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GeneQ18047036· pop 6· linked from 10 articles

Also known as EOPA, MITAP1, NDE1L1, NDE2, NUDEL, nudE neurodevelopment protein 1 like 1

Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.

Gene data

NDEL1
Name
nudE neurodevelopment protein 1 like 1
Type
protein-coding
Position
8,408,528–8,490,411 (+)
Aliases
EOPA, MITAP1, NDE1L1, NDE2, NUDEL
RefSeq RNA
NM_001025579.3, NM_001330129.2, NM_030808.5, XM_017025183.2, XM_017025184.2
RefSeq protein
NP_001020750.1, NP_001317058.1, NP_110435.1, XP_016880672.1, XP_016880673.1

This gene encodes a coiled-coil protein that plays a role in multiple processes including cytoskeletal organization, cell signaling and neuron migration, outgrowth and maintenance. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome X. [provided by RefSeq, Mar 2012]

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Gene · Ensembl

nudE neurodevelopment protein 1 like 1

Symbol
NDEL1
Biotype
Protein coding
Organism
Homo sapiens
Location
17:8,408,528-8,501,107
Strand
Forward (+)
Assembly
GRCh38
View on Ensembl →

via Ensembl · EMBL-EBI

Wikidata facts

Show 5 more facts
HomoloGene ID
32567
genomic end
8393729
genomic start
8316449
cytogenetic location
17p13.1
Sources (3)

via Wikidata · CC0

~2 min read

Article

3 sections
Contents
  • Other Interactions
  • References
  • Further reading

Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.

It plays a significant role in intracellular transport and the process of cellular division via regulation of the dynein motor protein and its cofactor protein, Lis1. Ndel1 is a highly conserved protein and its human gene, NDEL1 is expressed in a wide variety of brain tissues which contributes to neuronal function and development. Nde1 and Ndel1 were in the past referred to as NudE and NudEL respectively. The Nde1 protein is involved in nuclear migration throughout the process of neurogenesis. Studies have revealed that Ndel1 is structurally similar to Nde1 which both play a role in microtubule-based transport. Ndel1 and Nde1 are also thought to be associated with neurodevelopmental and psychiatric disorders. Secondary structure of Ndel1 is composed of various distinct domains: a C-terminal region, and a 200 amino acid N-terminal coiled-coil domain. The coiled-coil domain of Ndel1 serves as a self-associating stable parallel homodimer. Such structural components help with interactions between an array of binding partners, including the motor protein dynein and its cofactor protein, Lis1. Ndel1 forms a heterotetramer complex with Lis1 via the N-terminal coiled-coil domain. The Ndel1 N-terminal coiled-coil domain mediates binding to dynein, whereas the C-terminal domain interacts with Lis1, regulating the activity of the dynein complex.

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