Search Results

Overview

Uniprot IDP62308
Protein NameSmall nuclear ribonucleoprotein G
Gene NameSNRPG
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
10 KAHPPELKKFMDKKL
3 *****MSKAHPPELK

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). As part of the U7 snRNP it is involved in histone 3'-end processing (PubMed:12975319)

Protein Sequence

10 MSKAHPPELK 20 KFMDKKLSLK 30 LNGGRHVQGI 40 LRGFDPFMNL 50 VIDECVEMAT 60 SGQQNNIGMV 70 VIRGNSIIML EALERV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0034709 methylosome
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0043186 P granule
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:0097526 spliceosomal tri-snRNP 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:0071004 U2-type prespliceosome
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
Cellular Component GO:0005683 U7 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:0071045 nuclear histone mRNA catabolic process
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 D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] 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.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.