NAP1L1

This gene encodes a member of the nucleosome assembly protein (NAP) family. This protein participates in DNA replication and may play a role in modulating chromatin formation and contribute to the regulation of cell proliferation. Alternative splicing of this gene results in several transcript variants; however, not all have been fully described. [provided by RefSeq]

nucleosome assembly protein 1-like 1

Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:26841755).

Participates also in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616).

Stimulates also homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (PubMed:24798879).

Plays a key role in the regulation of embryonic neurogenesis (By similarity).

Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity).

Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity).

(Microbial infection) Positively regulates Epstein-Barr virus reactivation in epithelial cells through the induction of viral BZLF1 expression.

(Microbial infection) Together with human herpesvirus 8 protein LANA1, assists the proper assembly of the nucleosome on the replicated viral DNA.

DNA replication Source: ProtInc
Nucleosome assembly Source: GO_Central
Positive regulation of cell population proliferation Source: ProtInc
Positive regulation of neural precursor cell proliferation Source: UniProtKB
Positive regulation of neurogenesis Source: UniProtKB

Cytoplasm
Nucleus
Other locations
Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Monoglycylated on glutamate residues. Cannot be polyglycylated due to the absence of functional TTLL10 in human (By similarity).
Polyglutamylated by TTLL4 on glutamate residues, resulting in polyglutamate chains on the gamma-carboxyl group. Both polyglutamylation and monoglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally.