Search Results
Overview
| Uniprot ID | Q7KZF4 |
|---|---|
| Protein Name | Staphylococcal nuclease domain-containing protein 1 |
| Gene Name | SND1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 193 | FVDSHHQKPVNAIIE |
| 339 | PTANLDQKDKQFVAK |
| 341 | ANLDQKDKQFVAKVM |
| 414 | RKKLIGKKVNVTVDY |
| 497 | GKGLHSKKEVPIHRV |
| 513 | DISGDTQKAKQFLPF |
| 515 | SGDTQKAKQFLPFLQ |
| 541 | VFSGSRLKLYLPKET |
| 641 | AERSSYYKSLLSAEE |
| 651 | LSAEEAAKQKKEKVW |
| 653 | AEEAAKQKKEKVWAH |
| 886 | LNAQESAKSARLNLW |
| 93 | LRKKLIGKEVCFTIE |
Function
Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:18453631, PubMed:28546213). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0097433 | dense body |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0042470 | melanosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0031332 | RNAi effector complex |
| Molecular Function | GO:1990599 | 3' overhang single-stranded DNA endodeoxyribonuclease activity |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0004519 | endonuclease activity |
| Molecular Function | GO:1905172 | RISC complex binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0004521 | RNA endonuclease activity |
| Molecular Function | GO:0003712 | transcription coregulator activity |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0010587 | miRNA catabolic process |
| Biological Process | GO:0006402 | mRNA catabolic process |
| Biological Process | GO:0001649 | osteoblast differentiation |
| Biological Process | GO:0010564 | regulation of cell cycle process |
| Biological Process | GO:0031047 | regulatory ncRNA-mediated gene silencing |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.