Search Results
Overview
| Uniprot ID | Q922B1 |
|---|---|
| Protein Name | ADP-ribose glycohydrolase MACROD1 |
| Gene Name | Macrod1 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | KEAKSFLKGLSDKQR |
| 106 | FLKGLSDKQREEHYF |
| 115 | REEHYFCKDFIKLKK |
| 131 | PTWKETAKGLAVKVE |
| 136 | TAKGLAVKVEDPKYK |
| 141 | AVKVEDPKYKKDKQL |
| 146 | DPKYKKDKQLNEKIS |
| 207 | LQNCETGKAKITCGY |
| 209 | NCETGKAKITCGYRL |
| 94 | LSTSTDWKEAKSFLK |
Function
Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0140293 | ADP-ribosylglutamate hydrolase activity |
| Molecular Function | GO:0019213 | deacetylase activity |
| Molecular Function | GO:0016798 | hydrolase activity, acting on glycosyl bonds |
| Molecular Function | GO:0061463 | O-acetyl-ADP-ribose deacetylase activity |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0140291 | peptidyl-glutamate ADP-deribosylation |
| Biological Process | GO:0051725 | protein de-ADP-ribosylation |
| Biological Process | GO:0042278 | purine nucleoside metabolic process |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.