD are a cause of X-linked Emery-Dreifuss muscular dystrophy (X-EDMD) [MIM:310300]. X-EDMD is an X-linked disorder characterized by early contractures, muscle wasting and weakness and cardiomyopathy. Ref.16 Ref.15 Ref.33 Ref.34 |
| Sequence similarities | Contains 1 LEM domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Microtubule Nucleus |
| Disease | Cardiomyopathy Disease mutation |
| Domain | Transmembrane |
| Ligand | Actin-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | muscle contraction Ref.1 Traceable author statement. Source: ProtInc muscle organ development Ref.1Traceable author statement. Source: ProtInc |
| Cellular component | endoplasmic reticulum Inferred from direct assay. Source: HPA integral to membraneInferred from electronic annotation. Source: UniProtKB-KW nuclear outer membrane Ref.24Inferred from direct assay. Source: UniProtKB |
| Molecular function | actin binding Ref.16 Inferred from direct assay. Source: UniProtKB beta-tubulin binding Ref.24Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BCLAF1 | Q9NYF8 | 2 | EBI-489887,EBI-437804 | |
| SH3GL2 | Q99962 | 1 | EBI-489887,EBI-77938 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||
Molecule processing | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 254 | 254 | Emerin | PRO_0000206140 | |||||||||||||||
Regions | |||||||||||||||||||
| Transmembrane | 223 – 243 | 21 | Potential | ||||||||||||||||
| Domain | 1 – 45 | 45 | LEM | ||||||||||||||||
| Region | 46 – 222 | 177 | Interaction with F-actin Probable | ||||||||||||||||
| Region | 168 – 186 | 19 | Interaction with CTNNB1 | ||||||||||||||||
| Compositional bias | 192 – 199 | 8 | Poly-Ser | ||||||||||||||||
Amino acid modifications | |||||||||||||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.8 | ||||||||||||||||
| Modified residue | 8 | 1 | Phosphoserine Ref.26 | ||||||||||||||||
| Modified residue | 29 | 1 | Phosphoserine Ref.26 | ||||||||||||||||
| Modified residue | 49 | 1 | Phosphoserine; by PKA Ref.22 Ref.20 Ref.25 Ref.26 Ref.27 | ||||||||||||||||
| Modified residue | 52 | 1 | Phosphoserine Ref.27 | ||||||||||||||||
| Modified residue | 54 | 1 | Phosphoserine Ref.25 Ref.27 | ||||||||||||||||
| Modified residue | 59 | 1 | Phosphotyrosine Ref.17 Ref.25 | ||||||||||||||||
| Modified residue | 60 | 1 | Phosphoserine Ref.25 Ref.27 | ||||||||||||||||
| Modified residue | 66 | 1 | Phosphoserine Ref.27 | ||||||||||||||||
| Modified residue | 74 | 1 | Phosphotyrosine Ref.17 Ref.20 | ||||||||||||||||
| Modified residue | 85 | 1 | Phosphotyrosine Ref.17 Ref.18 | ||||||||||||||||
| Modified residue | 87 | 1 | Phosphoserine Ref.27 | ||||||||||||||||
| Modified residue | 95 | 1 | Phosphotyrosine Ref.18 | ||||||||||||||||
| Modified residue | 99 | 1 | Phosphotyrosine Ref.18 | ||||||||||||||||
| Modified residue | 105 | 1 | Phosphotyrosine Ref.19 | ||||||||||||||||
| Modified residue | 120 | 1 | Phosphoserine Ref.20 | ||||||||||||||||
| Modified residue | 161 | 1 | Phosphotyrosine Ref.17 | ||||||||||||||||
| Modified residue | 163 | 1 | Phosphoserine Ref.14 | ||||||||||||||||
| Modified residue | 167 | 1 | Phosphotyrosine Ref.14 Ref.17 Ref.20 | ||||||||||||||||
Natural variations | |||||||||||||||||||
| Natural variant | 54 | 1 | S → F in X-EDMD; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1. Ref.16 Ref.15 | VAR_005198 | |||||||||||||||
| Natural variant | 133 | 1 | Q → H in X-EDMD; loss of binding to F-actin. Ref.16 Ref.34 | VAR_016016 | |||||||||||||||
| Natural variant | 149 | 1 | D → H: dbSNP rs2070818. | VAR_038433 | |||||||||||||||
| Natural variant | 183 | 1 | P → H in X-EDMD; no loss of binding to F-actin and enhanced rate of actin polymerization. Ref.16 Ref.33 | VAR_005199 | |||||||||||||||
| Natural variant | 183 | 1 | P → T in X-EDMD. Ref.33 | VAR_005200 | |||||||||||||||
Experimental info | |||||||||||||||||||
| Mutagenesis | 49 | 1 | S → A: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. Ref.22 | ||||||||||||||||
| Mutagenesis | 49 | 1 | S → E: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. Ref.22 | ||||||||||||||||
| Mutagenesis | 196 | 1 | S → A: No loss of binding to F-actin; when associated with A-197. Ref.16 | ||||||||||||||||
| Mutagenesis | 197 | 1 | S → A: No loss of binding to F-actin; when associated with A-196. Ref.16 | ||||||||||||||||
Secondary structure | |||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||
| Turn | 4 – 6 | 3 | |||||||||||||||||
| Helix | 9 – 16 | 8 | |||||||||||||||||
| Beta strand | 17 – 19 | 3 | |||||||||||||||||
| Helix | 29 – 31 | 3 | |||||||||||||||||
| Helix | 32 – 37 | 6 | |||||||||||||||||
| Helix | 40 – 42 | 3 | |||||||||||||||||
Sequences
| ||||||||||||||||||
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: 7894480] [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: 8733135] [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: 8655156] [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: 8595407] [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] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta. |
| [7] | "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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-17. Tissue: Platelet. |
| [8] | 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma and Embryonic kidney. |
| [9] | "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: 9673989] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [10] | "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: 9472006] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION. |
| [11] | "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: 11792822] [Abstract] Cited for: INTERACTION WITH BANF1. |
| [12] | "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: 12755701] [Abstract] Cited for: INTERACTION WITH YTHDC1. |
| [13] | "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: 12493765] [Abstract] Cited for: INTERACTION WITH GMCL. |
| [14] | "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: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND TYR-167, MASS SPECTROMETRY. Tissue: T-cell. |
| [15] | "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: 15009215] [Abstract] Cited for: INTERACTION WITH BCLAF1, CHARACTERIZATION OF VARIANT X-EDMD PHE-54. |
| [16] | "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: 15328537] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACTB; SPTAN1 AND F-ACTIN, MUTAGENESIS OF SER-196 AND SER-197, CHARACTERIZATION OF VARIANTS X-EDMD PHE-54; HIS-133 AND HIS-183. |
| [17] | "Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)." Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A. J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-59; TYR-74; TYR-85; TYR-161 AND TYR-167, MASS SPECTROMETRY. Tissue: Epithelium. |
| [18] | "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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85; TYR-95 AND TYR-99, MASS SPECTROMETRY. |
| [19] | "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, MASS SPECTROMETRY. Tissue: T-cell. |
| [20] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; TYR-74; SER-120 AND TYR-167, MASS SPECTROMETRY. Tissue: Epithelium. |
| [21] | "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: 16858403] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTNNB1. |
| [22] | "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: 16972941] [Abstract] Cited for: PHOSPHORYLATION AT SER-49, SUBCELLULAR LOCATION, INTERACTION WITH LMNA, MASS SPECTROMETRY, MUTAGENESIS OF SER-49. |
| [23] | "The inner-nuclear-envelope protein emerin regulates HIV-1 infectivity." Jacque J.-M., Stevenson M. Nature 441:641-645(2006) [PubMed: 16680152] [Abstract] Cited for: FUNCTION. |
| [24] | "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: 17785515] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BETA-TUBULIN. |
| [25] | "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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-54; TYR-59 AND SER-60, MASS SPECTROMETRY. |
| [26] | "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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-29 AND SER-49, MASS SPECTROMETRY. |
| [27] | "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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-52; SER-54; SER-60; SER-66 AND SER-87, MASS SPECTROMETRY. |
| [28] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. |
| [30] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-60, MASS SPECTROMETRY. Tissue: T-cell. |
| [31] | "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: 11470279] [Abstract] Cited for: STRUCTURE BY NMR OF 2-54. |
| [32] | "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: 11435115] [Abstract] Cited for: STRUCTURE BY NMR OF 2-54. |
| [33] | "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: 10323252] [Abstract] Cited for: VARIANTS X-EDMD HIS-183 AND THR-183. |
| [34] | "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: 11587540] [Abstract] Cited for: VARIANT X-EDMD HIS-133. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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. BC000738 mRNA. Translation: AAH00738.1. | |||||||||||||||||||||||||
| IPI | IPI00032003. | ||||||||||||||||||||||||
| PIR | S50834. | ||||||||||||||||||||||||
| RefSeq | NP_000108.1. | ||||||||||||||||||||||||
| UniGene | Hs.522823 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P50402. 10 interactions. | ||||||||||||||||||||||||
| STRING | P50402. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | P50402. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PeptideAtlas | P50402. | ||||||||||||||||||||||||
| PRIDE | P50402. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000369842; ENSP00000358857; ENSG00000102119; Homo sapiens. [Genome view] | ||||||||||||||||||||||||
| GeneID | 2010. | ||||||||||||||||||||||||
| KEGG | hsa:2010. | ||||||||||||||||||||||||
| UCSC | uc004fkl.1. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 2010. | ||||||||||||||||||||||||
| GeneCards | GC0XP153260. | ||||||||||||||||||||||||
| H-InvDB | HIX0017151. | ||||||||||||||||||||||||
| HGNC | HGNC:3331. EMD. | ||||||||||||||||||||||||
| HPA | CAB001545. CAB002029. HPA000609. | ||||||||||||||||||||||||
| MIM | 300384. gene. 310300. phenotype. | ||||||||||||||||||||||||
| Orphanet | 261. Emery-Dreifuss muscular dystrophy. | ||||||||||||||||||||||||
| PharmGKB | PA27766. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P50402. | ||||||||||||||||||||||||
| HOVERGEN | P50402. | ||||||||||||||||||||||||
| OMA | GPVVGST | ||||||||||||||||||||||||
| OrthoDB | EOG9VT8H7 | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P50402. | ||||||||||||||||||||||||
| Bgee | P50402. | ||||||||||||||||||||||||
| CleanEx | HS_EMD. | ||||||||||||||||||||||||
| Genevestigator | P50402. | ||||||||||||||||||||||||
| GermOnline | ENSG00000102119. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR003887. LEM. IPR011015. LEM-like_fold. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:1.10.720.40. LEM. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF03020. LEM. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| SMART | SM00540. LEM. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS50954. LEM. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| NextBio | 8137. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | EMD_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P50402 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


