Search Results
Overview
| Uniprot ID | P10824 |
|---|---|
| Protein Name | Guanine nucleotide-binding protein G(i) subunit alpha-1 |
| Gene Name | Gnai1 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 132 | GVIKRLWKDSGVQAC |
| 180 | DVLRTRVKTTGIVET |
| 192 | VETHFTFKDLHFKMF |
| 46 | LGAGESGKSTIVKQM |
| 51 | SGKSTIVKQMKIIHE |
| 67 | GYSEEECKQYKAVVY |
| 92 | IRAMGRLKIDFGDAA |
Function
Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:19703466, PubMed:24596087, PubMed:25037222). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:21158412). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:21158412). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity of ADCY1, ADCY5 and ADCY6, leading to decreased intracellular cAMP levels (PubMed:19703466). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed:16870394). Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005938 | cell cortex |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0005834 | heterotrimeric G-protein complex |
| Cellular Component | GO:0030496 | midbody |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0098794 | postsynapse |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0010855 | adenylate cyclase inhibitor activity |
| Molecular Function | GO:0031749 | D2 dopamine receptor binding |
| Molecular Function | GO:0003925 | G protein activity |
| Molecular Function | GO:0001664 | G protein-coupled receptor binding |
| Molecular Function | GO:0031821 | G protein-coupled serotonin receptor binding |
| Molecular Function | GO:0031683 | G-protein beta/gamma-subunit complex binding |
| Molecular Function | GO:0019003 | GDP binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0032794 | GTPase activating protein binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Biological Process | GO:0007193 | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
| Biological Process | GO:0007198 | adenylate cyclase-inhibiting serotonin receptor signaling pathway |
| Biological Process | GO:0007188 | adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:1904322 | cellular response to forskolin |
| Biological Process | GO:0070098 | chemokine-mediated signaling pathway |
| Biological Process | GO:0007186 | G protein-coupled receptor signaling pathway |
| Biological Process | GO:0043303 | mast cell degranulation |
| Biological Process | GO:0050805 | negative regulation of synaptic transmission |
| Biological Process | GO:0099645 | neurotransmitter receptor localization to postsynaptic specialization membrane |
| Biological Process | GO:0045542 | positive regulation of cholesterol biosynthetic process |
| Biological Process | GO:1904778 | positive regulation of protein localization to cell cortex |
| Biological Process | GO:0060236 | regulation of mitotic spindle organization |
| Biological Process | GO:0034695 | response to prostaglandin E |
| Biological Process | GO:0072678 | T cell migration |
Reference
[1] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.
[2] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.