Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Emerin

Gene

EMD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL

GO - Biological processi

  • cellular response to growth factor stimulus Source: BHF-UCL
  • mitotic nuclear envelope disassembly Source: Reactome
  • mitotic nuclear envelope reassembly Source: Reactome
  • muscle contraction Source: ProtInc
  • muscle organ development Source: ProtInc
  • negative regulation of catenin import into nucleus Source: BHF-UCL
  • negative regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of protein export from nucleus Source: BHF-UCL
  • regulation of canonical Wnt signaling pathway Source: BHF-UCL
  • skeletal muscle cell differentiation Source: Ensembl

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

ReactomeiR-HSA-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
SIGNORiP50402.

Names & Taxonomyi

Protein namesi
Recommended name:
Emerin
Gene namesi
Name:EMD
Synonyms:EDMD, STA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3331. EMD.

Subcellular locationi

  • Nucleus inner membrane 1 Publication; Single-pass membrane protein; Nucleoplasmic side 1 Publication
  • 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.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei223 – 243HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • cytoplasm Source: CAFA
  • endoplasmic reticulum Source: HPA
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • nuclear envelope Source: LIFEdb
  • nuclear inner membrane Source: UniProtKB
  • nuclear membrane Source: HPA
  • nuclear outer membrane Source: UniProtKB
  • nucleoplasm Source: CAFA

Keywords - Cellular componenti

Membrane, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Emery-Dreifuss muscular dystrophy 1, X-linked (EDMD1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:310300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00519854S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1. 2 Publications1
Natural variantiVAR_016016133Q → H in EDMD1; loss of binding to F-actin. 2 Publications1
Natural variantiVAR_005199183P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. 2 PublicationsCorresponds to variant dbSNP:rs104894805Ensembl.1
Natural variantiVAR_005200183P → T in EDMD1. 1 PublicationCorresponds to variant dbSNP:rs104894806Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49S → A: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. 1 Publication1
Mutagenesisi49S → E: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. 1 Publication1
Mutagenesisi196S → A: No loss of binding to F-actin; when associated with A-197. 1 Publication1
Mutagenesisi197S → A: No loss of binding to F-actin; when associated with A-196. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Emery-Dreifuss muscular dystrophy

Organism-specific databases

DisGeNETi2010.
MalaCardsiEMD.
MIMi310300. phenotype.
OpenTargetsiENSG00000102119.
Orphaneti98863. X-linked Emery-Dreifuss muscular dystrophy.
PharmGKBiPA27766.

Polymorphism and mutation databases

BioMutaiEMD.
DMDMi1706639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002061401 – 254EmerinAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei8PhosphoserineCombined sources1
Modified residuei29PhosphoserineCombined sources1
Modified residuei49Phosphoserine; by PKACombined sources1 Publication1
Modified residuei54PhosphoserineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei87PhosphoserineCombined sources1
Modified residuei98PhosphoserineCombined sources1
Modified residuei141PhosphoserineBy similarity1
Modified residuei142PhosphoserineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei161PhosphotyrosineBy similarity1
Modified residuei171PhosphoserineCombined sources1
Modified residuei173PhosphoserineCombined sources1
Modified residuei175PhosphoserineBy similarity1

Post-translational modificationi

Found in four different phosphorylated forms, three of which appear to be associated with the cell cycle.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP50402.
PaxDbiP50402.
PeptideAtlasiP50402.
PRIDEiP50402.
TopDownProteomicsiP50402.

PTM databases

iPTMnetiP50402.
PhosphoSitePlusiP50402.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000102119.
CleanExiHS_EMD.
ExpressionAtlasiP50402. baseline and differential.
GenevisibleiP50402. HS.

Organism-specific databases

HPAiCAB001545.
CAB002029.
CAB062552.
HPA000609.

Interactioni

Subunit structurei

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. Interacts with TMEM201.By similarity10 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108325. 170 interactors.
DIPiDIP-34638N.
IntActiP50402. 109 interactors.
MINTiMINT-266014.
STRINGi9606.ENSP00000358857.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Helixi9 – 16Combined sources8
Beta strandi17 – 19Combined sources3
Helixi29 – 31Combined sources3
Helixi32 – 37Combined sources6
Helixi40 – 42Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JEINMR-A2-54[»]
2ODCNMR-I2-47[»]
2ODGNMR-C2-47[»]
ProteinModelPortaliP50402.
SMRiP50402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50402.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 45LEMPROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 222Interaction with F-actinCuratedAdd BLAST177
Regioni168 – 186Interaction with CTNNB11 PublicationAdd BLAST19

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi192 – 199Poly-Ser8

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJ10. Eukaryota.
ENOG410ZEWX. LUCA.
GeneTreeiENSGT00390000002034.
HOGENOMiHOG000081509.
HOVERGENiHBG001099.
InParanoidiP50402.
KOiK12569.
OMAiSVDSDMY.
OrthoDBiEOG091G0M7U.
PhylomeDBiP50402.
TreeFamiTF337236.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
InterProiView protein in InterPro
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
PfamiView protein in Pfam
PF03020. LEM. 1 hit.
SMARTiView protein in SMART
SM00540. LEM. 1 hit.
SUPFAMiSSF63451. SSF63451. 1 hit.
PROSITEiView protein in PROSITE
PS50954. LEM. 1 hit.

Sequencei

Sequence statusi: Complete.

P50402-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNYADLSDT ELTTLLRRYN IPHGPVVGST RRLYEKKIFE YETQRRRLSP
60 70 80 90 100
PSSSAASSYS FSDLNSTRGD ADMYDLPKKE DALLYQSKGY NDDYYEESYF
110 120 130 140 150
TTRTYGEPES AGPSRAVRQS VTSFPDADAF HHQVHDDDLL SSSEEECKDR
160 170 180 190 200
ERPMYGRDSA YQSITHYRPV SASRSSLDLS YYPTSSSTSF MSSSSSSSSW
210 220 230 240 250
LTRRAIRPEN RAPGAGLGQD RQVPLWGQLL LFLVFVIVLF FIYHFMQAEE

GNPF
Length:254
Mass (Da):28,994
Last modified:October 1, 1996 - v1
Checksum:iEB62EDD59B7A044F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00519854S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1. 2 Publications1
Natural variantiVAR_016016133Q → H in EDMD1; loss of binding to F-actin. 2 Publications1
Natural variantiVAR_038433149D → H. Corresponds to variant dbSNP:rs2070818Ensembl.1
Natural variantiVAR_005199183P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. 2 PublicationsCorresponds to variant dbSNP:rs104894805Ensembl.1
Natural variantiVAR_005200183P → T in EDMD1. 1 PublicationCorresponds to variant dbSNP:rs104894806Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14745.1.
PIRiS50834.
RefSeqiNP_000108.1. NM_000117.2.
UniGeneiHs.522823.

Genome annotation databases

EnsembliENST00000369842; ENSP00000358857; ENSG00000102119.
GeneIDi2010.
KEGGihsa:2010.
UCSCiuc004fkl.4. human.

Cross-referencesi

Web resourcesi

EMD db

"EMD mutation database"

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14745.1.
PIRiS50834.
RefSeqiNP_000108.1. NM_000117.2.
UniGeneiHs.522823.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JEINMR-A2-54[»]
2ODCNMR-I2-47[»]
2ODGNMR-C2-47[»]
ProteinModelPortaliP50402.
SMRiP50402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108325. 170 interactors.
DIPiDIP-34638N.
IntActiP50402. 109 interactors.
MINTiMINT-266014.
STRINGi9606.ENSP00000358857.

PTM databases

iPTMnetiP50402.
PhosphoSitePlusiP50402.

Polymorphism and mutation databases

BioMutaiEMD.
DMDMi1706639.

Proteomic databases

EPDiP50402.
PaxDbiP50402.
PeptideAtlasiP50402.
PRIDEiP50402.
TopDownProteomicsiP50402.

Protocols and materials databases

DNASUi2010.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369842; ENSP00000358857; ENSG00000102119.
GeneIDi2010.
KEGGihsa:2010.
UCSCiuc004fkl.4. human.

Organism-specific databases

CTDi2010.
DisGeNETi2010.
GeneCardsiEMD.
GeneReviewsiEMD.
HGNCiHGNC:3331. EMD.
HPAiCAB001545.
CAB002029.
CAB062552.
HPA000609.
MalaCardsiEMD.
MIMi300384. gene.
310300. phenotype.
neXtProtiNX_P50402.
OpenTargetsiENSG00000102119.
Orphaneti98863. X-linked Emery-Dreifuss muscular dystrophy.
PharmGKBiPA27766.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ10. Eukaryota.
ENOG410ZEWX. LUCA.
GeneTreeiENSGT00390000002034.
HOGENOMiHOG000081509.
HOVERGENiHBG001099.
InParanoidiP50402.
KOiK12569.
OMAiSVDSDMY.
OrthoDBiEOG091G0M7U.
PhylomeDBiP50402.
TreeFamiTF337236.

Enzyme and pathway databases

ReactomeiR-HSA-2993913. Clearance of Nuclear Envelope Membranes from Chromatin.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
SIGNORiP50402.

Miscellaneous databases

EvolutionaryTraceiP50402.
GeneWikiiEmerin.
GenomeRNAii2010.
PROiPR:P50402.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102119.
CleanExiHS_EMD.
ExpressionAtlasiP50402. baseline and differential.
GenevisibleiP50402. HS.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
InterProiView protein in InterPro
IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
PfamiView protein in Pfam
PF03020. LEM. 1 hit.
SMARTiView protein in SMART
SM00540. LEM. 1 hit.
SUPFAMiSSF63451. SSF63451. 1 hit.
PROSITEiView protein in PROSITE
PS50954. LEM. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEMD_HUMAN
AccessioniPrimary (citable) accession number: P50402
Secondary accession number(s): Q6FI02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 10, 2017
This is version 187 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.