Search Results

Overview

Uniprot ID	O43665
Protein Name	Regulator of G protein signaling 10
Gene Name	RGS10
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
12	AVSRLSRKRPPSDIH
154	LKSDLFLKHKRTEEE
173	PDAQTAAKRASRIYN

Function

Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the muscarinic acetylcholine receptor CHRM2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:10608901, PubMed:11443111, PubMed:18434541, PubMed:8774883, PubMed:9353196). Modulates the activity of potassium channels that are activated in response to CHRM2 signaling (PubMed:11443111). Activity on GNAZ is inhibited by palmitoylation of the G protein (PubMed:9353196)

Protein Sequence

10 MFNRAVSRLS 20 RKRPPSDIHD 30 SDGSSSSSHQ 40 SLKSTAKWAA 50 SLENLLEDPE 60 GVKRFREFLK 70 KEFSEENVLF 80 WLACEDFKKM 90 QDKTQMQEKA 100 KEIYMTFLSS 110 KASSQVNVEG 120 QSRLNEKILE 130 EPHPLMFQKL 140 QDQIFNLMKY 150 DSYSRFLKSD 160 LFLKHKRTEE 170 EEEDLPDAQT 180 AAKRASRIYN T

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0016604	nuclear body
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0045202	synapse
Molecular Function	GO:0001965	G-protein alpha-subunit binding
Molecular Function	GO:0005096	GTPase activator activity
Molecular Function	GO:0003924	GTPase activity
Biological Process	GO:0007213	G protein-coupled acetylcholine receptor signaling pathway
Biological Process	GO:0007186	G protein-coupled receptor signaling pathway
Biological Process	GO:0009968	negative regulation of signal transduction
Biological Process	GO:0043547	positive regulation of GTPase activity
Biological Process	GO:0008277	regulation of G protein-coupled receptor signaling pathway

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] 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.

[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.

[6] 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.