Reviewed, UniProtKB/Swiss-Prot P50402 (EMD_HUMAN)

Names and origin

Protein names

Recommended name:
    Emerin

Gene names

Name:	EMD
Synonyms:	EDMD, STA

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.1 Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: HPA integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear outer membrane Ref.24 Inferred from direct assay. Source: UniProtKB
Molecular function	actin binding Ref.16 Inferred from direct assay. Source: UniProtKB beta-tubulin binding Ref.24 Inferred 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

1

.

.

.

.

.

.

.

.

.

.

.

254

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	P50402-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EB62EDD59B7A044F	FASTA	254	28,994
	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

References

	« Hide 'large scale' referencesShow '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.

Web resources

EMD db

"EMD mutation database"

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JEI	NMR	-	A	2-54	[»]
2ODC	NMR	-	I	2-47	[»]
2ODG	NMR	-	C	2-47	[»]

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

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 109 of the entry and version 1 of the sequence. [Complete 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.