Nap1l4
entrez
17955
canonical
uniprot
Q78ZA7
canonical
ensembl
ENSMUSG00000059119
resolver
ensp
ENSMUSP00000072510
resolver
ensp
ENSMUSP00000146474
resolver
ensp
ENSMUSP00000147130
resolver
ensp
ENSMUSP00000241161
resolver
ensp
ENSMUSP00000241169
resolver
ensp
ENSMUSP00000241172
resolver
ensp
ENSMUSP00000241177
resolver
ensp
ENSMUSP00000241180
resolver
ensp
ENSMUSP00000241184
resolver
ensp
ENSMUSP00000241193
resolver
ensp
ENSMUSP00000241206
resolver
ensp
ENSMUSP00000241209
resolver
ensp
ENSMUSP00000241213
resolver
ensp
ENSMUSP00000241220
resolver
ensp
ENSMUSP00000241222
resolver
enst
ENSMUST00000072727
resolver
enst
ENSMUST00000208190
resolver
enst
ENSMUST00000209098
resolver
genesymbol
Nap1l4
resolver
uniprot
A0A140LJ96
resolver
uniprot
A2RSB1
resolver
uniprot
B7ZNL2
resolver
uniprot
O88701
resolver
uniprot_entry
A0A140LJ96_MOUSE
resolver
uniprot_entry
A2RSB1_MOUSE
resolver
uniprot_entry
B7ZNL2_MOUSE
resolver
uniprot_entry
NP1L4_MOUSE
resolver
uniprot_sec
O88701
resolver
amino_acid_sequence
MAENSLSDGGPADSVEAAKNASNTEKLTDQVMQNPQVLAALQERLDNVSHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESAWHSENEEEDKLAGDMKNKVVIAEKEAATVEELNPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNPVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFSPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDADVNPKV
uniprot
proteins
function
FUNCTION: Acts as a histone chaperone in nucleosome assembly (PubMed:28366643). In condensing spermatids, mediates the loading of the heterodimer composed of histones H2AB1 and H2BC1/TH2B onto the nucleosomes, thereby promoting the replacement of histones to protamine in male germ cells (PubMed:28366643). {ECO:0000269|PubMed:28366643}.
uniprot
proteins
mass_dalton
42679
uniprot
proteins
post_translational_modification
PTM: Polyglutamylated and polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Polyglutamylated by TTLL4. {ECO:0000269|PubMed:17499049}.; PTM: Phosphorylated at the G0/G1 boundary but it is not phosphorylated in S-phase. Phosphorylated protein remains in the cytoplasm in a complex with histones during the G0/G1 transition, whereas dephosphorylation triggers its transport into the nucleus at the G1/S-boundary. {ECO:0000250|UniProtKB:Q99733}.
uniprot
proteins
protein_family
Nucleosome assembly protein (NAP) family
uniprot
proteins
pubmed
11063728
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17499049
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21333655
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28366643
uniprot
proteins
pubmed
9618174
uniprot
proteins
sequence_length
375
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21333655}. Chromosome {ECO:0000269|PubMed:21333655}. Cytoplasm {ECO:0000269|PubMed:21333655}. Note=Present in the cytoplasm and excluded from the nucleus during G0/G1 phase, then relocates to the nucleus by the time cells are in S phase. Phosphorylated form localizes in the cytoplasm during the G0/G1 transition, whereas dephosphorylation leads to relocalization into the nucleus at the G1/S-boundary. {ECO:0000250|UniProtKB:Q99733}.
uniprot
proteins