critical for the survival of prostate cancer cells, suggesting that targeting tNASP expression can lead to a new approach for prostate cancer treatment
its role is to provide the functional link between linker histones and cell cycle progression during meiosis
14
splicing
initiation site
2294
-
449
all mitotic cells (adult embryonic) during five phases
2012
2196553
isoform 3 sNASP, somatic NASP
characterization of the histone H1-binding protein as a cell-cycle regulated somatic protein
possesses a unique binding specificity in that it forms specific complexes with both histone H1 and histones H3/H4
efficiently promoted the assembly of nucleosomes containing the conventional H3.1, H3.2, H3.3, or centromere-specific CENPA
tNASP : Golgi and acrosome nucleus, 5NASP:nuclear localization
basic FUNCTION
transporting histones into the nucleus of dividing cells (isoform 3)
directly promotes nucleosome assembly, providing compelling evidence that sNASP is a bona fide histone chaperone for H3.H4
specific function for the histone chaperone NASP to fine-tune a reservoir of soluble H3-H4 in the histone supply chain
unique genuine chaperone for histone H1
CELLULAR PROCESS
cell cycle, division
PHYSIOLOGICAL PROCESS
reproduction/sex
PATHWAY
metabolism
signaling
a component
INTERACTION
DNA
RNA
small molecule
nucleotide,
ATP
GTP
protein
binding to H1 histones
beyond their important role in the remodeling of paternal chromatin in the early stages of embryogenesis, NPM2 and NPM3 and NASP members can interact with a plethora of proteins in addition to histones in somatic cells