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Details on Person UniProt:P50402 EMD
| Class:Id | ReferenceGeneProduct:54286 |
|---|---|
| _chainChangeLog | chain:1-254 added on Fri February 6 2015 |
| _displayName | UniProt:P50402 EMD |
| _timestamp | 2024-11-03 20:05:13 |
| chain | chain:1-254 |
| checksum | EB62EDD59B7A044F |
| comment | 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. Required for proper localization of non-farnesylated prelamin-A/C. 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.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. Interacts with NEMP1 (PubMed:32923640).INTERACTION 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.DISEASE The disease is caused by variants affecting the gene represented in this entry.ONLINE INFORMATION EMD mutation database |
| description | recommendedName: Emerin |
| geneName | EMD EDMD STA |
| identifier | P50402 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Actin-binding Cardiomyopathy Direct protein sequencing Disease variant Emery-Dreifuss muscular dystrophy Membrane Microtubule Nucleus Phosphoprotein Proteomics identification Reference proteome Transmembrane Transmembrane helix |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | EMD |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8998284] ENSEMBL:ENSG00000102119 EMD [Homo sapiens] |
| secondaryIdentifier | EMD_HUMAN Q6FI02 |
| sequenceLength | 254 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:201573] EMD [nuclear envelope] [Homo sapiens] [EntityWithAccessionedSequence:9613988] EMD [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9613998] EMD [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:9715092] EMD [endosome membrane] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:P50402 EMD (54286)
