UniProt functional annotation for P50402



	UniProt functional annotation for P50402

UniProt code: P50402.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

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. Required for proper localization of non-farnesylated prelamin-A/C. {ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649}.

Subunit: 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. {ECO:0000250, ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12493765, ECO:0000269|PubMed:12755701, ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:15328537, ECO:0000269|PubMed:16858403, ECO:0000269|PubMed:16972941, ECO:0000269|PubMed:17785515, ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:21610090}.

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.

Tissue specificity: Skeletal muscle, heart, colon, testis, ovary and pancreas.

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}.

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:11587540, ECO:0000269|PubMed:15009215, ECO:0000269|PubMed:15328537}. Note=The disease is caused by variants affecting the gene represented in this entry.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



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. Required for proper localization of non-farnesylated prelamin-A/C. {ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16680152, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649}.


Subunit:		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. {ECO:0000250, ECO:0000269\|PubMed:11792822, ECO:0000269\|PubMed:12493765, ECO:0000269\|PubMed:12755701, ECO:0000269\|PubMed:15009215, ECO:0000269\|PubMed:15328537, ECO:0000269\|PubMed:16858403, ECO:0000269\|PubMed:16972941, ECO:0000269\|PubMed:17785515, ECO:0000269\|PubMed:19323649, ECO:0000269\|PubMed:21610090}.
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.
Tissue specificity:		Skeletal muscle, heart, colon, testis, ovary and pancreas.
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}.
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:11587540, ECO:0000269\|PubMed:15009215, ECO:0000269\|PubMed:15328537}. Note=The disease is caused by variants affecting the gene represented in this entry.