Search Results
Overview
| Uniprot ID | O00566 |
|---|---|
| Protein Name | U3 small nucleolar ribonucleoprotein protein MPP10 |
| Gene Name | MPHOSPH10 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 157 | ERAENSSKSDLRKSP |
| 185 | SKLEQQSKVQNKGQG |
| 612 | DQAGKYSKTVASEKL |
| 641 | EGKDKALKSSQAFFS |
| 649 | SSQAFFSKLQDQVKM |
| 655 | SKLQDQVKMQINDAK |
Function
Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (PubMed:12655004). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0000375 | RNA splicing, via transesterification reactions |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0034457 | Mpp10 complex |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0032040 | small-subunit processome |
| Cellular Component | GO:0005732 | sno(s)RNA-containing ribonucleoprotein complex |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0030490 | maturation of SSU-rRNA |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
| Biological Process | GO:0006396 | RNA processing |
| Biological Process | GO:0008380 | RNA splicing |
Reference
[1] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[4] 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.