Primary Information |
|---|
| BoMiProt ID | Bomi3640 |
|---|
| Protein Name | Active regulator of SIRT1/40S ribosomal protein S19-binding protein 1/RPS19-binding protein 1/S19BP |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | A6H7J2 |
|---|
| Milk Fraction | Whey |
|---|
| Ref Sequence ID | NP_001092386.1 |
|---|
| Aminoacid Length | 137 |
|---|
| Molecular Weight | 15367 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | RPS19BP1/AROS |
|---|
| Gene ID | 509108 |
|---|
| Protein Existence Status | reviewed |
|---|
Secondary Information |
|---|
| Protein Function | Participating in inhibition of p53/TP53-mediated transcriptional activity .This protein regulates SIRT1. by positively regulating SIRT1-mediated deacetylation of p53/TP53.AROS binds RPS19, a structural ribosomal protein, which also functions in ribosome biogenesis and is implicated in multiple disease states. |
|---|
| Biochemical Properties | NAD(+)-dependent enzyme. Shows deacetylase activity.Sirt1 regulates gene transcription via deacetylation of transcription factors.Sirt1 deacetylates p53 in the cytosol, blocking p53 nuclear translocation and ability to induce apoptosis .The structural integrity of the Zn2+-tetrathiolate is essential for Sirt1 deacetylase activity. |
|---|
| Significance in milk | involved in oxidative stress and lipid metabolism regulation. |
|---|
| PTMs | Citrullination, Phosphorylation,Glutathionylation |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A6H7J2|AROS_BOVIN Active regulator of SIRT1 OS=Bos taurus OX=9913 GN=RPS19BP1 PE=2 SV=1
MSAALLRRGLELLGAPEAPGAAPGHTKPSQAPMKRTRKAKATQAQKLRNSAKGKVPKSAL
AEFRKKERRGYLGVNLRFMTSARS*84TVDESVTRQIMRQNRGRKACDRPVTKTKKKKKAEGT
VFTEEDFQKFQREYFGS
|
|---|
| Predicted Disorder Regions | (1-137) |
|---|
| DisProt Annotation | |
|---|
| TM Helix Prediction | No TM helices |
|---|
| Significance of PTMs | Citrullination is carried out by PADI4. Sirt1 is both modified and inhibited by S-nitrosation.S-nitrosation of Sirt1 is reversible with thiol-based reductants.The S-nitrosation sites of Sirt1 are localized to Cys395 or Cys398 of the Zn2+-tetrathiolate via serine mutagenesis.The structural integrity of the Zn2+-tetrathiolate is essential for Sirt1 deacetylase activity because treatment of recombinant Sirt1 with nitrosating agents or mutation of any of the four tetrathiolate cysteines to serine resulted in Zn2+ loss.Primary hepatocytes from Wistar rats showed Sirt1 S-nitrosation when cultured in media supplemented with cholic acid to alter bile salt homeostasis.Glutathionylation can inhibit Sirt1 activity.In animal models, Sirt1 glutathionylation occurs during oxidative stress. Sirt1 glutathionylation was observed in livers of C57/B6J mice fed a high fat, high-sucrose diet, which promoted production of ROS (assessed via dichlorodihydrofluorescein fluorescence), inhibition of Sirt1 deacetylase activity, and apoptosis via increased p53 acetylation. |
|---|
| Additional Comments | Although Sirt1 can shuttle between the nucleus and cytoplasm, Sirt1 localization is primarily nuclear |
|---|
| Bibliography | 1.Kalous KS, Wynia-Smith SL, Smith BC. Sirtuin Oxidative Post-translational Modifications. Front Physiol. 2021 Nov 24;12:763417. doi: 10.3389/fphys.2021.763417. PMID: 34899389; PMCID: PMC8652059. 2.Maeda, N., Toku, S., Kenmochi, N., & Tanaka, T. (2006). A novel nucleolar protein interacts with ribosomal protein S19. Biochemical and biophysical research communications, 339(1), 41–46. https://doi.org/10.1016/j.bbrc.2005.10.184 3.Knight, J. R., Willis, A. E., & Milner, J. (2013). Active regulator of SIRT1 is required for ribosome biogenesis and function. Nucleic acids research, 41(7), 4185–4197. https://doi.org/10.1093/nar/gkt129 |
|---|
