NAP1L1
entrez
4673
canonical
uniprot
P55209
canonical
ensembl
ENSG00000187109
resolver
ensp
ENSP00000376947
resolver
ensp
ENSP00000445008
resolver
ensp
ENSP00000448167
resolver
ensp
ENSP00000450236
resolver
ensp
ENSP00000477538
resolver
ensp
ENSP00000550619
resolver
ensp
ENSP00000550621
resolver
enst
ENST00000535020
resolver
enst
ENST00000547773
resolver
enst
ENST00000880562
resolver
genesymbol
NAP1L1
resolver
genesymbol_syn
NRP
resolver
hgnc
HGNC:7637
resolver
uniprot
B3KNT8
resolver
uniprot
B3KV44
resolver
uniprot
B7Z2V4
resolver
uniprot
F5H4R6
resolver
uniprot
F8W543
resolver
uniprot
Q9H2B0
resolver
uniprot_entry
B7Z2V4_HUMAN
resolver
uniprot_entry
F5H4R6_HUMAN
resolver
uniprot_entry
F8W543_HUMAN
resolver
uniprot_entry
NP1L1_HUMAN
resolver
uniprot_entry
Q9H2B0_HUMAN
resolver
uniprot_sec
B3KNT8
resolver
uniprot_sec
B3KV44
resolver
amino_acid_sequence
MADIDNKEQSELDQDLDDVEEVEEEETGEETKLKARQLTVQMMQNPQILAALQERLDGLVETPTGYIESLPRVVKRRVNALKNLQVKCAQIEAKFYEEVHDLERKYAVLYQPLFDKRFEIINAIYEPTEEECEWKPDEEDEISEELKEKAKIEDEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMVQEHDEPILKHLKDIKVKFSDAGQPMSFVLEFHFEPNEYFTNEVLTKTYRMRSEPDDSDPFSFDGPEIMGCTGCQIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVSNDSFFNFFAPPEVPESGDLDDDAEAILAADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADEEGEEEGDEENDPDYDPKKDQNPAECKQQ
uniprot
proteins
function
FUNCTION: Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, PubMed:26841755). Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616). Also stimulates 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). {ECO:0000250|UniProtKB:P28656, ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:24798879, ECO:0000269|PubMed:26841755, ECO:0000269|PubMed:28369616}.; FUNCTION: (Microbial infection) Positively regulates Epstein-Barr virus reactivation in epithelial cells through the induction of viral BZLF1 expression. {ECO:0000269|PubMed:23691099}.; FUNCTION: (Microbial infection) Together with human herpesvirus 8 protein LANA1, assists the proper assembly of the nucleosome on the replicated viral DNA. {ECO:0000269|PubMed:27599637}.
uniprot
proteins
mass_dalton
45374
uniprot
proteins
mutagenesis
MUTAGEN 126; /note="E->A: Impaired binding to histones and ability to mediate histone chaperone activity."; /evidence="ECO:0000269|PubMed:21211722"; MUTAGEN 130; /note="E->A: Impaired binding to histones and ability to mediate histone chaperone activity."; /evidence="ECO:0000269|PubMed:21211722"; MUTAGEN 134; /note="W->A: Impaired binding to histones and ability to mediate histone chaperone activity."; /evidence="ECO:0000269|PubMed:21211722
uniprot
proteins
post_translational_modification
PTM: Monoglycylated on glutamate residues. Cannot be polyglycylated due to the absence of functional TTLL10 in human (By similarity). {ECO:0000250|UniProtKB:P28656, ECO:0000305}.; PTM: 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. {ECO:0000250|UniProtKB:P28656}.
uniprot
proteins
protein_family
Nucleosome assembly protein (NAP) family
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15308774
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18226242
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20002496
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21211722
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23691099
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24798879
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26841755
uniprot
proteins
pubmed
27599637
uniprot
proteins
pubmed
28369616
uniprot
proteins
pubmed
28659470
uniprot
proteins
pubmed
29899097
uniprot
proteins
pubmed
8297347
uniprot
proteins
sequence_length
391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:27599637}. Chromosome {ECO:0000250|UniProtKB:P28656}. Melanosome {ECO:0000269|PubMed:17081065}. Cytoplasm {ECO:0000269|PubMed:20002496, ECO:0000269|PubMed:28659470}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
uniprot
proteins