STIM1 (stromal interaction molecule 1) is a single-pass type I endoplasmic reticulum membrane protein that acts as the ER calcium sensor for store-operated calcium entry (SOCE). Its lumenal EF-hand/SAM region binds Ca(2+); depletion of ER Ca(2+) causes STIM1 to oligomerize and undergo a conformational change that exposes the cytoplasmic SOAR/CAD domain. STIM1 then accumulates at ER-plasma membrane junctions (cortical ER), where it directly binds and gates the ORAI1/2/3 CRAC channel pore subunits to drive calcium influx. STIM1 also regulates adenylyl cyclase and TRPC channels, tracks growing microtubule plus-ends via an EB1-binding motif, and in muscle resides in the sarcoplasmic reticulum. Gain-of-function mutations cause tubular aggregate myopathy/Stormorken syndrome and loss of function causes a CRAC channelopathy.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002020 protease binding | IPI PMID:25384971 A protease-independent function for SPPL3 in NFAT activation... | KEEP AS NON CORE | Summary: STIM1 binds the intramembrane protease SPPL3; the interaction promotes STIM1-ORAI1 association and is protease-independent. Reason: Binding a protease (SPPL3) is a specific interaction that regulates STIM1 coupling to ORAI1, peripheral to the core sensor-gating function. Supporting Evidence: PMID:25384971 SPPL3 associates with STIM1 through at least two independent domains, the transmembrane region and the CRAC activation domain (CAD), and can promote the association of the STIM1 CAD with Orai1 |
| GO:0002115 store-operated calcium entry | IBA GO_REF:0000033 | ACCEPT | Summary: Store-operated calcium entry, inherited across the STIM clade. Reason: Core biological process for STIM1. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0002115 store-operated calcium entry | IDA PMID:19182790 SOAR and the polybasic STIM1 domains gate and regulate Orai ... | ACCEPT | Summary: SOAR/polybasic domains gate and regulate Orai channels in SOCE. Reason: Core process. Supporting Evidence: PMID:19182790 SOAR and the polybasic STIM1 domains gate and regulate Orai channels |
| GO:0002115 store-operated calcium entry | IDA PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(... | ACCEPT | Summary: STIM1 mediates mitochondria-controlled SOCE. Reason: Core process. Supporting Evidence: PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(+) and redox signals |
| GO:0005246 calcium channel regulator activity | IBA GO_REF:0000033 | ACCEPT | Summary: Calcium channel regulator activity, inherited across the STIM clade. Reason: Core molecular function - STIM1 gates CRAC channels. Supporting Evidence: PMID:19249086 STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1 |
| GO:0005246 calcium channel regulator activity | IDA PMID:25326555 Clinical, histological and genetic characterisation of patie... | ACCEPT | Summary: Myopathy mutants show altered channel regulation. Reason: Core molecular function. Supporting Evidence: PMID:25326555 tubular aggregate myopathy caused by mutations in STIM1 |
| GO:0005246 calcium channel regulator activity | IDA PMID:26322679 Proteomic mapping of ER-PM junctions identifies STIMATE as a... | ACCEPT | Summary: STIM1 regulates Ca2+ influx at ER-PM junctions. Reason: Core molecular function. Supporting Evidence: PMID:26322679 a regulator of Ca |
| GO:0005246 calcium channel regulator activity | IEA GO_REF:0000120 | ACCEPT | Summary: Automated calcium channel regulator activity. Reason: Consistent with direct evidence. Supporting Evidence: PMID:19249086 STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1 |
| GO:0005246 calcium channel regulator activity | IGI PMID:31009446 Molecular understanding of calcium permeation through the op... | ACCEPT | Summary: Genetic interaction with ORAI shows STIM1 gates the open channel. Reason: Core molecular function. Supporting Evidence: PMID:31009446 Molecular understanding of calcium permeation through the open Orai channel |
| GO:0005509 calcium ion binding | IBA GO_REF:0000033 | ACCEPT | Summary: Calcium ion binding (EF-hand), inherited across the STIM clade. Reason: The lumenal EF-hand binds ER Ca(2+); core sensor function. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0005509 calcium ion binding | IDA PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-tri... | ACCEPT | Summary: STIM1 EF-hand binds Ca(2+) as the store sensor. Reason: Core sensor function. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0005509 calcium ion binding | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA calcium ion binding. Reason: Consistent with the EF-hand sensor. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0005513 detection of calcium ion | IDA PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-tri... | ACCEPT | Summary: Detection of calcium ion - the EF-hand detects ER store Ca(2+) depletion. Reason: Core sensing process. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0005515 protein binding | IPI PMID:11463338 Identification and characterization of the STIM (stromal int... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:17905723 STIM2 protein mediates distinct store-dependent and store-in... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:18484746 Calmodulin binding to the polybasic C-termini of STIM protei... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:19182790 SOAR and the polybasic STIM1 domains gate and regulate Orai ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:19249086 STIM1 clusters and activates CRAC channels via direct bindin... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:19632184 An EB1-binding motif acts as a microtubule tip localization ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:19706554 Molecular determinants of fast Ca2+-dependent inactivation a... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:19897728 Activation of TRPC1 by STIM1 in ER-PM microdomains involves ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:20418871 A novel EF-hand protein, CRACR2A, is a cytosolic Ca2+ sensor... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:20418871 A novel EF-hand protein, CRACR2A, is a cytosolic Ca2+ sensor... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:21408196 Local Ca²+ entry via Orai1 regulates plasma membrane recruit... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:21427704 STIM1 couples to ORAI1 via an intramolecular transition into... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:21876174 Calcium store sensor stromal-interaction molecule 1-dependen... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:21941299 Modulation of STIM1 and capacitative Ca2+ entry by the endop... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22084111 POST, partner of stromal interaction molecule 1 (STIM1), tar... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22084111 POST, partner of stromal interaction molecule 1 (STIM1), tar... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22451904 Structural and mechanistic insights into the activation of S... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22464749 SARAF inactivates the store operated calcium entry machinery... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22464749 SARAF inactivates the store operated calcium entry machinery... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22494970 Direct binding between Orai1 and AC8 mediates dynamic interp... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22494970 Direct binding between Orai1 and AC8 mediates dynamic interp... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:22586105 Junctate is a Ca2+-sensing structural component of Orai1 and... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:24954132 Remodeling of channel-forming ORAI proteins determines an on... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:24996186 Atomic force microscopy (AFM) imaging suggests that stromal ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:25996873 TMEM203 Is a Novel Regulator of Intracellular Calcium Homeos... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:26322679 Proteomic mapping of ER-PM junctions identifies STIMATE as a... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:27185316 Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhib... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:27185316 Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhib... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:30194290 Interrogating the protein interactomes of RAS isoforms ident... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:30481768 EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-S... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:30481768 EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-S... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:30481768 EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-S... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:30481768 EFHB is a Novel Cytosolic Ca2+ Sensor That Modulates STIM1-S... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32415068 The native ORAI channel trio underlies the diversity of Ca(2... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32415068 The native ORAI channel trio underlies the diversity of Ca(2... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32415068 The native ORAI channel trio underlies the diversity of Ca(2... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human c... | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005515 protein binding | IPI PMID:40355756 The solute carrier superfamily interactome. | REMOVE | Summary: Generic protein binding (IPI), various partners. Reason: GO:0005515 is uninformative about molecular function. STIM1 interactions are numerous and curated in UniProt SUBUNIT; removal follows the protein-binding policy and does not dispute any interaction. STIM1's informative regulatory function is captured by calcium channel regulator activity (GO:0005246) and identical protein binding (homo-oligomerization). |
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: Endoplasmic reticulum, inherited across the STIM clade. Reason: Core location - STIM1 is an ER-resident Ca(2+) sensor. Supporting Evidence: PMID:26322679 The ER-resident Ca2+ sensor protein, STIM1 |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: Immunofluorescence localizes STIM1 to the ER. Reason: Core location. Supporting Evidence: PMID:26322679 The ER-resident Ca2+ sensor protein, STIM1 |
| GO:0005783 endoplasmic reticulum | IDA PMID:27185316 Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhib... | ACCEPT | Summary: STIM1 localized to ER in CASQ1 study. Reason: Core location. Supporting Evidence: PMID:27185316 Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhibiting STIM1 Aggregation |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:16208375 STIM1 is a Ca2+ sensor that activates CRAC channels and migr... | ACCEPT | Summary: STIM1 is an ER-membrane Ca2+ sensor. Reason: Core location (single-pass ER membrane protein). Supporting Evidence: PMID:16208375 STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:22586105 Junctate is a Ca2+-sensing structural component of Orai1 and... | ACCEPT | Summary: STIM1 at the ER membrane (junctate study). Reason: Core location. Supporting Evidence: PMID:22586105 Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt ER membrane mapping. Reason: Core location. Supporting Evidence: file:human/STIM1/STIM1-uniprot.txt translocates from the endoplasmic reticulum to the plasma membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-1168376 | ACCEPT | Summary: Reactome places STIM1 at the ER membrane. Reason: Core location. Supporting Evidence: Reactome:R-HSA-1168376 |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2089927 | ACCEPT | Summary: Reactome ER membrane localization. Reason: Core location. Supporting Evidence: Reactome:R-HSA-2089927 |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2089943 | ACCEPT | Summary: Reactome ER membrane localization. Reason: Core location. Supporting Evidence: Reactome:R-HSA-2089943 |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt SubCell cytoskeleton mapping, reflecting the EB1-binding microtubule tip association. Reason: STIM1 tracks microtubule plus-ends via an EB1 motif; a peripheral association, not the core ER role. Supporting Evidence: PMID:19632184 An EB1-binding motif acts as a microtubule tip localization signal |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | MODIFY | Summary: Plasma membrane, inherited; STIM1 is active at ER-PM junctions, from the ER side, not in the plasma membrane proper. Reason: STIM1 is an ER protein that gates ORAI across ER-PM junctions from the ER membrane; the family function annotated here as plasma membrane is more precisely the endoplasmic reticulum-plasma membrane contact site (GO:0140268, a part of the plasma membrane region). A minor glycosylated genuinely-surface pool has been reported in the literature but is not what this inherited is_active_in assertion captures. Replaced with the contact-site term. Propagation Review Root cause: TERM SCOPING PROBLEM Proposed replacements: endoplasmic reticulum-plasma membrane contact site Supporting Evidence: PMID:17517596 activates Ca 2+ channels in the plasma membrane (PM) |
| GO:0005886 plasma membrane | IDA PMID:16208375 STIM1 is a Ca2+ sensor that activates CRAC channels and migr... | MODIFY | Summary: Early study reported STIM1 migration to the plasma membrane; mechanistically this is redistribution to ER-PM junctions. Reason: The "migration to the plasma membrane" is STIM1 oligomerizing and accumulating at ER-PM junctions upon store depletion, where it gates ORAI from the ER side; the accurate location is the ER-plasma membrane contact site (GO:0140268), a more specific part of the plasma membrane region, not PM insertion. Proposed replacements: endoplasmic reticulum-plasma membrane contact site Supporting Evidence: PMID:16208375 migrates from the Ca2+ store to the plasma membrane |
| GO:0005886 plasma membrane | IDA PMID:19171672 Capacitative Ca2+ entry via Orai1 and stromal interacting mo... | MODIFY | Summary: STIM1 at the PM region in the AC8/capacitative entry study; this is the ER-PM junction. Reason: Capacitative (store-operated) entry is gated by STIM1 at ER-PM junctions; the accurate location is the ER-plasma membrane contact site (GO:0140268) rather than the plasma membrane proper. Proposed replacements: endoplasmic reticulum-plasma membrane contact site Supporting Evidence: PMID:19171672 Capacitative Ca2+ entry via Orai1 and stromal interacting molecule 1 (STIM1) regulates adenylyl cyclase type 8 |
| GO:0005886 plasma membrane | IDA PMID:27185316 Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhib... | MODIFY | Summary: STIM1 near the PM in the CASQ1 study; this is the ER-PM junction. Reason: STIM1 aggregation/SOCE occurs at ER-PM junctions; the accurate location is the ER-plasma membrane contact site (GO:0140268) rather than the plasma membrane proper. Proposed replacements: endoplasmic reticulum-plasma membrane contact site Supporting Evidence: PMID:27185316 Calsequestrin-1 Regulates Store-Operated Ca2+ Entry by Inhibiting STIM1 Aggregation |
| GO:0005886 plasma membrane | IDA PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(... | MODIFY | Summary: STIM1 near the PM in the mitochondria/SOCE study; this is the ER-PM junction. Reason: Store-operated entry is gated by STIM1 at ER-PM junctions; the accurate location is the ER-plasma membrane contact site (GO:0140268) rather than the plasma membrane proper. Proposed replacements: endoplasmic reticulum-plasma membrane contact site Supporting Evidence: PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(+) and redox signals |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | MODIFY | Summary: UniProt SubCell plasma membrane mapping, reflecting the store-depletion translocation toward the PM. Reason: The UniProt "translocates from the endoplasmic reticulum to the plasma membrane" describes STIM1 redistributing to ER-PM junctions on store depletion; the accurate location is the ER-plasma membrane contact site (GO:0140268), a more specific part of the plasma membrane region, not PM insertion. Proposed replacements: endoplasmic reticulum-plasma membrane contact site Supporting Evidence: file:human/STIM1/STIM1-uniprot.txt translocates from the endoplasmic reticulum to the plasma membrane |
| GO:0006874 intracellular calcium ion homeostasis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Intracellular calcium ion homeostasis, inherited. Reason: True and important but broader than the specific SOCE role; retained as non-core. Supporting Evidence: file:human/STIM1/STIM1-uniprot.txt a Ca(2+) influx following depletion |
| GO:0016529 sarcoplasmic reticulum | EXP PMID:25326555 Clinical, histological and genetic characterisation of patie... | KEEP AS NON CORE | Summary: STIM1 in the sarcoplasmic reticulum in muscle (myopathy patients). Reason: SR is the muscle-specialized ER; a tissue-specific location of the same protein. Supporting Evidence: PMID:25326555 tubular aggregate myopathy caused by mutations in STIM1 |
| GO:0016529 sarcoplasmic reticulum | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt SubCell sarcoplasmic reticulum mapping. Reason: Tissue-specific (muscle) location. Supporting Evidence: file:human/STIM1/STIM1-uniprot.txt translocates from the endoplasmic reticulum to the plasma membrane |
| GO:0032237 activation of store-operated calcium channel activity | IDA PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-tri... | ACCEPT | Summary: STIM1 activates store-operated calcium channels. Reason: Core process - the direct output of STIM1 gating. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0032237 activation of store-operated calcium channel activity | IDA PMID:26322679 Proteomic mapping of ER-PM junctions identifies STIMATE as a... | ACCEPT | Summary: STIM1 activates SOC channels at ER-PM junctions. Reason: Core process. Supporting Evidence: PMID:26322679 store operated calcium entry (SOCE) |
| GO:0032237 activation of store-operated calcium channel activity | IDA PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(... | ACCEPT | Summary: STIM1 activation of SOC channels (mitochondria study). Reason: Core process. Supporting Evidence: PMID:28219928 Mitochondria control store-operated Ca(2+) entry through Na(+) and redox signals |
| GO:0032541 cortical endoplasmic reticulum | IDA PMID:22586105 Junctate is a Ca2+-sensing structural component of Orai1 and... | ACCEPT | Summary: STIM1 at cortical ER (ER-PM junctions). Reason: Core location where STIM1 gates ORAI across the junction. Supporting Evidence: PMID:22586105 Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 |
| GO:0032541 cortical endoplasmic reticulum | TAS PMID:26322679 Proteomic mapping of ER-PM junctions identifies STIMATE as a... | ACCEPT | Summary: Cortical ER at ER-PM junctions. Reason: Core location. Supporting Evidence: PMID:26322679 map the proteome of ER-PM junctions that are dedicated to store operated calcium entry |
| GO:0033017 sarcoplasmic reticulum membrane | IDA PMID:25326555 Clinical, histological and genetic characterisation of patie... | KEEP AS NON CORE | Summary: STIM1 in sarcoplasmic reticulum membrane (muscle). Reason: Tissue-specific location of the ER-membrane protein. Supporting Evidence: PMID:25326555 tubular aggregate myopathy caused by mutations in STIM1 |
| GO:0042802 identical protein binding | IPI PMID:17517596 Live-cell imaging reveals sequential oligomerization and loc... | ACCEPT | Summary: Identical protein binding - STIM1 homo-oligomerization. Reason: STIM1 oligomerizes on Ca(2+)-store depletion; self-association is central to its activation mechanism. Supporting Evidence: PMID:17517596 Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2+ store depletion |
| GO:0042802 identical protein binding | IPI PMID:19249086 STIM1 clusters and activates CRAC channels via direct bindin... | ACCEPT | Summary: Identical protein binding - STIM1 homo-oligomerization. Reason: STIM1 oligomerizes on Ca(2+)-store depletion; self-association is central to its activation mechanism. Supporting Evidence: PMID:17517596 Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2+ store depletion |
| GO:0042802 identical protein binding | IPI PMID:20418871 A novel EF-hand protein, CRACR2A, is a cytosolic Ca2+ sensor... | ACCEPT | Summary: Identical protein binding - STIM1 homo-oligomerization. Reason: STIM1 oligomerizes on Ca(2+)-store depletion; self-association is central to its activation mechanism. Supporting Evidence: PMID:17517596 Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2+ store depletion |
| GO:0042802 identical protein binding | IPI PMID:21427704 STIM1 couples to ORAI1 via an intramolecular transition into... | ACCEPT | Summary: Identical protein binding - STIM1 homo-oligomerization. Reason: STIM1 oligomerizes on Ca(2+)-store depletion; self-association is central to its activation mechanism. Supporting Evidence: PMID:17517596 Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2+ store depletion |
| GO:0042802 identical protein binding | IPI PMID:22451904 Structural and mechanistic insights into the activation of S... | ACCEPT | Summary: Identical protein binding - STIM1 homo-oligomerization. Reason: STIM1 oligomerizes on Ca(2+)-store depletion; self-association is central to its activation mechanism. Supporting Evidence: PMID:17517596 Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2+ store depletion |
| GO:0042802 identical protein binding | IPI PMID:24996186 Atomic force microscopy (AFM) imaging suggests that stromal ... | ACCEPT | Summary: Identical protein binding - STIM1 homo-oligomerization. Reason: STIM1 oligomerizes on Ca(2+)-store depletion; self-association is central to its activation mechanism. Supporting Evidence: PMID:17517596 Live-cell imaging reveals sequential oligomerization and local plasma membrane targeting of stromal interaction molecule 1 after Ca2+ store depletion |
| GO:0044853 plasma membrane raft | IDA PMID:19171672 Capacitative Ca2+ entry via Orai1 and stromal interacting mo... | KEEP AS NON CORE | Summary: STIM1 in plasma membrane rafts regulating AC8. Reason: Minor PM-raft pool linked to adenylyl cyclase regulation; peripheral. Supporting Evidence: PMID:19171672 Capacitative Ca2+ entry via Orai1 and stromal interacting molecule 1 (STIM1) regulates adenylyl cyclase type 8 |
| GO:0045762 positive regulation of adenylate cyclase activity | IDA PMID:19171672 Capacitative Ca2+ entry via Orai1 and stromal interacting mo... | KEEP AS NON CORE | Summary: STIM1/Orai1-dependent capacitative entry positively regulates adenylyl cyclase 8. Reason: Downstream signaling output of SOCE; peripheral to the core sensor-gating function. Supporting Evidence: PMID:19171672 regulates adenylyl cyclase type 8 |
| GO:0045766 positive regulation of angiogenesis | IMP PMID:26694763 MicroRNA-185 inhibits angiogenesis in human microvascular en... | KEEP AS NON CORE | Summary: STIM1 promotes angiogenesis (miR-185 knockdown of STIM1 reduces it). Reason: Downstream physiological role of SOCE in endothelial cells; not a core STIM1 function. Supporting Evidence: PMID:26694763 MicroRNA-185 inhibits angiogenesis in human microvascular endothelial cells through targeting stromal interaction molecule 1 |
| GO:0051010 microtubule plus-end binding | IDA PMID:19632184 An EB1-binding motif acts as a microtubule tip localization ... | KEEP AS NON CORE | Summary: STIM1 binds microtubule plus-ends via an EB1-binding tip motif. Reason: A genuine but peripheral molecular function; links ER tubules to growing microtubules. Supporting Evidence: PMID:19632184 An EB1-binding motif acts as a microtubule tip localization signal |
| GO:0051924 regulation of calcium ion transport | IDA PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-tri... | KEEP AS NON CORE | Summary: Regulation of calcium ion transport. Reason: True and directly supported, but broader than the specific SOCE activation terms; retained as non-core. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0051924 regulation of calcium ion transport | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA regulation of calcium ion transport. Reason: Consistent broad regulatory term; non-core. Supporting Evidence: PMID:16005298 STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx |
| GO:0070166 enamel mineralization | IMP PMID:24621671 STIM1 and SLC24A4 Are Critical for Enamel Maturation. | KEEP AS NON CORE | Summary: STIM1 is required for enamel maturation. Reason: Tissue-specific developmental outcome of SOCE in ameloblasts; downstream of the core function. Supporting Evidence: PMID:24621671 STIM1 and SLC24A4 Are Critical for Enamel Maturation |
| GO:2001256 regulation of store-operated calcium entry | IMP PMID:23332920 Constitutive activation of the calcium sensor STIM1 causes t... | ACCEPT | Summary: Regulation of store-operated calcium entry; constitutively active STIM1 mutants cause myopathy. Reason: Core regulatory process directly tied to STIM1 activation state. Supporting Evidence: PMID:23332920 Constitutive activation of the calcium sensor STIM1 causes tubular-aggregate myopathy |
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Download this section (compressed HTML)Q: What fraction of STIM1 genuinely resides in the plasma membrane versus accumulating at ER-PM junctions, and does the surface pool have a distinct function?
Q: How do STIM1 GoF myopathy mutations alter the conformational switch independently of ER Ca(2+)?
Experiment: Super-resolution and split-fluorophore ER-PM junction imaging in cells expressing STIM1 variants to quantify junctional versus surface STIM1 and correlate with CRAC current.
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