InterPro : IPR002164

Name  Nucleosome assembly protein (NAP) Short Name  NAP_family
Type  Family Description  It is thought that NAPs act as histone chaperones, shuttling both core and linker histones from their site of synthesis in the cytoplasm to the nucleus. The proteins may be involved in regulating gene expression and therefore cellular differentiation [, ].The centrosomal protein c-Nap1, also known as Cep250, has been implicated in thecell-cycle-regulated cohesion of microtubule-organizing centres. This 281 kDaprotein consists mainly of domains predicted to form coiled coil structures. The C-terminalregion defines a novel histone-binding domain that is responsible for targeting CNAP1, and possibly condensin, to mitoticchromosomes []. During interphase, C-Nap1 localizes to the proximalends of both parental centrioles, but it dissociates from these structures at the onset of mitosis. Re-association with centriolesthen occurs in late telophase or at the very beginning of G1 phase, when daughter cells are still connected by post-mitoticbridges. Electron microscopic studies performed on isolated centrosomes suggest that a proteinaceous linker connects parental centrioles and C-Nap1 may be part of a linker structure that assures the cohesion of duplicated centrosomes during interphase, but that is dismantled upon centrosome separation at the onset of mitosis [].
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InterPro protein domain ID --> Contigs

 

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4 Publications

First Author Title Year Journal Volume Pages
Rodriguez P Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone. 1997 Genomics 44 253-65
Schnieders F Testis-specific protein, Y-encoded (TSPY) expression in testicular tissues. 1996 Hum Mol Genet 5 1801-7
Ball AR Jr Identification of a chromosome-targeting domain in the human condensin subunit CNAP1/hCAP-D2/Eg7. 2002 Mol Cell Biol 22 5769-81
Mayor T The mechanism regulating the dissociation of the centrosomal protein C-Nap1 from mitotic spindle poles. 2002 J Cell Sci 115 3275-84



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)