Nap1l1
entrez
53605
canonical
uniprot
P28656
canonical
ensembl
ENSMUSG00000058799
resolver
ensp
ENSMUSP00000070068
resolver
ensp
ENSMUSP00000151750
resolver
ensp
ENSMUSP00000151972
resolver
ensp
ENSMUSP00000338569
resolver
ensp
ENSMUSP00000353847
resolver
enst
ENSMUST00000065917
resolver
enst
ENSMUST00000217908
resolver
enst
ENSMUST00000218828
resolver
genesymbol
Nap1l1
resolver
genesymbol_syn
Nrp
resolver
uniprot
Q3UL14
resolver
uniprot_entry
NP1L1_MOUSE
resolver
uniprot_sec
Q3UL14
resolver
amino_acid_sequence
MADIDNKEQSELDQDLEDVEEVEEEETGEETKIKARQLTVQMMQNPQILAALQERLDGLVDTPTGYIESLPKVVKRRVNALKNLQVKCAQIEAKFYEEVHDLERKYAVLYQPLFDKRFEIINAIYEPTEEECEWKPDEEDEVSEELKEKAKIEDEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMVQEHDEPILKHLKDIKVKFSDAGQPMSFVLEFHFEPNDYFTNEVLTKTYRMRSEPDDSDPFSFDGPEIMGCTGCQIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVSNDSFFNFFAPPEVPENGDLDDDAEAILAADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADEEGEEEGDEENDPDYDPKKDQNPAECKQQ
uniprot
proteins
function
FUNCTION: Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly. Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair. Also stimulates homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (By similarity). Plays a key role in the regulation of embryonic neurogenesis (PubMed:29490266). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (PubMed:29490266). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (PubMed:29490266). {ECO:0000250|UniProtKB:P55209, ECO:0000269|PubMed:29490266}.
uniprot
proteins
mass_dalton
45345
uniprot
proteins
mutagenesis
MUTAGEN 359; /note="E->D: Reduced polyglycylation."; /evidence="ECO:0000269|PubMed:18331838"; MUTAGEN 360; /note="E->D: Reduced polyglycylation."; /evidence="ECO:0000269|PubMed:18331838
uniprot
proteins
post_translational_modification
PTM: Polyglycylated by TTLL10 on glutamate residues, resulting in polyglycine chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. {ECO:0000269|PubMed:18331838}.; PTM: Polyglutamylated by TTLL4 on glutamate residues, resulting in polyglutamate chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. {ECO:0000269|PubMed:17499049}.
uniprot
proteins
protein_family
Nucleosome assembly protein (NAP) family
uniprot
proteins
pubmed
12106288
uniprot
proteins
pubmed
15345747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17499049
uniprot
proteins
pubmed
18331838
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21333655
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
29490266
uniprot
proteins
sequence_length
391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21333655, ECO:0000269|PubMed:29490266}. Chromosome {ECO:0000269|PubMed:21333655}. Cytoplasm {ECO:0000269|PubMed:21333655, ECO:0000269|PubMed:29490266}. Melanosome {ECO:0000250|UniProtKB:P55209}.
uniprot
proteins