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P50402

- EMD_HUMAN

UniProt

P50402 - EMD_HUMAN

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Protein

Emerin

Gene

EMD

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. actin binding Source: UniProtKB
  2. beta-tubulin binding Source: UniProtKB

GO - Biological processi

  1. cellular response to growth factor stimulus Source: BHF-UCL
  2. mitotic cell cycle Source: Reactome
  3. mitotic nuclear envelope disassembly Source: Reactome
  4. mitotic nuclear envelope reassembly Source: Reactome
  5. muscle contraction Source: ProtInc
  6. muscle organ development Source: ProtInc
  7. negative regulation of catenin import into nucleus Source: BHF-UCL
  8. negative regulation of fibroblast proliferation Source: BHF-UCL
  9. positive regulation of protein export from nucleus Source: BHF-UCL
  10. regulation of canonical Wnt signaling pathway Source: BHF-UCL
  11. skeletal muscle cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Emerin
Gene namesi
Name:EMD
Synonyms:EDMD, STA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:3331. EMD.

Subcellular locationi

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.

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. microtubule Source: UniProtKB-KW
  5. nuclear envelope Source: BHF-UCL
  6. nuclear inner membrane Source: BHF-UCL
  7. nuclear membrane Source: HPA
  8. nuclear outer membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1.
VAR_005198
Natural varianti133 – 1331Q → H in EDMD1; loss of binding to F-actin. 1 Publication
VAR_016016
Natural varianti183 – 1831P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. 1 Publication
VAR_005199
Natural varianti183 – 1831P → T in EDMD1. 1 Publication
VAR_005200

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491S → A: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. 1 Publication
Mutagenesisi49 – 491S → E: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA. 1 Publication
Mutagenesisi196 – 1961S → A: No loss of binding to F-actin; when associated with A-197. 1 Publication
Mutagenesisi197 – 1971S → A: No loss of binding to F-actin; when associated with A-196. 1 Publication

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Emery-Dreifuss muscular dystrophy

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254EmerinPRO_0000206140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine7 Publications
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei49 – 491Phosphoserine; by PKA5 Publications
Modified residuei54 – 541Phosphoserine1 Publication
Modified residuei60 – 601Phosphoserine2 Publications
Modified residuei87 – 871Phosphoserine1 Publication
Modified residuei161 – 1611PhosphotyrosineBy similarity
Modified residuei171 – 1711Phosphoserine1 Publication

Post-translational modificationi

Found in four different phosphorylated forms, three of which appear to be associated with the cell cycle.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP50402.
PaxDbiP50402.
PeptideAtlasiP50402.
PRIDEiP50402.

PTM databases

PhosphoSiteiP50402.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP50402.
CleanExiHS_EMD.
ExpressionAtlasiP50402. baseline and differential.
GenevestigatoriP50402.

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.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCLAF1Q9NYF83EBI-489887,EBI-437804
CTNNB1P352223EBI-489887,EBI-491549
SH3GL2Q999622EBI-489887,EBI-77938
Sun1Q9D6664EBI-489887,EBI-6752574From a different organism.
SUN2Q9UH993EBI-489887,EBI-1044964

Protein-protein interaction databases

BioGridi108325. 123 interactions.
DIPiDIP-34638N.
IntActiP50402. 26 interactions.
MINTiMINT-266014.
STRINGi9606.ENSP00000358857.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Helixi9 – 168Combined sources
Beta strandi17 – 193Combined sources
Helixi29 – 313Combined sources
Helixi32 – 376Combined sources
Helixi40 – 423Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP50402.

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei223 – 24321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4545LEMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 222177Interaction with F-actinCuratedAdd
BLAST
Regioni168 – 18619Interaction with CTNNB1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi192 – 1998Poly-Ser

Sequence similaritiesi

Contains 1 LEM domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46326.
GeneTreeiENSGT00390000002034.
HOGENOMiHOG000081509.
HOVERGENiHBG001099.
InParanoidiP50402.
KOiK12569.
OMAiSIAHYRP.
PhylomeDBiP50402.
TreeFamiTF337236.

Family and domain databases

Gene3Di1.10.720.40. 1 hit.
InterProiIPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view]
PfamiPF03020. LEM. 1 hit.
[Graphical view]
SMARTiSM00540. LEM. 1 hit.
[Graphical view]
SUPFAMiSSF63451. SSF63451. 1 hit.
PROSITEiPS50954. LEM. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541S → F in EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1.
VAR_005198
Natural varianti133 – 1331Q → H in EDMD1; loss of binding to F-actin. 1 Publication
VAR_016016
Natural varianti149 – 1491D → H.
Corresponds to variant rs2070818 [ dbSNP | Ensembl ].
VAR_038433
Natural varianti183 – 1831P → H in EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization. 1 Publication
VAR_005199
Natural varianti183 – 1831P → T in EDMD1. 1 Publication
VAR_005200

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi1706639.

Cross-referencesi

Web resourcesi

EMD db

"EMD mutation database"

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14745.1.
PIRi S50834.
RefSeqi NP_000108.1. NM_000117.2.
UniGenei Hs.522823.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JEI NMR - A 2-54 [» ]
2ODC NMR - I 2-47 [» ]
2ODG NMR - C 2-47 [» ]
ProteinModelPortali P50402.
SMRi P50402. Positions 2-54.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108325. 123 interactions.
DIPi DIP-34638N.
IntActi P50402. 26 interactions.
MINTi MINT-266014.
STRINGi 9606.ENSP00000358857.

PTM databases

PhosphoSitei P50402.

Polymorphism databases

DMDMi 1706639.

Proteomic databases

MaxQBi P50402.
PaxDbi P50402.
PeptideAtlasi P50402.
PRIDEi P50402.

Protocols and materials databases

DNASUi 2010.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369842 ; ENSP00000358857 ; ENSG00000102119 .
GeneIDi 2010.
KEGGi hsa:2010.
UCSCi uc004fkl.3. human.

Organism-specific databases

CTDi 2010.
GeneCardsi GC0XP153607.
GeneReviewsi EMD.
HGNCi HGNC:3331. EMD.
HPAi CAB001545.
CAB002029.
CAB062552.
HPA000609.
MIMi 300384. gene.
310300. phenotype.
neXtProti NX_P50402.
Orphaneti 98863. X-linked Emery-Dreifuss muscular dystrophy.
PharmGKBi PA27766.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46326.
GeneTreei ENSGT00390000002034.
HOGENOMi HOG000081509.
HOVERGENi HBG001099.
InParanoidi P50402.
KOi K12569.
OMAi SIAHYRP.
PhylomeDBi P50402.
TreeFami TF337236.

Enzyme and pathway databases

Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

EvolutionaryTracei P50402.
GeneWikii Emerin.
GenomeRNAii 2010.
NextBioi 8137.
PROi P50402.
SOURCEi Search...

Gene expression databases

Bgeei P50402.
CleanExi HS_EMD.
ExpressionAtlasi P50402. baseline and differential.
Genevestigatori P50402.

Family and domain databases

Gene3Di 1.10.720.40. 1 hit.
InterProi IPR011015. LEM/LEM-like_dom.
IPR003887. LEM_dom.
[Graphical view ]
Pfami PF03020. LEM. 1 hit.
[Graphical view ]
SMARTi SM00540. LEM. 1 hit.
[Graphical view ]
SUPFAMi SSF63451. SSF63451. 1 hit.
PROSITEi PS50954. LEM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. 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. 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. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
  31. 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. 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. 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.

Entry informationi

Entry nameiEMD_HUMAN
AccessioniPrimary (citable) accession number: P50402
Secondary accession number(s): Q6FI02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 161 of the entry and version 1 of the sequence. [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
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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