Search by BoMiProt ID - Bomi7707


Primary Information

BoMiProt ID Bomi7707
Protein Name Nucleosome assembly protein 1-like 1
Organism Bos taurus
Uniprot IdA6H767
Milk FractionExosomes
Ref Sequence Id NP_001092685.1
Aminoacid Length 391
Molecular Weight 45376
Fasta Sequence https://www.uniprot.org/uniprot/A6H767.fasta
Gene Name NAP1L1
Gene Id 790872
Protein Existence Status reviewed

Secondary Information

Protein Function Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly. Participates also in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair. Stimulates also homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair
PTMs Acetylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A6H767|NP1L1_BOVIN Nucleosome assembly protein 1-like 1 OS=Bos taurus OX=9913 GN=NAP1L1 PE=2 SV=1 MADIDNKEQS*10ELDQDLDDVEEVEEEETGEETKIKARQLTVQMMQNPQILAALQERLDGLV ET*62PT*64GYIES*69LPRVVKRRVNALKNLQVKCAQIEAKFYEEVHDLERKYAVLYQPLFDKRFEI INAIYEPTEEECEWKPDEEDEIS*143EELKEKAKVEDEKKDEEKEDPKGIPEFWLTVFKNVDL LSDMVQEHDEPILKHLKDIKVKFSDAGQPMSFVLEFHFEPNEYFTNEVLTKTYRMRSEPD DSDPFSFDGPEIMGCTGCQIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVSNDSFFNF FAPPEVPESGDLDDDSEAILAADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEE ADEEGEEEGDEENDPDYDPKKDQNPAECKQQ
Predicted Disorder Regions 1-46, 128-166, 237-250, 266-289, 302-317, 338-391
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs 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. 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.