Search Results
Overview
| Uniprot ID | P62316 |
|---|---|
| Protein Name | Small nuclear ribonucleoprotein Sm D2 |
| Gene Name | SNRPD2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 118 | RNPLIAGK******* |
| 8 | MSLLNKPKSEMTPEE |
Function
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0034709 | methylosome |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0034715 | pICln-Sm protein complex |
| Cellular Component | GO:0071011 | precatalytic spliceosome |
| Cellular Component | GO:0030532 | small nuclear ribonucleoprotein complex |
| Cellular Component | GO:0034719 | SMN-Sm protein complex |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Cellular Component | GO:0005685 | U1 snRNP |
| Cellular Component | GO:0005689 | U12-type spliceosomal complex |
| Cellular Component | GO:0005686 | U2 snRNP |
| Cellular Component | GO:0071007 | U2-type catalytic step 2 spliceosome |
| Cellular Component | GO:0071005 | U2-type precatalytic spliceosome |
| Cellular Component | GO:0005684 | U2-type spliceosomal complex |
| Cellular Component | GO:0005687 | U4 snRNP |
| Cellular Component | GO:0046540 | U4/U6 x U5 tri-snRNP complex |
| Cellular Component | GO:0005682 | U5 snRNP |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0036261 | 7-methylguanosine cap hypermethylation |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0048025 | negative regulation of mRNA splicing, via spliceosome |
| Biological Process | GO:0008380 | RNA splicing |
| Biological Process | GO:0000245 | spliceosomal complex assembly |
| Biological Process | GO:0000387 | spliceosomal snRNP assembly |
| Biological Process | GO:0000244 | spliceosomal tri-snRNP complex assembly |
| Biological Process | GO:0000388 | spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) |
| Biological Process | GO:1903241 | U2-type prespliceosome assembly |
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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[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.