Primary Information |
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| BoMiProt ID | Bomi7707 |
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| Protein Name | Nucleosome assembly protein 1-like 1 |
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| Organism | Bos taurus |
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| Uniprot ID | A6H767 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001092685.1 |
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| Aminoacid Length | 391 |
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| Molecular Weight | 45376 |
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| FASTA Sequence |
Download |
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| Gene Name | NAP1L1 |
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| Gene ID | 790872 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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 |
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| PTMs | Acetylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation |
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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
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| Predicted Disorder Regions | 1-46, 128-166, 237-250, 266-289, 302-317, 338-391 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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. |
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