Search Results
Overview
| Uniprot ID | Q13586 |
|---|---|
| Protein Name | Stromal interaction molecule 1 |
| Gene Name | STIM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 279 | HRTVEVEKVHLEKKL |
| 580 | PDSPALAKKALLALN |
| 581 | DSPALAKKALLALNH |
| 650 | RIPHLAGKKAVAEED |
| 651 | IPHLAGKKAVAEEDN |
Function
Acts as a Ca(2+) sensor that gates two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19182790, PubMed:19249086, PubMed:19622606, PubMed:19706554, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:25326555, PubMed:26322679, PubMed:28219928, PubMed:32415068). Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate sustained and oscillatory Ca(2+) entry (PubMed:16208375, PubMed:16537481, PubMed:32415068). Involved in enamel formation (PubMed:24621671). Plays a role in regulating the type I interferon response by retaining the signaling adapter STING at the endoplasmic reticulum (PubMed:30643259)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0032541 | cortical endoplasmic reticulum |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0044853 | plasma membrane raft |
| Cellular Component | GO:0033017 | sarcoplasmic reticulum membrane |
| Molecular Function | GO:0005246 | calcium channel regulator activity |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0051010 | microtubule plus-end binding |
| Molecular Function | GO:0002020 | protease binding |
| Biological Process | GO:0032237 | activation of store-operated calcium channel activity |
| Biological Process | GO:0005513 | detection of calcium ion |
| Biological Process | GO:0070166 | enamel mineralization |
| Biological Process | GO:0006874 | intracellular calcium ion homeostasis |
| Biological Process | GO:0045762 | positive regulation of adenylate cyclase activity |
| Biological Process | GO:0045766 | positive regulation of angiogenesis |
| Biological Process | GO:0051924 | regulation of calcium ion transport |
| Biological Process | GO:2001256 | regulation of store-operated calcium entry |
| Biological Process | GO:0002115 | store-operated calcium entry |
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] 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.
[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.