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Nepro
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0.016s
Type
Details
Score
Publication
First Author:
Mouse Genome Informatics
Year:
2010
Journal:
Database Release
Title:
Protein Ontology Association Load.
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Publication
First Author:
Mouse Genome Informatics Scientific Curators
Year:
2009
Journal:
Database Download
Title:
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
First Author:
Allen Institute for Brain Science
Year:
2004
Journal:
Allen Institute
Title:
Allen Brain Atlas: mouse riboprobes
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Publication
First Author:
Bairoch A
Year:
1999
Journal:
Database Release
Title:
SWISS-PROT Annotated protein sequence database
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Publication
First Author:
Mouse Genome Informatics Scientific Curators
Year:
2005
Title:
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
First Author:
Mouse Genome Informatics Scientific Curators
Year:
2009
Journal:
Database Download
Title:
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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DO Term
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Protein
Organism:
Mus musculus/domesticus
Length:
564
Fragment?:
false
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Protein
Organism:
Mus musculus/domesticus
Length:
118
Fragment?:
true
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Protein
Organism:
Mus musculus/domesticus
Length:
532
Fragment?:
true
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Protein
Organism:
Mus musculus/domesticus
Length:
233
Fragment?:
false
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Publication
First Author:
Narayanan DL
Year:
2019
Journal:
Am J Med Genet A
Title:
An emerging ribosomopathy affecting the skeleton due to biallelic variations in NEPRO.
Volume:
179
Issue:
9
Pages:
1709-1717
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Protein Domain
Type:
Domain
Description:
This entry represents a domain found in Nucleolus and neural progenitor protein from mouse (Nepro) and similar eukaryotic sequences. Nepro may play a role in cortex development as part of the Notch signaling pathway. Downstream of Notch may repress the expression of proneural genes and inhibit neuronal differentiation thereby maintaining neural progenitors []. It may also be involved in preimplentation embryo development []. NEPRO interacts with multiple protein subunits of RMRP and is implicated in Anauxetic dysplasia 3 []. The specific function of this domain, which is predicted to have a four-helix bundle structure, is still unknown.
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