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Gene Review:

NES - nestin

Gallus gallus

Hemken, P.M. et al., Fischer, A.J. et al., Yuan, Y. et al.

Fischer, Omar,

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High impact information on NES

The derived amino acid sequence of paranemin (1,606 residues; 178,161 kDa) contains the conserved IF rod domain (308 amino acids), which has highest homology to the rod domains of nestin and tanabin [1].
We show that transitin is an intermediate filament protein with a core domain most closely resembling nestin and tanabin [2].

Anatomical context of NES

Transitin, a nestin-related intermediate filament, is expressed by neural progenitors and can be induced in Müller glia in the chicken retina [3].

References

Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin. Hemken, P.M., Bellin, R.M., Sernett, S.W., Becker, B., Huiatt, T.W., Robson, R.M. J. Biol. Chem. (1997) [Pubmed]
Molecular cloning of a new intermediate filament protein expressed by radial glia and demonstration of alternative splicing in a novel heptad repeat region located in the carboxy-terminal tail domain. Yuan, Y., Lee, J.A., Napier, A., Cole, G.J. Mol. Cell. Neurosci. (1997) [Pubmed]
Transitin, a nestin-related intermediate filament, is expressed by neural progenitors and can be induced in Müller glia in the chicken retina. Fischer, A.J., Omar, G. J. Comp. Neurol. (2005) [Pubmed]

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