CALM1 encodes calmodulin, a small calcium-sensor protein with four EF-hand calcium-binding sites. Human CALM1, CALM2 and CALM3 share the canonical calmodulin protein sequence, while their disease-associated variants and gene regulation remain distinct. Calcium-dependent conformational changes and target binding enable calmodulin to activate enzymes such as CaMKII and calcineurin and to regulate ion channels. Calmodulin supplies regulatory activity rather than the kinase, phosphatase or channel-pore activity of its partners. It acts in soluble pools and in partner-associated membrane and intracellular complexes. In cardiac cells, its control of CaV1.2 inactivation and RyR2 calcium release links calcium sensing to electrical and contractile function; pathogenic CALM1 variants can disrupt these interactions and cause severe arrhythmia.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005509 calcium ion binding | IBA GO_REF:0000033 | ACCEPT | Summary: The cached PAINT export places calcium binding at PTN000549682 and includes experimentally annotated human calmodulins among its descendants. Reason: The cached PAINT export places calcium binding at PTN000549682 and includes experimentally annotated human calmodulins among its descendants. Target-specific calcium-binding measurements and EF-hand structures independently support this central sensing mechanism; the target appearing among donors is legitimate experimental grounding, not circular transfer. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000549682 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. Supporting Evidence: PMID:23040497 Both CALM1 substitutions demonstrated compromised calcium binding |
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The exact PTN008588804 nuclear IBD is present in the cached family export, with rat calmodulin donors. Reason: The exact PTN008588804 nuclear IBD is present in the cached family export, with rat calmodulin donors. Retain the nuclear pool as a context-dependent localization, corroborated by the curated human sperm-nucleus proteomic annotation; the individual mass-spectrometry target record and full phylogenetic tree were not inspected. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN008588804 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. Supporting Evidence: |
| GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: PTN008588809 carries the exact sarcoplasmic-reticulum calcium-release regulation IBD, including human target evidence. Reason: PTN008588809 carries the exact sarcoplasmic-reticulum calcium-release regulation IBD, including human target evidence. Direct calmodulin-dependent regulation of RyR2 and human CALM1 arrhythmia variants support transfer; the mouse R2474S RyR2 experiment is model evidence rather than a CALM1 patient experiment. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008588809 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. |
| GO:0005513 detection of calcium ion | IBA GO_REF:0000033 | ACCEPT | Summary: The exact calcium-detection IBD at PTN008588809 is present, with human calmodulins as experimentally grounded descendants. Reason: The exact calcium-detection IBD at PTN008588809 is present, with human calmodulins as experimentally grounded descendants. Calcium binding changes target regulation rather than simply sequestering an ion, supporting the sensing process. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008588809 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. |
| GO:0097720 calcineurin-mediated signaling | IBA GO_REF:0000033 | ACCEPT | Summary: The exact PTN008588809 calcineurin-signaling IBD is present. Reason: The exact PTN008588809 calcineurin-signaling IBD is present. Human calmodulin mutagenesis directly couples calcium-dependent conformational opening to calcineurin activation; calmodulin supplies the regulatory activity, while calcineurin performs dephosphorylation. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008588809 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. Supporting Evidence: |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: The exact PTN008588804 cytoplasmic IBD agrees with human cellular assays and the curated UniProt localization. Reason: The exact PTN008588804 cytoplasmic IBD agrees with human cellular assays and the curated UniProt localization. Calmodulin acts as a soluble regulator and can be recruited to membrane-associated partners; the broad source compartment is retained without claiming exclusive cytosolic residence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008588804 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. |
| GO:0005813 centrosome | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PTN008588806 explicitly carries centrosome localization with human calmodulin source evidence. Reason: PTN008588806 explicitly carries centrosome localization with human calmodulin source evidence. The CP110 study and UniProt support a centrosomal pool and mitotic redistribution, retained as a cell-cycle context rather than the defining location of all calmodulin activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN008588806 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. Supporting Evidence: |
| GO:0043209 myelin sheath | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The cached PTN008588809 IBD explicitly supports myelin-sheath localization from rodent descendants. Reason: The cached PTN008588809 IBD explicitly supports myelin-sheath localization from rodent descendants. Human brain myelin-basic-protein association is compatible independent context, but is not itself proof of in situ sheath localization; the conserved localization is retained with that distinction. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN008588809 SUPPORTS TRANSFER Exact node/term IBD read in cached PTHR23048 PAINT table. Full tree and MSA were not independently reconstructed; human target evidence is legitimate descendant grounding. Supporting Evidence: |
| GO:0000922 spindle pole | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. Reason: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. The accessible CP110 cache contains selected narrative rather than the complete localization experiment, so the precise source resolution is retained by curator deference without claiming a newly inspected image. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00092938 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB-SubCell:SL-0448 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0002027 regulation of heart rate | IEA GO_REF:0000117 | ACCEPT | Summary: Human CALM1 variants segregate with or arise de novo in severe ventricular arrhythmia, and target-channel studies connect calcium sensing to rhythm control. Reason: Human CALM1 variants segregate with or arise de novo in severe ventricular arrhythmia, and target-channel studies connect calcium sensing to rhythm control. This supports the regulatory role in heart rate; it does not identify CALM1 as the pacemaker ion channel. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00087882 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0005246 calcium channel regulator activity | IEA GO_REF:0000117 | ACCEPT | Summary: Calmodulin directly regulates calcium-channel gating, including calcium-dependent inactivation of CaV1.2 and inhibition of RyR2-mediated calcium release. Reason: Calmodulin directly regulates calcium-channel gating, including calcium-dependent inactivation of CaV1.2 and inhibition of RyR2-mediated calcium release. This target-supported activity justifies the broad electronic regulator assertion; the protein is a regulator rather than a pore-forming channel. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00085486 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0005509 calcium ion binding | IEA GO_REF:0000120 | ACCEPT | Summary: The EF-hand/ARBA calcium-binding mapping is independently supported by human calmodulin calcium-affinity measurements and structures. Reason: The EF-hand/ARBA calcium-binding mapping is independently supported by human calmodulin calcium-affinity measurements and structures. Calcium binding is intrinsic to the protein and supplies the sensing mechanism for its downstream regulatory activities. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00043315 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. InterPro:IPR002048 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0005513 detection of calcium ion | IEA GO_REF:0000117 | ACCEPT | Summary: The ARBA calcium-detection assertion agrees with direct coupling between calcium binding, conformational change and target-enzyme activation. Reason: The ARBA calcium-detection assertion agrees with direct coupling between calcium binding, conformational change and target-enzyme activation. This is the calcium-sensor mechanism, not catalytic conversion of calcium. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00086881 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0005813 centrosome | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. Reason: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. The accessible CP110 cache contains selected narrative rather than the complete localization experiment, so the precise source resolution is retained by curator deference without claiming a newly inspected image. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00029136 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB-SubCell:SL-0048 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0005819 spindle | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. Reason: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. The accessible CP110 cache contains selected narrative rather than the complete localization experiment, so the precise source resolution is retained by curator deference without claiming a newly inspected image. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-SubCell:SL-0251 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0005876 spindle microtubule | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. Reason: The electronic spindle/centrosome localization agrees with the experimentally curated UniProt record, which describes mitotic enrichment at spindle poles and spindle microtubules. The accessible CP110 cache contains selected narrative rather than the complete localization experiment, so the precise source resolution is retained by curator deference without claiming a newly inspected image. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00033575 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0010856 adenylate cyclase activator activity | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Direct structural evidence establishes activation of the anthrax edema-factor adenylate cyclase by human calmodulin. Reason: Direct structural evidence establishes activation of the anthrax edema-factor adenylate cyclase by human calmodulin. Retain that real biochemical activity as a pathogen-associated context; this paper alone does not establish activation of a mammalian GPCR-linked adenylate cyclase. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00084977 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion | IEA GO_REF:0000117 | ACCEPT | Summary: Calmodulin regulates RyR2-dependent sarcoplasmic-reticulum calcium release, linking its own channel-regulatory work to cardiac contraction. Reason: Calmodulin regulates RyR2-dependent sarcoplasmic-reticulum calcium release, linking its own channel-regulatory work to cardiac contraction. The human CALM1 variant study and mouse RyR2 model provide complementary evidence, with their gene and species roles kept distinct. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00084948 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0019901 protein kinase binding | IEA GO_REF:0000117 | MODIFY | Summary: Binding to CaMKII is mechanistically coupled to release of kinase autoinhibition, rather than an unspecified kinase association. Reason: Binding to CaMKII is mechanistically coupled to release of kinase autoinhibition, rather than an unspecified kinase association. Refine the broad electronic binding claim to the independently demonstrated protein serine/threonine kinase activator activity; this does not imply that every kinase bound by calmodulin is activated. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: ARBA:ARBA00028598 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Proposed replacements: protein serine/threonine kinase activator activity |
| GO:0030017 sarcomere | IEA GO_REF:0000117 | ACCEPT | Summary: The curated RyR2 study places calmodulin in a sarcomeric calcium-release context, and independent FRET work reports Z-line-associated RyR2-bound calmodulin. Reason: The curated RyR2 study places calmodulin in a sarcomeric calcium-release context, and independent FRET work reports Z-line-associated RyR2-bound calmodulin. Retain the localization without equating calmodulin with a load-bearing sarcomeric structural protein or claiming that the original image was inspected. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00028261 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0031432 titin binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The primary human cardiac titin study directly tests recombinant kinase-region constructs and synthetic peptides for calcium-dependent calmodulin binding. Reason: The primary human cardiac titin study directly tests recombinant kinase-region constructs and synthetic peptides for calcium-dependent calmodulin binding. Retain this specific interaction; activation of titin kinase or a mechanosensory role is not established by the inspected abstract. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00085850 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0031514 motile cilium | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The electronic ciliary localization maps to the curated UniProt flagellar location, explicitly inferred from the mouse ortholog. Reason: The electronic ciliary localization maps to the curated UniProt flagellar location, explicitly inferred from the mouse ortholog. Retain this specialized localization with the source inference intact; no new human ciliary imaging or motility assay was inspected. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-SubCell:SL-0117 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0032465 regulation of cytokinesis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Calmodulin binding to CP110 has functional consequences for completion of cytokinesis: a CP110 mutant defective in calmodulin binding induces binucleate cells. Reason: Calmodulin binding to CP110 has functional consequences for completion of cytokinesis: a CP110 mutant defective in calmodulin binding induces binucleate cells. This provides more than an undifferentiated depletion phenotype, but defines a cell-cycle regulatory context rather than a separate universal core activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00084247 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: PMID:16760425 expression of a CP110 mutant unable to bind CaM also promotes cytokinesis failure |
| GO:0034704 calcium channel complex | IEA GO_REF:0000117 | ACCEPT | Summary: Calmodulin is a bound regulatory component of calcium-channel assemblies. Reason: Calmodulin is a bound regulatory component of calcium-channel assemblies. Human RyR2-peptide binding, RyR2-directed FRET and CaV1.2 inactivation experiments support channel-complex association; the source remains a broad complex annotation without an invented channel-specific complex identifier. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00085266 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0043539 protein serine/threonine kinase activator activity | IEA GO_REF:0000117 | ACCEPT | Summary: Human CaMKII/calmodulin structural and binding experiments show how calmodulin releases autoinhibition and permits kinase activation. Reason: Human CaMKII/calmodulin structural and binding experiments show how calmodulin releases autoinhibition and permits kinase activation. The phosphate-transfer activity belongs to CaMKII, while calmodulin is its calcium-responsive activator. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00085523 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0046872 metal ion binding | IEA GO_REF:0000043 | MODIFY | Summary: The metal-binding claim is correct but broader than the established EF-hand calcium-binding activity. Reason: The metal-binding claim is correct but broader than the established EF-hand calcium-binding activity. Refine it to calcium ion binding using the direct human calcium-affinity and structural evidence. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB-KW:KW-0479 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Proposed replacements: calcium ion binding |
| GO:0060291 long-term synaptic potentiation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: CaMKII activation provides a plausible regulatory contribution to long-term synaptic potentiation, and the cited structural paper discusses that established pathway. Reason: CaMKII activation provides a plausible regulatory contribution to long-term synaptic potentiation, and the cited structural paper discusses that established pathway. Its inspected experiments are purified human kinase/calmodulin structures and binding assays, not a new neuronal potentiation assay; retain the curated pathway assertion as contextual. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00091239 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0072542 protein phosphatase activator activity | IEA GO_REF:0000117 | ACCEPT | Summary: Human calmodulin mutants that restrict calcium-induced conformational change lose the ability to activate calcineurin, with activity recovered on chemical reduction. Reason: Human calmodulin mutants that restrict calcium-induced conformational change lose the ability to activate calcineurin, with activity recovered on chemical reduction. This supports the electronic phosphatase-regulatory/calcineurin-signaling assertion without transferring phosphatase catalysis to calmodulin. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00090664 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0097720 calcineurin-mediated signaling | IEA GO_REF:0000117 | ACCEPT | Summary: Human calmodulin mutants that restrict calcium-induced conformational change lose the ability to activate calcineurin, with activity recovered on chemical reduction. Reason: Human calmodulin mutants that restrict calcium-induced conformational change lose the ability to activate calcineurin, with activity recovered on chemical reduction. This supports the electronic phosphatase-regulatory/calcineurin-signaling assertion without transferring phosphatase catalysis to calmodulin. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00090525 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:1901844 regulation of cell communication by electrical coupling involved in cardiac conduction | IEA GO_REF:0000117 | ACCEPT | Summary: The human CALM1 arrhythmia study establishes a role in cardiac electrical regulation together with altered calcium sensing and RyR2 interaction. Reason: The human CALM1 arrhythmia study establishes a role in cardiac electrical regulation together with altered calcium sensing and RyR2 interaction. Retain the curated conduction-related regulation; no direct intercellular gap-junction conductance experiment is claimed from the abstract. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00091451 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0005515 protein binding | IPI PMID:30842726 An IQSEC2 Mutation Associated With Intellectual Disability a... | KEEP AS NON CORE | Summary: Calmodulin binds and modulates IQSEC2 in the tested calcium-dependent system. Reason: PMID:30842726 directly tests tagged IQSEC2 with calmodulin constructs in HEK293T cells and calmodulin affinity assays; calcium and detergent conditions affect the measured interaction. Cellular Arf6 activation supports a proposed regulatory mechanism, but it does not establish the old clathrin-binding assertion. Retain the experimentally supported IQSEC2 interaction as non-core. These shared calmodulin protein experiments do not establish CALM1-specific expression or regulation. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31983428 Interaction between IDH1 WT and calmodulin and its implicati... | MODIFY | Summary: Direct IDH1 binding supports enzyme binding. Reason: The complete PMID:31983428 abstract explicitly reports recombinant-protein pull-down, quantitative Kd measurements, peptide NMR and cellular co-immunoprecipitation for IDH1 and calmodulin. These establish binding to the catalytic enzyme; the reported migration/proliferation effects do not establish activation of IDH1 catalytic activity. Full Methods and Results were unavailable. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: Retain the curated OpenCell IQSEC2 association with independent target-binding corroboration. Reason: The accessible PMID:35271311 abstract and Discussion describe endogenous tagging and affinity-proteomic association mapping; the individual IQSEC2 target record was not inspected. Retain the original curated edge with explicit curator deference, supported independently by the directly inspected IQSEC2-calmodulin experiments in PMID:30842726. No binary interface or CALM1-specific endogenous function is inferred from the screen. |
| GO:0000086 G2/M transition of mitotic cell cycle | IEA GO_REF:0000120 | UNDECIDED | Summary: The source transfers a mouse calmodulin G2/M-transition assertion, but its exact donor experiment has not been inspected. Reason: The source transfers a mouse calmodulin G2/M-transition assertion, but its exact donor experiment has not been inspected. The human CP110 evidence addresses late cytokinesis and does not by itself establish the distinct G2/M transition; neither a wrong ortholog nor a contradictory human function is established. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P0DP26 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP27 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP28 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0008076 voltage-gated potassium channel complex | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The orthology assertion agrees with direct Kv7.2/Kv7.3 calmodulin-complex structures and the curated potassium-channel interactions. Reason: The orthology assertion agrees with direct Kv7.2/Kv7.3 calmodulin-complex structures and the curated potassium-channel interactions. Retain this specific complex context while distinguishing the Kv7 structural constructs from a direct experiment on the original mouse donor. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P0DP26 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP28 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0016020 membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Membrane association is independently supported by target-bound calmodulin at plasma-membrane channels and receptors. Reason: Membrane association is independently supported by target-bound calmodulin at plasma-membrane channels and receptors. The broad orthology-derived membrane term is compatible with peripheral recruitment and does not assert that calmodulin is an integral membrane protein. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0031982 vesicle | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse-derived vesicle assertion is compatible with the curated human exosome-like-vesicle proteomic annotation and calmodulin-dependent vesicle-transport regulation. Reason: The mouse-derived vesicle assertion is compatible with the curated human exosome-like-vesicle proteomic annotation and calmodulin-dependent vesicle-transport regulation. Retain the contextual association without claiming an inspected individual proteomic target table or an active secretion mechanism. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0043209 myelin sheath | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The mouse orthology-derived myelin-sheath assertion agrees with the independently curated PAINT node and brain myelin-basic-protein interactions. Reason: The mouse orthology-derived myelin-sheath assertion agrees with the independently curated PAINT node and brain myelin-basic-protein interactions. It remains a specialized localization; binding to purified myelin basic protein alone is not treated as a new sheath-localization assay. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P0DP26 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP28 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0044305 calyx of Held | IEA GO_REF:0000120 | UNDECIDED | Summary: The exact mouse calyx-of-Held donor assay has not been accessed. Reason: The exact mouse calyx-of-Held donor assay has not been accessed. General neuronal calmodulin function does not establish this fine synaptic location, but absence of an inspected experiment is not evidence that the trusted source assertion is wrong. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P0DP26 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP27 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP28 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0048306 calcium-dependent protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: Calcium-dependent target binding is a genuine mechanism demonstrated with human titin fragments, CaMKII and conformationally constrained calmodulin mutants. Reason: Calcium-dependent target binding is a genuine mechanism demonstrated with human titin fragments, CaMKII and conformationally constrained calmodulin mutants. Retain the broad interaction property because it spans distinct targets; it is incorporated into the specific regulatory cores rather than a duplicate generic-binding core. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0050848 regulation of calcium-mediated signaling | IEA GO_REF:0000107 | ACCEPT | Summary: Calmodulin directly couples calcium binding to changes in kinase, phosphatase and channel activity. Reason: Calmodulin directly couples calcium binding to changes in kinase, phosphatase and channel activity. This provides target-specific support for the orthology-derived regulation of calcium-mediated signaling, without treating every downstream phenotype as a direct calmodulin process. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0097225 sperm midpiece | IEA GO_REF:0000107 | UNDECIDED | Summary: The mouse sperm-midpiece source annotation is preserved, but the exact donor localization evidence is uninspected. Reason: The mouse sperm-midpiece source annotation is preserved, but the exact donor localization evidence is uninspected. The human sperm-nucleus proteomic paper concerns a different compartment and cannot validate the midpiece assertion. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P0DP26 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0099523 presynaptic cytosol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: A presynaptic cytosolic pool is consistent with the conserved soluble calcium sensor and its neuronal target regulation. Reason: A presynaptic cytosolic pool is consistent with the conserved soluble calcium sensor and its neuronal target regulation. Retain the curated mouse-to-human localization as contextual, while acknowledging that the exact original donor localization experiment was not independently inspected. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0140238 presynaptic endocytosis | IEA GO_REF:0000120 | UNDECIDED | Summary: The original mouse presynaptic-endocytosis evidence was not inspected. Reason: The original mouse presynaptic-endocytosis evidence was not inspected. The available KIF1A study addresses dense-core-vesicle cargo binding and transport, not the distinct endocytic step, so it cannot fill that source-specific gap. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P0DP26 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP27 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. UniProtKB:P0DP28 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Supporting Evidence: |
| GO:0141110 transporter inhibitor activity | IEA GO_REF:0000107 | MODIFY | Summary: The broad transporter-inhibitor assertion can be refined to the directly demonstrated inhibition of calcium channels by calmodulin. Reason: The broad transporter-inhibitor assertion can be refined to the directly demonstrated inhibition of calcium channels by calmodulin. Human CaV1.2 inactivation and RyR2 inhibition provide target-specific corroboration, while the original mouse donor experiment remains uninspected. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB:P0DP27 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 SUPPORTS TRANSFER Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. Proposed replacements: calcium channel inhibitor activity |
| GO:1905913 negative regulation of calcium ion export across plasma membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact mouse-derived negative regulation of calcium export has not been traced to an inspected assay. Reason: The exact mouse-derived negative regulation of calcium export has not been traced to an inspected assay. Inhibition of calcium entry through CaV1.2 or release through RyR2 is not the same directional process as inhibiting export across the plasma membrane, so those experiments cannot substantiate this assertion. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P0DP27 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. ensembl:ENSMUSP00000105709 UNRESOLVED Literal source identifier preserved. Exact donor/rule experiment access and independent human corroboration are delimited in the reason; no source count or target-self circularity argument is used. |
| GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion | IDA PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The CALM1 variant study combines human arrhythmia genetics with altered calcium binding and RyR2-domain interaction. Reason: The CALM1 variant study combines human arrhythmia genetics with altered calcium binding and RyR2-domain interaction. Retain the curated regulation of cardiac contraction through calcium release, distinguishing protein-level mechanism from a direct contraction experiment not exposed in the cached abstract. |
| GO:1901844 regulation of cell communication by electrical coupling involved in cardiac conduction | IDA PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: Human CALM1 substitutions are associated with ventricular arrhythmia and disturbed calcium-sensor/channel coupling. Reason: Human CALM1 substitutions are associated with ventricular arrhythmia and disturbed calcium-sensor/channel coupling. Retain the curated electrical-coupling regulatory process with that evidence boundary; the abstract does not independently demonstrate a gap-junction mechanism. Supporting Evidence: |
| GO:0005246 calcium channel regulator activity | IDA PMID:20226167 Defective calmodulin binding to the cardiac ryanodine recept... | ACCEPT | Summary: In a mouse RyR2-R2474S model, altered calmodulin affinity accompanies abnormal calcium release, and added calmodulin attenuates calcium sparks. Reason: In a mouse RyR2-R2474S model, altered calmodulin affinity accompanies abnormal calcium release, and added calmodulin attenuates calcium sparks. This supports calmodulin channel regulation and its calcium-release/contraction consequences; the mutated molecule in that experiment is RyR2, not CALM1. Supporting Evidence: |
| GO:0010881 regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion | IDA PMID:20226167 Defective calmodulin binding to the cardiac ryanodine recept... | ACCEPT | Summary: In a mouse RyR2-R2474S model, altered calmodulin affinity accompanies abnormal calcium release, and added calmodulin attenuates calcium sparks. Reason: In a mouse RyR2-R2474S model, altered calmodulin affinity accompanies abnormal calcium release, and added calmodulin attenuates calcium sparks. This supports calmodulin channel regulation and its calcium-release/contraction consequences; the mutated molecule in that experiment is RyR2, not CALM1. Supporting Evidence: |
| GO:0060291 long-term synaptic potentiation | TAS PMID:20668654 Structure of the CaMKIIdelta/calmodulin complex reveals the ... | KEEP AS NON CORE | Summary: CaMKII activation provides a plausible regulatory contribution to long-term synaptic potentiation, and the cited structural paper discusses that established pathway. Reason: CaMKII activation provides a plausible regulatory contribution to long-term synaptic potentiation, and the cited structural paper discusses that established pathway. Its inspected experiments are purified human kinase/calmodulin structures and binding assays, not a new neuronal potentiation assay; retain the curated pathway assertion as contextual. Supporting Evidence: |
| GO:0097720 calcineurin-mediated signaling | IDA PMID:8631777 Blocking the Ca2+-induced conformational transitions in calm... | ACCEPT | Summary: The experiment uses engineered human liver calmodulin with intramolecular disulfides that restrict calcium-induced opening. Reason: The experiment uses engineered human liver calmodulin with intramolecular disulfides that restrict calcium-induced opening. Loss and chemical restoration of calcineurin activation directly support calmodulin phosphatase-activator function and its participation in calcineurin signaling, not phosphatase catalysis. Supporting Evidence: |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6786205 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The event identifies cytosolic CAMKMT as the enzyme that methylates calmodulin at the reported lysine. CALM1 is the methylation substrate; this does not confer methyltransferase activity on calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005515 protein binding | IPI PMID:11807546 Structural basis for the activation of anthrax adenylyl cycl... | MODIFY | Summary: Calmodulin directly activates anthrax edema-factor adenylate cyclase. Reason: PMID:11807546 reports structures of edema factor with and without calmodulin and an allosteric structural change stabilizing the active enzyme. This supports the specific activator activity in the host-pathogen biochemical context. The bacterial partner retains the cyclase catalytic activity; calmodulin provides activation. Only the complete cached abstract was available. Proposed replacements: adenylate cyclase activator activity Supporting Evidence: PMID:11807546 stabilizes a disordered loop and leads to enzyme activation |
| GO:0005515 protein binding | IPI PMID:11984006 The Chediak-Higashi protein interacts with SNARE complex and... | UNDECIDED | Summary: The source supports an interaction-screen framework, but the calmodulin-LYST target evidence remains unresolved. Reason: The complete PMID:11984006 abstract describes human LYST-fragment yeast two-hybrid screening and follow-up of selected partners, but does not identify the calmodulin target experiment. The accessible publisher preview did not supply that result and the primary full-text attempt failed. Preserve the original experimental assertion without declaring it wrong; the target-specific evidence and any more specific activity remain unresolved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19855925 Structural analysis of the complex between calmodulin and fu... | KEEP AS NON CORE | Summary: Retain the myelin-basic-protein interaction in its biochemical context. Reason: The complete PMID:19855925 abstract describes calmodulin-affinity capture of human brain myelin basic protein and structural/biophysical binding experiments with full-length protein and rodent peptides. Retain the exact curated partner P02687; the individual accession-to-assay mapping and full Methods were not independently inspected. The official 2010 correction replaces Figure 5 panels and corrects the circular-dichroism axis unit; its prose was read, but corrected images were not reanalysed. This supports bounded binding without a separate enzyme-regulatory claim. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27564677 Structural Insights into the M-Channel Proximal C-Terminus/C... | MODIFY | Summary: Calmodulin binds the Kv7.2/Kv7.3 channel cytoplasmic domains. Reason: The complete PMID:27564677 abstract directly reports a 1:1 calmodulin complex with a chimeric Kv7.3/Kv7.2 proximal C-terminal region and a high-resolution structure. The specific binding category is transmembrane transporter binding. Preserve the exact O43525 source partner; the chimeric structural and electrophysiological evidence does not imply that every physiological property was tested independently for each native channel. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0043539 protein serine/threonine kinase activator activity | IDA PMID:35568036 A family of conserved bacterial virulence factors dampens in... | ACCEPT | Summary: The OspC study measures reduced CaMKII phosphorylation and calmodulin association after bacterial-effector expression, and constitutively active CaMKII bypasses the IFN inhibition. Reason: The OspC study measures reduced CaMKII phosphorylation and calmodulin association after bacterial-effector expression, and constitutively active CaMKII bypasses the IFN inhibition. This supports the calmodulin-activator mechanism in human cell systems, independently established by human CaMKII/calmodulin structural work; the paper is not Reactome evidence. Supporting Evidence: PMID:14722083 binding, substrate phosphorylation, and autophosphorylation |
| GO:0005509 calcium ion binding | IDA PMID:35568036 A family of conserved bacterial virulence factors dampens in... | ACCEPT | Summary: The OspC study distinguishes apo-calmodulin binding in EDTA from calcium-containing conditions and calcium-dependent downstream signaling. Reason: The OspC study distinguishes apo-calmodulin binding in EDTA from calcium-containing conditions and calcium-dependent downstream signaling. The intrinsic calcium-binding activity is independently established by direct human protein measurements; this retained IDA row is not relabeled as pathway-database evidence. |
| GO:0035458 cellular response to interferon-beta | IDA PMID:35568036 A family of conserved bacterial virulence factors dampens in... | KEEP AS NON CORE | Summary: Human HeLa and HEK293T experiments show that calmodulin depletion or inhibition reduces IFN-responsive expression and STAT1 activation, while active CaMKII bypasses OspC inhibition. Reason: Human HeLa and HEK293T experiments show that calmodulin depletion or inhibition reduces IFN-responsive expression and STAT1 activation, while active CaMKII bypasses OspC inhibition. Retain this experimentally supported immune-signaling context, without claiming that calmodulin itself phosphorylates STAT1 or that the shared-protein depletion isolates CALM1 gene-specific effects. Supporting Evidence: PMID:35568036 blocking CaM kinase II and downstream JAK/STAT signaling |
| GO:0043539 protein serine/threonine kinase activator activity | IDA PMID:14722083 Comparative analyses of the three-dimensional structures and... | ACCEPT | Summary: The primary study compares human CaMKII isozyme structures and enzymatic properties, including calmodulin-dependent activation. Reason: The primary study compares human CaMKII isozyme structures and enzymatic properties, including calmodulin-dependent activation. This supports the activator activity directly; it is distinct from the kinase reaction performed by CaMKII. |
| GO:0046427 positive regulation of receptor signaling pathway via JAK-STAT | IDA PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphoryla... | KEEP AS NON CORE | Summary: The cached Results show calcium/calmodulin-dependent kinase activity toward STAT1, together with IFN-gamma responses in NIH3T3 and human U3A systems. Reason: The cached Results show calcium/calmodulin-dependent kinase activity toward STAT1, together with IFN-gamma responses in NIH3T3 and human U3A systems. Retain the curated calmodulin contribution to this signaling context; CaMKII performs phosphorylation and the paper does not isolate a CALM1-specific transcriptional effect. Supporting Evidence: |
| GO:0046427 positive regulation of receptor signaling pathway via JAK-STAT | IDA PMID:35568036 A family of conserved bacterial virulence factors dampens in... | KEEP AS NON CORE | Summary: Human HeLa and HEK293T experiments show that calmodulin depletion or inhibition reduces IFN-responsive expression and STAT1 activation, while active CaMKII bypasses OspC inhibition. Reason: Human HeLa and HEK293T experiments show that calmodulin depletion or inhibition reduces IFN-responsive expression and STAT1 activation, while active CaMKII bypasses OspC inhibition. Retain this experimentally supported immune-signaling context, without claiming that calmodulin itself phosphorylates STAT1 or that the shared-protein depletion isolates CALM1 gene-specific effects. Supporting Evidence: |
| GO:0071346 cellular response to type II interferon | IDA PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphoryla... | KEEP AS NON CORE | Summary: The cached Results show calcium/calmodulin-dependent kinase activity toward STAT1, together with IFN-gamma responses in NIH3T3 and human U3A systems. Reason: The cached Results show calcium/calmodulin-dependent kinase activity toward STAT1, together with IFN-gamma responses in NIH3T3 and human U3A systems. Retain the curated calmodulin contribution to this signaling context; CaMKII performs phosphorylation and the paper does not isolate a CALM1-specific transcriptional effect. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28890335 The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates ... | KEEP AS NON CORE | Summary: Retain PIK3C3 association in the calcium-dependent autophagy-regulatory context. Reason: The complete PMID:28890335 abstract establishes the VMP1/SERCA/calmodulin framework, and the canonical calmodulin UniProt SUBUNIT entry explicitly reports PIK3C3 association and kinase modulation. Retain the exact curated PIK3C3 binding assertion with curator deference. The source-specific PIK3C3 experiment was not independently inspected, so no purified direct interface or finer catalytic-regulatory claim is asserted. |
| GO:0016240 autophagosome membrane docking | IDA PMID:28890335 The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates ... | KEEP AS NON CORE | Summary: The primary abstract explicitly identifies calmodulin as a sensor/effector modulating VMP1/SERCA-dependent ER contacts, supporting a regulatory contribution to these organelle-contact processes. Reason: The primary abstract explicitly identifies calmodulin as a sensor/effector modulating VMP1/SERCA-dependent ER contacts, supporting a regulatory contribution to these organelle-contact processes. The detailed experiments are unavailable in the canonical cache, and calmodulin is not assigned the physical tether or SERCA ATPase activity; retain the trusted IDA context with that limit. Supporting Evidence: |
| GO:0140056 organelle localization by membrane tethering | IDA PMID:28890335 The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates ... | KEEP AS NON CORE | Summary: The primary abstract explicitly identifies calmodulin as a sensor/effector modulating VMP1/SERCA-dependent ER contacts, supporting a regulatory contribution to these organelle-contact processes. Reason: The primary abstract explicitly identifies calmodulin as a sensor/effector modulating VMP1/SERCA-dependent ER contacts, supporting a regulatory contribution to these organelle-contact processes. The detailed experiments are unavailable in the canonical cache, and calmodulin is not assigned the physical tether or SERCA ATPase activity; retain the trusted IDA context with that limit. Supporting Evidence: |
| GO:1990456 mitochondrion-endoplasmic reticulum membrane tethering | IDA PMID:28890335 The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates ... | KEEP AS NON CORE | Summary: The primary abstract explicitly identifies calmodulin as a sensor/effector modulating VMP1/SERCA-dependent ER contacts, supporting a regulatory contribution to these organelle-contact processes. Reason: The primary abstract explicitly identifies calmodulin as a sensor/effector modulating VMP1/SERCA-dependent ER contacts, supporting a regulatory contribution to these organelle-contact processes. The detailed experiments are unavailable in the canonical cache, and calmodulin is not assigned the physical tether or SERCA ATPase activity; retain the trusted IDA context with that limit. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:31454269 Genetic Mosaicism in Calmodulinopathy. | ACCEPT | Summary: The study directly measures impaired C-domain calcium affinity of recombinant E141V and E141K calmodulin proteins. Reason: The study directly measures impaired C-domain calcium affinity of recombinant E141V and E141K calmodulin proteins. CALM1-E141V and CALM3-E141K are distinct genetic observations despite their shared wild-type protein sequence; the two mosaic pedigrees in this paper involve CALM3. Supporting Evidence: |
| GO:0098901 regulation of cardiac muscle cell action potential | IMP PMID:31454269 Genetic Mosaicism in Calmodulinopathy. | ACCEPT | Summary: Human iPSC-derived cardiomyocytes overexpressing wild-type or E141 mutant calmodulin show altered L-type-channel calcium-dependent inactivation and action-potential duration. Reason: Human iPSC-derived cardiomyocytes overexpressing wild-type or E141 mutant calmodulin show altered L-type-channel calcium-dependent inactivation and action-potential duration. This directly supports the protein regulatory function; full supplemental Methods were not available and CALM3 mosaicism is not attributed to CALM1. Supporting Evidence: |
| GO:1901842 negative regulation of high voltage-gated calcium channel activity | IMP PMID:31454269 Genetic Mosaicism in Calmodulinopathy. | ACCEPT | Summary: Human iPSC-derived cardiomyocytes overexpressing wild-type or E141 mutant calmodulin show altered L-type-channel calcium-dependent inactivation and action-potential duration. Reason: Human iPSC-derived cardiomyocytes overexpressing wild-type or E141 mutant calmodulin show altered L-type-channel calcium-dependent inactivation and action-potential duration. This directly supports the protein regulatory function; full supplemental Methods were not available and CALM3 mosaicism is not attributed to CALM1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30021165 Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca(... | MODIFY | Summary: Direct KIF1A binding supports kinesin binding. Reason: Selected PMID:30021165 Results and Methods show tagged calmodulin association with KIF1A fragments, calcium sensitivity and loss of binding after mutation of a mapped hydrophobic motif. The Methods identify rat KIF1A variant-2 constructs and rat neuronal cultures; the HEK293 expression assays and this provenance are kept distinct. Preserve the literal F1M4A4 partner. Calmodulin is the kinesin-binding regulator, not the motor. Proposed replacements: kinesin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30287853 Calcineurin B homologous protein 3 binds with high affinity ... | MODIFY | Summary: Calmodulin directly binds the NHE1 cytoplasmic domain. Reason: The actual PMID:30287853 Methods describe human calmodulin and human NHE1 C-terminal constructs, and Results show calcium-dependent complex formation by size-exclusion chromatography with loss after EGTA treatment. This supports transmembrane transporter binding despite the title foregrounding CHP3. It does not by itself establish the direction of NHE1 transport regulation. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0010856 adenylate cyclase activator activity | IDA PMID:11807546 Structural basis for the activation of anthrax adenylyl cycl... | KEEP AS NON CORE | Summary: The primary structure demonstrates activation of the anthrax edema-factor adenylate cyclase by calmodulin. Reason: The primary structure demonstrates activation of the anthrax edema-factor adenylate cyclase by calmodulin. This is genuine calmodulin activator activity in a microbial-toxin context, not proof of mammalian GPCR-linked cyclase activation. Supporting Evidence: |
| GO:0034704 calcium channel complex | IDA PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The paper reports calmodulin interaction with a RyR2 calmodulin-binding-domain peptide and altered binding of a CALM1 variant. Reason: The paper reports calmodulin interaction with a RyR2 calmodulin-binding-domain peptide and altered binding of a CALM1 variant. Independent RyR2-directed FRET corroborates association with the channel assembly; the isolated peptide experiment is not described as a resolved intact complex. |
| GO:0000922 spindle pole | IDA PMID:16760425 CP110 cooperates with two calcium-binding proteins to regula... | KEEP AS NON CORE | Summary: The curated IDA localization is consistent with UniProt mitotic spindle-pole and spindle-microtubule redistribution, and with the CP110/calmodulin association study. Reason: The curated IDA localization is consistent with UniProt mitotic spindle-pole and spindle-microtubule redistribution, and with the CP110/calmodulin association study. The complete localization figure is absent from the selected cached narrative, so retain the trusted source resolution without claiming a newly inspected image. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10692436 Ca(2+)-dependent and Ca(2+)-independent calmodulin binding s... | MODIFY | Summary: Binding to erythrocyte protein 4.1R supports cytoskeletal protein binding. Reason: The complete PMID:10692436 abstract reports calmodulin binding to protein 4.1R, mapping two binding sites by peptide/deletion analysis and measuring their effects on association with band 3. Protein 4.1R is the membrane-cytoskeletal partner. This supports cytoskeletal protein binding without transferring the partner structural activity to calmodulin; full Methods were unavailable. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15140941 Ca2+-binding protein-1 facilitates and forms a postsynaptic ... | MODIFY | Summary: Direct CaV1.2 association supports transmembrane transporter binding. Reason: The complete PMID:15140941 abstract and accessible Methods/Discussion support competitive calmodulin association with the channel C terminus and calmodulin-dependent inactivation. The Methods use rat rbcII channel constructs in HEK293T cells and commercial calmodulin; the cache omits the central Results despite its full-text flag. Refine the interaction to transporter binding while retaining the source partner Q13936. Channel inhibition is relevant biological context, but the pore activity belongs to the channel and the source is not a CALM1-specific human physiological assay. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15632291 Myristoyl moiety of HIV Nef is involved in regulation of the... | KEEP AS NON CORE | Summary: Retain the direct HIV-1 Nef interaction. Reason: The complete PMID:15632291 abstract explicitly reports cellular co-immunoprecipitation, recombinant GST-Nef pull-down and binding of Nef peptides to calmodulin, with myristoylation affecting binding. The actual cached body supplies Introduction/Discussion rather than complete Methods/Results. Retain this viral-partner interaction as non-core without inferring a separate calmodulin catalytic activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16760425 CP110 cooperates with two calcium-binding proteins to regula... | KEEP AS NON CORE | Summary: Retain the direct CP110 interaction within a centrosomal protein assembly. Reason: PMID:16760425 abstract and accessible Discussion distinguish direct calmodulin-CP110 association from an indirect centrin interaction. Binding-defective CP110 mutants inform the functional context, but do not independently establish a more specific adaptor or catalytic activity of calmodulin. Retain the exact O43303 edge; selected Discussion was read, not all primary assay figures. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21299499 IQ-motif selectivity in human IQGAP2 and IQGAP3: binding of ... | KEEP AS NON CORE | Summary: Retain calmodulin binding to IQGAP2 IQ motifs. Reason: Selected PMID:21299499 Methods and Results describe recombinant human calmodulin and IQGAP2-derived IQ peptides, with calcium-dependent mobility-shift binding assays. These establish the peptide-binding interaction and support the curated full-protein edge. Preserve the original partner; motif-peptide affinities do not establish the affinity or regulatory direction of every intact cellular complex, or confer GTPase activity on calmodulin. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:3111527 Comparison of S100b protein with calmodulin: interactions wi... | UNDECIDED | Summary: The original calmodulin-tau assay remains unresolved in the available source. Reason: The canonical PMID:3111527 abstract is explicitly truncated and primarily describes S100b/melittin interactions. The target calmodulin-tau experiment was not recovered from the publisher. Preserve the curator experimental assertion without a wrong-protein claim; the available source does not support a confident refinement or removal. An independently indexed later tau-calmodulin paper was only an uncached lead and is not used as YAML support. Supporting Evidence: |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | KEEP AS NON CORE | Summary: The primary abstract describes proteomics of purified human sperm nuclei, matching the curated nuclear association. Reason: The primary abstract describes proteomics of purified human sperm nuclei, matching the curated nuclear association. The individual calmodulin peptide assignment was not inspected, and shared calmodulin peptides do not establish CALM1-specific nuclear expression. Supporting Evidence: |
| GO:0005737 cytoplasm | TAS PMID:10899953 Calmodulin regulation of basal and agonist-stimulated G prot... | ACCEPT | Summary: The human mu-opioid-receptor study describes direct calmodulin interaction with the receptor intracellular loop and movement from the plasma membrane on receptor activation in HEK293 cells. Reason: The human mu-opioid-receptor study describes direct calmodulin interaction with the receptor intracellular loop and movement from the plasma membrane on receptor activation in HEK293 cells. Retain the cytoplasmic and peripheral plasma-membrane pools, without assigning membrane-spanning topology. Supporting Evidence: PMID:10899953 CaM release from plasma membranes |
| GO:0005813 centrosome | IDA PMID:16760425 CP110 cooperates with two calcium-binding proteins to regula... | KEEP AS NON CORE | Summary: The curated IDA localization is consistent with UniProt mitotic spindle-pole and spindle-microtubule redistribution, and with the CP110/calmodulin association study. Reason: The curated IDA localization is consistent with UniProt mitotic spindle-pole and spindle-microtubule redistribution, and with the CP110/calmodulin association study. The complete localization figure is absent from the selected cached narrative, so retain the trusted source resolution without claiming a newly inspected image. Supporting Evidence: |
| GO:0005876 spindle microtubule | IDA PMID:16760425 CP110 cooperates with two calcium-binding proteins to regula... | KEEP AS NON CORE | Summary: The curated IDA localization is consistent with UniProt mitotic spindle-pole and spindle-microtubule redistribution, and with the CP110/calmodulin association study. Reason: The curated IDA localization is consistent with UniProt mitotic spindle-pole and spindle-microtubule redistribution, and with the CP110/calmodulin association study. The complete localization figure is absent from the selected cached narrative, so retain the trusted source resolution without claiming a newly inspected image. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS PMID:10899953 Calmodulin regulation of basal and agonist-stimulated G prot... | ACCEPT | Summary: The human mu-opioid-receptor study describes direct calmodulin interaction with the receptor intracellular loop and movement from the plasma membrane on receptor activation in HEK293 cells. Reason: The human mu-opioid-receptor study describes direct calmodulin interaction with the receptor intracellular loop and movement from the plasma membrane on receptor activation in HEK293 cells. Retain the cytoplasmic and peripheral plasma-membrane pools, without assigning membrane-spanning topology. Supporting Evidence: |
| GO:0007186 G protein-coupled receptor signaling pathway | TAS PMID:10899953 Calmodulin regulation of basal and agonist-stimulated G prot... | KEEP AS NON CORE | Summary: The human mu-opioid-receptor experiments identify calmodulin as a direct receptor-associated regulator of basal G-protein coupling. Reason: The human mu-opioid-receptor experiments identify calmodulin as a direct receptor-associated regulator of basal G-protein coupling. Retain this GPCR signaling context separately from activation of bacterial edema-factor adenylate cyclase; the latter is not evidence for this process. Supporting Evidence: |
| GO:0021762 substantia nigra development | HEP PMID:22926577 Quantitative proteomic analysis of human substantia nigra in... | UNDECIDED | Summary: The accessible abstract describes proteomic characterization of adult human substantia nigra, but does not establish a developmental role for calmodulin. Reason: The accessible abstract describes proteomic characterization of adult human substantia nigra, but does not establish a developmental role for calmodulin. The relevant full experiment and individual target evidence were not accessed; this limitation warrants uncertainty rather than rejection of the curated experimental assertion from its title. Supporting Evidence: |
| GO:0031982 vesicle | HDA PMID:19190083 Characterization of exosome-like vesicles released from huma... | KEEP AS NON CORE | Summary: The study reports proteomic analysis of exosome-like vesicles from human airway epithelia, consistent with the curated vesicle association. Reason: The study reports proteomic analysis of exosome-like vesicles from human airway epithelia, consistent with the curated vesicle association. The individual calmodulin entry and vesicle-loading mechanism were not inspected; no active secretion or dedicated extracellular function is inferred. Supporting Evidence: |
| GO:0032465 regulation of cytokinesis | IMP PMID:16760425 CP110 cooperates with two calcium-binding proteins to regula... | KEEP AS NON CORE | Summary: The CP110 study combines direct calmodulin binding with a binding-defective CP110 mutant that disrupts late cytokinesis. Reason: The CP110 study combines direct calmodulin binding with a binding-defective CP110 mutant that disrupts late cytokinesis. This supports a functional regulatory contribution beyond mere depletion, while the precise downstream machinery remains unresolved and the role is contextual. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:11807546 Structural basis for the activation of anthrax adenylyl cycl... | ACCEPT | Summary: The calmodulin/edema-factor structure provides direct calcium-bound calmodulin evidence. Reason: The calmodulin/edema-factor structure provides direct calcium-bound calmodulin evidence. Calcium binding belongs to calmodulin, whereas adenylate cyclase catalysis belongs to the bacterial partner. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:19855925 Structural analysis of the complex between calmodulin and fu... | KEEP AS NON CORE | Summary: The source directly studies complexes between calmodulin and myelin-basic-protein constructs. Reason: The source directly studies complexes between calmodulin and myelin-basic-protein constructs. Retain the broad complex association without treating every transient complex as a distinct core function or inventing a more specific complex identifier. Supporting Evidence: |
| GO:1902494 catalytic complex | IDA PMID:11807546 Structural basis for the activation of anthrax adenylyl cycl... | KEEP AS NON CORE | Summary: The edema-factor/calmodulin structure places calmodulin in a catalytic assembly as the regulatory partner. Reason: The edema-factor/calmodulin structure places calmodulin in a catalytic assembly as the regulatory partner. Retain this microbial-toxin complex context; it does not make calmodulin catalytic or establish a mammalian GPCR pathway. Supporting Evidence: |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-482772 | KEEP AS NON CORE | Summary: Retain context-limited extracellular calmodulin presence after platelet activation. Reason: Platelet stimulation releases non-granular cytosolic proteins. The narrative explicitly allows a contribution from platelet lysis and does not expose a CALM1-specific detection assay. Extracellular presence does not establish active calmodulin secretion or a specialized extracellular molecular function. Retain the curated extracellular-location assertion as non-core with this release/lysis boundary; do not elevate it to a constitutive secretory localization or a demonstrated extracellular effector mechanism. Supporting Evidence: Reactome:R-HSA-482772 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-111915 | ACCEPT | Summary: Retain calmodulin in the curated nuclear regulatory-complex pool. Reason: Calmodulin binding and CAMKK-dependent T200 phosphorylation precede CAMK4 autophosphorylation at N-terminal sites. The summary does not independently document a nuclear localization assay. The kinase chemistry belongs to CAMK4/CAMKK, not calmodulin. The existing nucleoplasm assertion is retained with curator deference and corroboration from CaM-containing NFAT complexes entering the nucleus. This is not an assertion that calmodulin itself catalyses phosphorylation or directly binds DNA. Supporting Evidence: Reactome:R-HSA-111915 Reactome:R-HSA-2730867 Reactome:R-HSA-4551465 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2730867 | ACCEPT | Summary: Retain calmodulin in the curated nuclear regulatory-complex pool. Reason: The event title explicitly includes CaM in the calcineurin:calmodulin:NFAT complex translocating to the nucleus. The narrative describes dephosphorylated NFAT-calcineurin nuclear translocation and transcriptional activation, supporting the curated nuclear pool without demonstrating CALM1 locus specificity. The existing nucleoplasm assertion is retained with curator deference and corroboration from CaM-containing NFAT complexes entering the nucleus. This is not an assertion that calmodulin itself catalyses phosphorylation or directly binds DNA. Supporting Evidence: Reactome:R-HSA-2730867 Reactome:R-HSA-4551465 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-442749 | ACCEPT | Summary: Retain the supported nucleoplasmic calmodulin pool while distinguishing uncertainty about the original CaMKK reaction. Reason: The located_in annotation asserts that calmodulin can occupy the nucleoplasm, not that this particular CaMKK reaction was localized there. Independent human Reactome R-HSA-2730867 and R-HSA-4551465 explicitly name CaM-containing calcineurin:NFAT complexes translocating to the nucleus, supporting the curated nuclear pool. The original R-HSA-442749 narrative leaves CaMKK autophosphorylation in the cytosol, nucleus or both because CaMKK localization is uncertain. It does not independently establish a nuclear localization assay for this reaction. The linked primary localization experiments and structured participant graph were not inspected. Accepting the independently corroborated target location does not resolve that event-specific compartment or establish CALM1-locus specificity for the shared calmodulin protein. Supporting Evidence: Reactome:R-HSA-442749 Reactome:R-HSA-2730867 Reactome:R-HSA-4551465 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4551465 | ACCEPT | Summary: Retain calmodulin in the curated nuclear regulatory-complex pool. Reason: The title identifies NFATC1:calcineurin:CaM translocation to the nucleus; the narrative describes NFAT-calcineurin nuclear translocation. This supports the curated nuclear complex pool, not an intrinsic DNA-binding or phosphatase activity of calmodulin. The existing nucleoplasm assertion is retained with curator deference and corroboration from CaM-containing NFAT complexes entering the nucleus. This is not an assertion that calmodulin itself catalyses phosphorylation or directly binds DNA. Supporting Evidence: Reactome:R-HSA-4551465 Reactome:R-HSA-2730867 |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-9618916 | ACCEPT | Summary: Retain the supported nucleoplasmic calmodulin pool while distinguishing uncertainty about the original CaMKK reaction. Reason: The located_in annotation asserts that calmodulin can occupy the nucleoplasm, not that this particular CaMKK reaction was localized there. Independent human Reactome R-HSA-2730867 and R-HSA-4551465 explicitly name CaM-containing calcineurin:NFAT complexes translocating to the nucleus, supporting the curated nuclear pool. The original R-NUL-9618916 experiment combines recombinant mouse Camkk1 with recombinant human calmodulin. Its narrative leaves the cytosolic versus nuclear reaction compartment unresolved; that mixed-species binding experiment is not a human nuclear localization assay. The linked primary localization experiments and structured participant graph were not inspected. Accepting the independently corroborated target location does not resolve that event-specific compartment or establish CALM1-locus specificity for the shared calmodulin protein. Supporting Evidence: Reactome:R-NUL-9618916 Reactome:R-HSA-2730867 Reactome:R-HSA-4551465 |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-9619177 | ACCEPT | Summary: Retain the supported nucleoplasmic calmodulin pool while distinguishing uncertainty about the original CaMKK reaction. Reason: The located_in annotation asserts that calmodulin can occupy the nucleoplasm, not that this particular CaMKK reaction was localized there. Independent human Reactome R-HSA-2730867 and R-HSA-4551465 explicitly name CaM-containing calcineurin:NFAT complexes translocating to the nucleus, supporting the curated nuclear pool. The original R-NUL-9619177 experiment combines rat Camkk2, human CAMK4 and recombinant calmodulin. The source assumes human calmodulin from sequence conservation rather than independently establishing its identity, and does not describe a nuclear localization assay. The linked primary localization experiments and structured participant graph were not inspected. Accepting the independently corroborated target location does not resolve that event-specific compartment or establish CALM1-locus specificity for the shared calmodulin protein. Supporting Evidence: Reactome:R-NUL-9619177 Reactome:R-HSA-2730867 Reactome:R-HSA-4551465 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202110 | ACCEPT | Summary: Retain a peripheral plasma-membrane-associated calmodulin pool. Reason: Calmodulin binds the eNOS:CAV1 complex and relieves CAV1 inhibition before dissociation. This is calmodulin regulation of the NOS complex, not nitric-oxide synthesis by calmodulin. The cached summary does not expose a structured compartment field. The curated plasma-membrane location is retained for the associated regulatory complex, with corroboration from the CaM-containing eNOS/CAV1/HSP90 events. No integral-membrane topology or independently inspected localization assay is asserted. Supporting Evidence: Reactome:R-HSA-202110 Reactome:R-HSA-202129 Reactome:R-HSA-202144 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202111 | ACCEPT | Summary: Retain a peripheral plasma-membrane-associated calmodulin pool. Reason: AKT1 phosphorylates eNOS at S1177 using HSP90 as a scaffold. The summary emphasizes AKT1/eNOS and does not independently identify calmodulin localization; the adjacent calmodulin-binding eNOS events provide the regulatory-complex context. The curated plasma-membrane location is retained for the associated regulatory complex, with corroboration from the CaM-containing eNOS/CAV1/HSP90 events. No integral-membrane topology or independently inspected localization assay is asserted. Supporting Evidence: Reactome:R-HSA-202111 Reactome:R-HSA-202110 Reactome:R-HSA-202129 Reactome:R-HSA-202144 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202129 | ACCEPT | Summary: Retain a peripheral plasma-membrane-associated calmodulin pool. Reason: HSP90 binds the eNOS:CAV1:CaM complex and promotes displacement of CAV1 by calmodulin. This documents CaM in the regulatory complex; a plasma-membrane compartment is supplied by the curated GOA assertion rather than a structured field in this cache. The curated plasma-membrane location is retained for the associated regulatory complex, with corroboration from the CaM-containing eNOS/CAV1/HSP90 events. No integral-membrane topology or independently inspected localization assay is asserted. Supporting Evidence: Reactome:R-HSA-202129 Reactome:R-HSA-202110 Reactome:R-HSA-202144 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202137 | ACCEPT | Summary: Retain a peripheral plasma-membrane-associated calmodulin pool. Reason: AKT1 is recruited to the eNOS complex through the HSP90 middle domain. CaM is not separately discussed in the summary; its complex membership is corroborated by the adjacent eNOS:CAV1:CaM and eNOS:CaM:HSP90 events. The curated plasma-membrane location is retained for the associated regulatory complex, with corroboration from the CaM-containing eNOS/CAV1/HSP90 events. No integral-membrane topology or independently inspected localization assay is asserted. Supporting Evidence: Reactome:R-HSA-202137 Reactome:R-HSA-202110 Reactome:R-HSA-202129 Reactome:R-HSA-202144 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202144 | ACCEPT | Summary: Retain a peripheral plasma-membrane-associated calmodulin pool. Reason: HSP90 facilitates calmodulin-mediated displacement of CAV1 from the eNOS:CaM:HSP90 complex. The event supports a peripheral regulatory association, not an integral-membrane topology for calmodulin. The curated plasma-membrane location is retained for the associated regulatory complex, with corroboration from the CaM-containing eNOS/CAV1/HSP90 events. No integral-membrane topology or independently inspected localization assay is asserted. Supporting Evidence: Reactome:R-HSA-202144 Reactome:R-HSA-202110 Reactome:R-HSA-202129 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5626549 | ACCEPT | Summary: Retain a peripheral plasma-membrane-associated calmodulin pool. Reason: The summary describes calcium-dependent binding of calmodulin to IQ repeats in IQGAP1/2/3 and inhibition of IQGAP association with F-actin. It does not expose a localization assay or structured compartment field; it does not support the historical nuclear-NFAT quotation attached to this plasma-membrane row. The curated plasma-membrane location is retained for the associated regulatory complex, with corroboration from the CaM-containing eNOS/CAV1/HSP90 events. No integral-membrane topology or independently inspected localization assay is asserted. The prior supporting quotation about NFAT nuclear translocation is not evidence for this IQGAP/plasma-membrane assertion and is omitted. Supporting Evidence: Reactome:R-HSA-5626549 Reactome:R-HSA-202110 Reactome:R-HSA-202129 Reactome:R-HSA-202144 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-111966 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Ca2+-bound calmodulin binds and inhibits GRK2; PKC phosphorylation can abolish this inhibition. Calmodulin is a regulator, not the kinase in this event. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-111966 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1497784 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes BH4-dependent electron transfer within eNOS and does not separately discuss calmodulin. Calmodulin-containing eNOS complex context is supported by adjacent events; no NOS redox chemistry is assigned to calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-1497784 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1497796 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes competition of BH2 with BH4 and eNOS uncoupling, without a calmodulin-specific assay. This supports pathway context only, not redox activity of calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-1497796 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1497810 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes superoxide production by uncoupled eNOS and does not separately assay calmodulin. Calmodulin remains a complex regulator; it is not the superoxide-producing catalyst. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-1497810 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1855153 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The event title places IP3 phosphorylation by ITPKA/B/C in the cytosol. The cached narrative does not give a calmodulin-specific localization experiment. ITPK proteins, not calmodulin, catalyse the phosphorylation. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-1855153 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202110 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calmodulin binds the eNOS:CAV1 complex and relieves CAV1 inhibition before dissociation. This is calmodulin regulation of the NOS complex, not nitric-oxide synthesis by calmodulin. The cached summary does not expose a structured compartment field. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-202110 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202111 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: AKT1 phosphorylates eNOS at S1177 using HSP90 as a scaffold. The summary emphasizes AKT1/eNOS and does not independently identify calmodulin localization; the adjacent calmodulin-binding eNOS events provide the regulatory-complex context. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-202111 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202127 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The event describes NOS-mediated NO synthesis and BH4 requirements. The summary does not separately assay calmodulin; the neighboring CaM-containing eNOS events supply the regulatory context. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-202127 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202129 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: HSP90 binds the eNOS:CAV1:CaM complex and promotes displacement of CAV1 by calmodulin. This documents CaM in the regulatory complex; a plasma-membrane compartment is supplied by the curated GOA assertion rather than a structured field in this cache. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-202129 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2025890 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calcium and calmodulin activate calcineurin, which binds NFAT. The source notes mouse B-cell experiments and an inferred calcineurin subunit composition; the human header does not convert every supporting experiment into a direct human assay. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-2025890 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730849 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calcineurin dephosphorylates cytoplasmic NFAT before nuclear translocation. The neighboring activation event explicitly supplies the calmodulin regulatory interaction; calmodulin is not the phosphatase. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-2730849 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730867 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The event title explicitly includes CaM in the calcineurin:calmodulin:NFAT complex translocating to the nucleus. The narrative describes dephosphorylated NFAT-calcineurin nuclear translocation and transcriptional activation, supporting the curated nuclear pool without demonstrating CALM1 locus specificity. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-2730867 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730872 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Activated calmodulin binds the calcineurin regulatory domain, releases autoinhibition and activates the phosphatase. This is direct regulatory binding rather than intrinsic calmodulin phosphatase chemistry. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-2730872 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3229181 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Ca2+-calmodulin binds the CNG-channel beta subunit and lowers affinity for cGMP. Calmodulin is a channel-associated regulator, not the channel pore or a cGMP-processing enzyme. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-3229181 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4332358 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calmodulin dissociation permits CAMK2 T305/T306 autophosphorylation, which prevents calmodulin rebinding. Dissociated calmodulin and CAMK2 kinase activity must not be conflated. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-4332358 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4332359 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Activated calmodulin binds CAMK2 and displaces its inhibitory segment, enabling CAMK2 autophosphorylation. The narrative also discusses oncogenic KRAS4B interference with CaM/CAMK2 signaling; it does not assign kinase activity to CaM. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-4332359 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4332363 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes CAMK2 T286 autophosphorylation after calmodulin binding. The catalytic activity belongs to CAMK2; calmodulin supplies calcium-dependent regulation. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-4332363 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-445797 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calcium-activated calmodulin binds and activates MYLK. This is regulatory association of calmodulin with the kinase, not calmodulin-mediated phosphorylation. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-445797 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-445813 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes MYLK-dependent phosphorylation of myosin light chains. The adjacent MYLK-calmodulin binding event establishes the regulator context; the cache does not independently assay calmodulin localization. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-445813 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-451283 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The event describes glutamate binding the extracellular N-terminal region of kainate receptors; calmodulin is not independently discussed in the summary. The CALM1 GOA row is cytosol and does not transfer receptor glutamate-binding activity or extracellular topology to calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-451283 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-451311 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes calcium-permeable, Q/R-unedited kainate receptors and does not expose the calmodulin participant or localization experiment. The broad cytosolic CALM1 assertion can be assessed independently of this thin event narrative. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-451311 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4551451 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The source describes WNT/calcium-dependent calcineurin/NFAT signaling using Xenopus, mouse F9 and human mammary-cell evidence. Calcineurin performs NFAT dephosphorylation; these mixed-system results are not a CALM1 locus-specific human assay. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-4551451 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4551465 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The title identifies NFATC1:calcineurin:CaM translocation to the nucleus; the narrative describes NFAT-calcineurin nuclear translocation. This supports the curated nuclear complex pool, not an intrinsic DNA-binding or phosphatase activity of calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-4551465 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-482772 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Platelet stimulation releases non-granular cytosolic proteins. The narrative explicitly allows a contribution from platelet lysis and does not expose a CALM1-specific detection assay. Extracellular presence does not establish active calmodulin secretion or a specialized extracellular molecular function. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-482772 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary describes RAS GEF-mediated GDP/GTP exchange and membrane-localized RAS without separately detailing calmodulin. The related Rasgrf1 event supplies CaM cofactor context; RAS nucleotide exchange remains GEF activity. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-5672965 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-71541 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The narrative explicitly describes a cytosolic phosphorylase-kinase complex containing PHKA1, PHKB, PHKG1 and CALM. Human PYGM oligomeric behavior is inferred from rabbit studies. Calmodulin is a regulatory subunit, not the phosphorylase-kinase catalytic subunit. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-71541 Reactome:R-HSA-6786205 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-71588 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The narrative explicitly describes a cytosolic phosphorylase-kinase complex containing PHKA2, PHKB, PHKG2 and CALM. The source includes cross-species inference about glycogen phosphorylase behavior; CALM is the regulatory component. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-71588 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9618785 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Apo-calmodulin binds neurogranin in a dynamic dendritic-spine pool; the summary discusses diffusion, calcium sensitivity and mouse Nrgn-loss phenotypes. These results do not distinguish the three human CALM loci. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9618785 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9619355 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The title specifies cytosolic CaMKK autophosphorylation, but the narrative expressly leaves CaMKK localization uncertain between cytosol and nucleus. This uncertainty does not negate the separately established cytosolic calmodulin pool. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9619355 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9619376 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Activated calmodulin binds the CAMK1 C-terminal region, exposing CAMKK target residue T177. Calmodulin regulates substrate accessibility; CAMKK supplies the phosphorylation. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9619376 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9653585 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calmodulin binds KRAS4B, can reduce its plasma-membrane affinity and can be diverted from CAMK2 regulation by oncogenic KRAS4B. Phosphorylation of KRAS4B modulates this interaction; no calmodulin lipidation or kinase activity is inferred. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9653585 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654521 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calcium/calmodulin binding dissociates KRAS4B from the plasma membrane independently of nucleotide state. This supports a soluble/peripheral regulatory pool rather than integral-membrane calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9654521 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654523 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: ARL2:GTP changes PDE6D conformation and releases the KRAS4B prenyl group. The summary does not separately assay calmodulin; earlier CaM-mediated KRAS4B release provides pathway context, not an ARL2-like activity for calmodulin. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9654523 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654525 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The title includes the KRAS4B:CALM:Ca2+ complex, and the summary places PDE6D binding after calmodulin-stimulated KRAS4B membrane release. It supports the curated soluble-complex pool without establishing a CALM1-specific transport mechanism. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9654525 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9654533 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The summary discusses ARL2/PDE6D-mediated release and recycling of KRAS4B to the plasma membrane and explicitly says details are incomplete. Calmodulin is not separately assayed in this step; the earlier CaM release event supplies context only. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9654533 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9865670 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Calmodulin:Ca2+ binds the C-terminal region of TRPV4 monomers and potentiates channel activity. Calmodulin is the cytosolic channel regulator, not the membrane-spanning pore. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-HSA-9865670 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-9617449 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Unlike the other cache headers, this record is Rattus norvegicus. The narrative explicitly combines recombinant rat Rasgrf1 expressed in human HEK293T cells, endogenous human activated calmodulin and recombinant human HRAS. The R-NUL prefix does not mean the calmodulin reagent is nonhuman; Rasgrf1, not calmodulin, performs nucleotide exchange. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-NUL-9617449 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-9619243 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: The header is human, but the described binding uses recombinant mouse Camkk1 and recombinant human calmodulin. The narrative leaves nucleus versus cytosol unresolved; no direct localization assay is exposed. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-NUL-9619243 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-9619396 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Porcine-brain CAMKK1 phosphorylates recombinant human CAMK1 at T177 in a calmodulin-dependent assay. The summary does not specify calmodulin species or independently measure its compartment; it is not a direct all-human kinase experiment. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-NUL-9619396 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-9619413 | ACCEPT | Summary: Retain the cytosolic calmodulin pool in the curated event context. Reason: Human CAMKK2 phosphorylates recombinant rat Camk1. The cache does not separately describe calmodulin identity or localization in this experiment; calmodulin regulation is corroborated by the surrounding CAMKK/CAMK1 events. The existing broad cytosol assertion is retained with curator deference and independent corroboration from the explicit cytosolic calmodulin methylation/phosphorylase-kinase records; the event-specific location is not presented as a newly inspected primary assay. Supporting Evidence: Reactome:R-NUL-9619413 Reactome:R-HSA-6786205 Reactome:R-HSA-71541 |
| GO:0002027 regulation of heart rate | IMP PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The CALM1 study identifies segregating and de novo variants with compromised calcium binding and altered RyR2-domain interaction in an arrhythmia context. Reason: The CALM1 study identifies segregating and de novo variants with compromised calcium binding and altered RyR2-domain interaction in an arrhythmia context. This directly links calmodulin sensing to heart-rhythm regulation; its N53I/N97S nomenclature omits the initiator methionine, corresponding to UniProt N54I/N98S. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The primary CALM1 study directly measures compromised calcium binding of disease-associated calmodulin variants. Reason: The primary CALM1 study directly measures compromised calcium binding of disease-associated calmodulin variants. The mutant names use mature-protein numbering, one residue lower than the UniProt precursor convention. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:7607248 A calmodulin-binding sequence in the C-terminus of human car... | ACCEPT | Summary: The human cardiac titin study observes calcium-dependent calmodulin/kinase-region complex formation and conformational changes. Reason: The human cardiac titin study observes calcium-dependent calmodulin/kinase-region complex formation and conformational changes. The intrinsic calcium-binding activity is additionally supported by direct calmodulin-affinity experiments, without assigning titin catalytic activity to calmodulin. |
| GO:0005509 calcium ion binding | IDA PMID:8631777 Blocking the Ca2+-induced conformational transitions in calm... | ACCEPT | Summary: Engineered human calmodulin disulfide mutants have decreased calcium affinity and lose target-enzyme activation, with regulatory activity restored after reduction. Reason: Engineered human calmodulin disulfide mutants have decreased calcium affinity and lose target-enzyme activation, with regulatory activity restored after reduction. This directly links EF-hand-dependent calcium binding and conformational regulation. Supporting Evidence: |
| GO:0005513 detection of calcium ion | IMP PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The CALM1 study identifies segregating and de novo variants with compromised calcium binding and altered RyR2-domain interaction in an arrhythmia context. Reason: The CALM1 study identifies segregating and de novo variants with compromised calcium binding and altered RyR2-domain interaction in an arrhythmia context. This directly links calmodulin sensing to heart-rhythm regulation; its N53I/N97S nomenclature omits the initiator methionine, corresponding to UniProt N54I/N98S. Supporting Evidence: |
| GO:0010880 regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum | IDA PMID:20226167 Defective calmodulin binding to the cardiac ryanodine recept... | ACCEPT | Summary: In a mouse RyR2-R2474S model, altered calmodulin affinity accompanies abnormal calcium release, and added calmodulin attenuates calcium sparks. Reason: In a mouse RyR2-R2474S model, altered calmodulin affinity accompanies abnormal calcium release, and added calmodulin attenuates calcium sparks. This supports calmodulin channel regulation and its calcium-release/contraction consequences; the mutated molecule in that experiment is RyR2, not CALM1. Supporting Evidence: |
| GO:0019901 protein kinase binding | IPI PMID:20668654 Structure of the CaMKIIdelta/calmodulin complex reveals the ... | MODIFY | Summary: The source measures direct binding of human calmodulin to the exact CaMKII isozyme and explains release of kinase autoinhibition. Reason: The source measures direct binding of human calmodulin to the exact CaMKII isozyme and explains release of kinase autoinhibition. Refine the unspecified kinase-binding row to the demonstrated serine/threonine kinase activator activity, preserving the original alpha/delta partner and its experimental evidence. Proposed replacements: protein serine/threonine kinase activator activity Supporting Evidence: |
| GO:0030017 sarcomere | IDA PMID:20226167 Defective calmodulin binding to the cardiac ryanodine recept... | ACCEPT | Summary: Retain the curated sarcomeric localization in the RyR2 model. Reason: Retain the curated sarcomeric localization in the RyR2 model. The original localization experiment is not exposed in the cached abstract, but independent FRET experiments place RyR2-associated calmodulin at Z-lines; this does not make calmodulin a sarcomeric structural component. |
| GO:0031432 titin binding | IPI PMID:7607248 A calmodulin-binding sequence in the C-terminus of human car... | KEEP AS NON CORE | Summary: The source directly tests human titin kinase-region constructs and synthetic peptides for equimolar calcium-dependent binding to calmodulin. Reason: The source directly tests human titin kinase-region constructs and synthetic peptides for equimolar calcium-dependent binding to calmodulin. Retain the exact titin partner; the inspected evidence proposes, rather than establishes, a kinase-regulatory consequence. Supporting Evidence: |
| GO:0043539 protein serine/threonine kinase activator activity | TAS PMID:20668654 Structure of the CaMKIIdelta/calmodulin complex reveals the ... | ACCEPT | Summary: The human CaMKII/calmodulin structure and solution-binding experiments explain how calmodulin displaces the inhibitory segment and enables the active kinase configuration. Reason: The human CaMKII/calmodulin structure and solution-binding experiments explain how calmodulin displaces the inhibitory segment and enables the active kinase configuration. This is calmodulin activator activity, while ATP binding and phosphoryl transfer remain activities of CaMKII. Supporting Evidence: |
| GO:0044325 transmembrane transporter binding | IPI PMID:21167176 Solution NMR structure of Apo-calmodulin in complex with the... | KEEP AS NON CORE | Summary: NMR and solution experiments directly demonstrate apo-calmodulin binding to the human NaV1.5 IQ motif. Reason: NMR and solution experiments directly demonstrate apo-calmodulin binding to the human NaV1.5 IQ motif. Retain the specific transmembrane-transporter interaction; the peptide structure alone does not establish every proposed effect on intact-channel gating. Supporting Evidence: |
| GO:0044325 transmembrane transporter binding | IPI PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The CALM1 variant paper directly measures interaction with the RyR2 calmodulin-binding-domain peptide. Reason: The CALM1 variant paper directly measures interaction with the RyR2 calmodulin-binding-domain peptide. Retain the exact RyR2 partner and transporter-binding subactivity as part of the channel-regulatory mechanism, without claiming that a peptide assay alone resolves the intact complex. |
| GO:0051592 response to calcium ion | IDA PMID:7607248 A calmodulin-binding sequence in the C-terminus of human car... | ACCEPT | Summary: Calcium addition changes calmodulin binding and conformation in the human titin-fragment experiments. Reason: Calcium addition changes calmodulin binding and conformation in the human titin-fragment experiments. This is a genuine calcium response by the sensor protein, incorporated into its target-regulatory mechanism without transferring titin enzyme activity. Supporting Evidence: |
| GO:0055117 regulation of cardiac muscle contraction | IMP PMID:23040497 Mutations in calmodulin cause ventricular tachycardia and su... | ACCEPT | Summary: The human CALM1 variant study supports regulation of cardiac function through calcium sensing and RyR2 coupling. Reason: The human CALM1 variant study supports regulation of cardiac function through calcium sensing and RyR2 coupling. Retain the broader cardiac-contraction regulatory assertion alongside its existing more mechanistic calcium-release child, without adding a redundant new annotation. |
| GO:0072542 protein phosphatase activator activity | IDA PMID:8631777 Blocking the Ca2+-induced conformational transitions in calm... | ACCEPT | Summary: The experiment uses engineered human liver calmodulin with intramolecular disulfides that restrict calcium-induced opening. Reason: The experiment uses engineered human liver calmodulin with intramolecular disulfides that restrict calcium-induced opening. Loss and chemical restoration of calcineurin activation directly support calmodulin phosphatase-activator function and its participation in calcineurin signaling, not phosphatase catalysis. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:26164367 Distinctive malfunctions of calmodulin mutations associated ... | ACCEPT | Summary: The source directly compares calcium binding of CPVT- and LQTS-associated human calmodulin variants. Reason: The source directly compares calcium binding of CPVT- and LQTS-associated human calmodulin variants. Their target-specific functional effects differ, so impaired calcium affinity is not treated as a uniform effect on all calcium channels. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:26969752 Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded... | ACCEPT | Summary: Direct recombinant-protein measurements establish impaired C-domain calcium affinity of E141G calmodulin. Reason: Direct recombinant-protein measurements establish impaired C-domain calcium affinity of E141G calmodulin. The cached author narrative and PubMed abstract differ in cohort counts, which are not used here; the biochemical finding is consistent across them. Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:27516456 Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A1... | ACCEPT | Summary: The source studies CALM3-A103V clinical disease but explicitly compares the shared calmodulin protein with established CALM1 N54I/N98S variants. Reason: The source studies CALM3-A103V clinical disease but explicitly compares the shared calmodulin protein with established CALM1 N54I/N98S variants. Retain calcium binding as a well-established function of the identical wild-type protein; neither the clinical CALM3 mutation nor its case count is reassigned to CALM1. |
| GO:0005737 cytoplasm | IDA PMID:27165696 Arrhythmogenic calmodulin mutations impede activation of sma... | ACCEPT | Summary: The SK2 study uses human calmodulin constructs in HEK293 cells and describes intracellular distribution experiments. Reason: The SK2 study uses human calmodulin constructs in HEK293 cells and describes intracellular distribution experiments. Retain the broad cytoplasmic source localization, while not confusing SK2 membrane-protein distribution controls with proof of exclusive calmodulin localization. Supporting Evidence: |
| GO:0019855 calcium channel inhibitor activity | IDA PMID:26969752 Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded... | ACCEPT | Summary: Wild-type calmodulin mediates calcium-dependent inactivation of CaV1.2, whereas E141G reduces that inactivation in whole-cell and ventricular-myocyte experiments. Reason: Wild-type calmodulin mediates calcium-dependent inactivation of CaV1.2, whereas E141G reduces that inactivation in whole-cell and ventricular-myocyte experiments. This supports calcium-channel inhibitor activity, without implying that calmodulin inhibits every channel it binds. |
| GO:0060314 regulation of ryanodine-sensitive calcium-release channel activity | IDA PMID:22067155 FRET detection of calmodulin binding to the cardiac RyR2 cal... | ACCEPT | Summary: RyR2-directed FRET resolves calmodulin binding in SR vesicles and permeabilized ventricular myocytes, with calcium-dependent affinity and dissociation. Reason: RyR2-directed FRET resolves calmodulin binding in SR vesicles and permeabilized ventricular myocytes, with calcium-dependent affinity and dissociation. Retain the curated channel-regulatory role, corroborated by direct inhibition experiments in other cited studies; the FRET measurement itself reports binding rather than a new gating assay. |
| GO:0060315 negative regulation of ryanodine-sensitive calcium-release channel activity | IDA PMID:26164367 Distinctive malfunctions of calmodulin mutations associated ... | ACCEPT | Summary: The source compares human calmodulin variants using calcium-affinity, RyR2-binding and channel-activity assays, supporting wild-type inhibition of RyR2. Reason: The source compares human calmodulin variants using calcium-affinity, RyR2-binding and channel-activity assays, supporting wild-type inhibition of RyR2. CPVT variants impair that control, while LQTS variants can show different target effects; a universal loss-of-function model is not assumed. Supporting Evidence: PMID:26164367 modulation of [(3)H]ryanodine binding to RyR2 |
| GO:0005515 protein binding | IPI PMID:16127172 Calcium/calmodulin regulates ubiquitination of the ubiquitin... | MODIFY | Summary: Direct USP6 binding supports protease binding. Reason: The complete PMID:16127172 abstract explicitly describes calcium-dependent direct binding of calmodulin to the ubiquitin-specific protease USP6 in vitro and in cells, with binding-site mutants. Its reported functional effect concerns ubiquitination of USP6, not demonstrated activation of USP6 deubiquitinase catalysis. Refine to protease binding; the bound enzyme remains the protease and no calmodulin ubiquitin-ligase activity is implied. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005509 calcium ion binding | IDA PMID:27564677 Structural Insights into the M-Channel Proximal C-Terminus/C... | ACCEPT | Summary: The Kv7 calmodulin-complex crystal structure contains four bound calcium ions and demonstrates a target-associated hybrid conformation. Reason: The Kv7 calmodulin-complex crystal structure contains four bound calcium ions and demonstrates a target-associated hybrid conformation. Retain direct calcium binding while distinguishing the chimeric Kv7.3/Kv7.2 construct from an intact native channel assembly. Supporting Evidence: PMID:27564677 four Ca(2+) ions are bound |
| GO:0005515 protein binding | IPI PMID:19855925 Structural analysis of the complex between calmodulin and fu... | KEEP AS NON CORE | Summary: Retain the myelin-basic-protein interaction in its biochemical context. Reason: The complete PMID:19855925 abstract describes calmodulin-affinity capture of human brain myelin basic protein and structural/biophysical binding experiments with full-length protein and rodent peptides. Retain the exact curated partner P04370; the individual accession-to-assay mapping and full Methods were not independently inspected. The official 2010 correction replaces Figure 5 panels and corrects the circular-dichroism axis unit; its prose was read, but corrected images were not reanalysed. This supports bounded binding without a separate enzyme-regulatory claim. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19855925 Structural analysis of the complex between calmodulin and fu... | KEEP AS NON CORE | Summary: Retain the myelin-basic-protein interaction in its biochemical context. Reason: The complete PMID:19855925 abstract describes calmodulin-affinity capture of human brain myelin basic protein and structural/biophysical binding experiments with full-length protein and rodent peptides. Retain the exact curated partner P81558; the individual accession-to-assay mapping and full Methods were not independently inspected. The official 2010 correction replaces Figure 5 panels and corrects the circular-dichroism axis unit; its prose was read, but corrected images were not reanalysed. This supports bounded binding without a separate enzyme-regulatory claim. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21299499 IQ-motif selectivity in human IQGAP2 and IQGAP3: binding of ... | KEEP AS NON CORE | Summary: Retain calmodulin binding to IQGAP3 IQ motifs. Reason: Selected PMID:21299499 Methods and Results describe recombinant human calmodulin and IQGAP3-derived IQ peptides, with calcium-dependent mobility-shift binding assays. These establish the peptide-binding interaction and support the curated full-protein edge. Preserve the original partner; motif-peptide affinities do not establish the affinity or regulatory direction of every intact cellular complex, or confer GTPase activity on calmodulin. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27564677 Structural Insights into the M-Channel Proximal C-Terminus/C... | MODIFY | Summary: Calmodulin binds the Kv7.2/Kv7.3 channel cytoplasmic domains. Reason: The complete PMID:27564677 abstract directly reports a 1:1 calmodulin complex with a chimeric Kv7.3/Kv7.2 proximal C-terminal region and a high-resolution structure. The specific binding category is transmembrane transporter binding. Preserve the exact O43526 source partner; the chimeric structural and electrophysiological evidence does not imply that every physiological property was tested independently for each native channel. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0019901 protein kinase binding | IPI PMID:20668654 Structure of the CaMKIIdelta/calmodulin complex reveals the ... | MODIFY | Summary: The source measures direct binding of human calmodulin to the exact CaMKII isozyme and explains release of kinase autoinhibition. Reason: The source measures direct binding of human calmodulin to the exact CaMKII isozyme and explains release of kinase autoinhibition. Refine the unspecified kinase-binding row to the demonstrated serine/threonine kinase activator activity, preserving the original alpha/delta partner and its experimental evidence. Proposed replacements: protein serine/threonine kinase activator activity Supporting Evidence: |
Loading supporting content…
Download this section (compressed HTML)Q: How do CALM1-specific transcript regulation and pathogenic variants alter target occupancy when CALM2 and CALM3 supply an identical wild-type calmodulin protein?
Q: Which original experiments resolve the remaining G2/M-transition, sperm-midpiece, calyx-of-Held, presynaptic-endocytosis and calcium-export assertions, and distinguish nuclear from cytosolic CaMKK reaction contexts within the established nuclear and cytosolic calmodulin pools?
Q: Can the original LYST and tau target-interaction records be recovered to resolve the remaining source-specific uncertainty?
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)