EMD
entrez
2010
canonical
uniprot
P50402
canonical
ensembl
ENSG00000102119
resolver
ensp
ENSP00000358857
resolver
ensp
ENSP00000507533
resolver
enst
ENST00000369842
resolver
enst
ENST00000683627
resolver
genesymbol
EMD
resolver
genesymbol_syn
EDMD
resolver
genesymbol_syn
STA
resolver
hgnc
HGNC:3331
resolver
uniprot
Q6FI02
resolver
uniprot_entry
EMD_HUMAN
resolver
uniprot_sec
Q6FI02
resolver
amino_acid_sequence
MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKEDALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSAYQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLFFIYHFMQAEEGNPF
uniprot
proteins
disease_involvement
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. {ECO:0000269|PubMed:10323252, ECO:0000269|PubMed:10382909, ECO:0000269|PubMed:10393813, ECO:0000269|PubMed:11587540, ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:32549231}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, dilated, 3C (CMD3C) [MIM:301163]: An X-linked, severe form of dilated cardiomyopathy, a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:18266676, ECO:0000269|PubMed:24997722, ECO:0000269|PubMed:32755394, ECO:0000269|PubMed:40065010}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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 (PubMed:15328537). 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 (PubMed:16858403). Links centrosomes to the nuclear envelope via a microtubule association (PubMed:17785515). Required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). 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. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:32923640}.
uniprot
proteins
mass_dalton
28994
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="S->A: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA."; /evidence="ECO:0000269|PubMed:16972941"; MUTAGEN 49; /note="S->E: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA."; /evidence="ECO:0000269|PubMed:16972941"; MUTAGEN 196; /note="S->A: No loss of binding to F-actin; when associated with A-197."; /evidence="ECO:0000269|PubMed:15328537"; MUTAGEN 197; /note="S->A: No loss of binding to F-actin; when associated with A-196."; /evidence="ECO:0000269|PubMed:15328537
uniprot
proteins
post_translational_modification
PTM: Found in four different phosphorylated forms, three of which appear to be associated with the cell cycle. {ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:9472006}.
uniprot
proteins
pubmed
10323252
uniprot
proteins
pubmed
10382909
uniprot
proteins
pubmed
10393813
uniprot
proteins
pubmed
11435115
uniprot
proteins
pubmed
11470279
uniprot
proteins
pubmed
11587540
uniprot
proteins
pubmed
11792822
uniprot
proteins
pubmed
12493765
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12755701
uniprot
proteins
pubmed
15009215
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15328537
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16680152
uniprot
proteins
pubmed
16858403
uniprot
proteins
pubmed
16972941
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17785515
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18266676
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19167377
uniprot
proteins
pubmed
19323649
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21610090
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24997722
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32549231
uniprot
proteins
pubmed
32755394
uniprot
proteins
pubmed
32923640
uniprot
proteins
pubmed
40065010
uniprot
proteins
pubmed
7894480
uniprot
proteins
pubmed
8595407
uniprot
proteins
pubmed
8655156
uniprot
proteins
pubmed
8733135
uniprot
proteins
pubmed
9472006
uniprot
proteins
pubmed
9673989
uniprot
proteins
sequence_length
254
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:19167377}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:19167377}. 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.
uniprot
proteins
transmembrane_region
TRANSMEM 223..243; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins