CACNB3 encodes the cytoplasmic beta3 regulatory subunit of voltage-gated calcium channels. Its SH3βguanylate-kinase-like module binds pore-forming alpha subunits, modulates channel gating and supports functional surface expression, influencing calcium influx in excitable cells.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005245 voltage-gated calcium channel activity | IDA PMID:11160515 Biophysical properties, pharmacology, and modulation of huma... | MODIFY | Summary: Beta3 regulates the pore-forming alpha subunit. Coexpression establishes a contribution to channel activity, while calcium channel regulator activity specifies the beta-subunit mechanism. Reason: Beta3 regulates the pore-forming alpha subunit. Coexpression establishes a contribution to channel activity, while calcium channel regulator activity specifies the beta-subunit mechanism. Proposed replacements: calcium channel regulator activity Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005245 voltage-gated calcium channel activity | IEA GO_REF:0000120 | MODIFY | Summary: Beta3 regulates the pore-forming alpha subunit. Coexpression establishes a contribution to channel activity, while calcium channel regulator activity specifies the beta-subunit mechanism. Reason: Beta3 regulates the pore-forming alpha subunit. Coexpression establishes a contribution to channel activity, while calcium channel regulator activity specifies the beta-subunit mechanism. Proposed replacements: calcium channel regulator activity Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005245 voltage-gated calcium channel activity | TAS PMID:8119293 Cloning, chromosomal location and functional expression of t... | MODIFY | Summary: Beta3 regulates the pore-forming alpha subunit. Coexpression establishes a contribution to channel activity, while calcium channel regulator activity specifies the beta-subunit mechanism. Reason: Beta3 regulates the pore-forming alpha subunit. Coexpression establishes a contribution to channel activity, while calcium channel regulator activity specifies the beta-subunit mechanism. Proposed replacements: calcium channel regulator activity Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005246 calcium channel regulator activity | ISS GO_REF:0000024 | ACCEPT | Summary: Human beta3 coexpression modulates L-type channel currents; regulation is its direct molecular role. Reason: Human beta3 coexpression modulates L-type channel currents; regulation is its direct molecular role. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005246 calcium channel regulator activity | ISS PMID:25527503 Functional characterization of CaVΞ±2Ξ΄ mutations associated w... | ACCEPT | Summary: Human beta3 coexpression modulates L-type channel currents; regulation is its direct molecular role. Reason: Human beta3 coexpression modulates L-type channel currents; regulation is its direct molecular role. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005515 protein binding | IPI PMID:18535142 Calmodulin-dependent gating of Ca(v)1.2 calcium channels in ... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:37207277 Using brain cell-type-specific protein interactomes to inter... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. Reason: The physical interaction is retained, but generic protein binding does not specify the channel-regulatory mechanism. The high-throughput interaction is not used as proof of an additional enzymatic function. |
| GO:0005737 cytoplasm | EXP PMID:34234349 Structure of human Ca(v)2.2 channel blocked by the painkille... | UNDECIDED | Summary: The cited experimental publication is not accessible in the local cache after the retrieval attempt; its specific cytoplasmic-localization observation remains unresolved. Reason: The cited experimental publication is not accessible in the local cache after the retrieval attempt; its specific cytoplasmic-localization observation remains unresolved. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: CACNB3 is an intracellular accessory subunit acting on the cytoplasmic face of the calcium-channel complex. Reason: CACNB3 is an intracellular accessory subunit acting on the cytoplasmic face of the calcium-channel complex. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-210420 | ACCEPT | Summary: The beta subunit is a cytosolic regulator that associates with intracellular portions of channel alpha subunits. Reason: The beta subunit is a cytosolic regulator that associates with intracellular portions of channel alpha subunits. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005891 voltage-gated calcium channel complex | IBA GO_REF:0000033 | ACCEPT | Summary: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Reason: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005891 voltage-gated calcium channel complex | IDA PMID:11160515 Biophysical properties, pharmacology, and modulation of huma... | ACCEPT | Summary: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Reason: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005891 voltage-gated calcium channel complex | IEA GO_REF:0000120 | ACCEPT | Summary: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Reason: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0005891 voltage-gated calcium channel complex | TAS PMID:8119293 Cloning, chromosomal location and functional expression of t... | ACCEPT | Summary: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Reason: Reconstitution experiments place human beta3 in functional calcium-channel complexes. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0006816 calcium ion transport | IBA GO_REF:0000033 | ACCEPT | Summary: Beta3 participates in calcium-ion transport by regulating functional channel complexes; it need not itself form the pore. Reason: Beta3 participates in calcium-ion transport by regulating functional channel complexes; it need not itself form the pore. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0006816 calcium ion transport | IDA PMID:11160515 Biophysical properties, pharmacology, and modulation of huma... | ACCEPT | Summary: Beta3 participates in calcium-ion transport by regulating functional channel complexes; it need not itself form the pore. Reason: Beta3 participates in calcium-ion transport by regulating functional channel complexes; it need not itself form the pore. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0008331 high voltage-gated calcium channel activity | IBA GO_REF:0000033 | MODIFY | Summary: The high-voltage-activated channel is a multimeric assembly. Calcium channel regulator activity captures the beta3 subunit-specific role. Reason: The high-voltage-activated channel is a multimeric assembly. Calcium channel regulator activity captures the beta3 subunit-specific role. Proposed replacements: calcium channel regulator activity Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0016020 membrane | IDA PMID:16525042 Alternative splicing of the voltage-gated Ca2+ channel beta4... | ACCEPT | Summary: Association with membrane channel complexes is consistent with membrane proteomics; this does not imply a transmembrane beta subunit. Reason: Association with membrane channel complexes is consistent with membrane proteomics; this does not imply a transmembrane beta subunit. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0030315 T-tubule | IEA GO_REF:0000117 | UNDECIDED | Summary: The cited reviews discuss calcium-channel organization, but the evidence needed to assign a T-tubule location specifically to beta3 has not been isolated here. This is not a rejection based on a paper foregrounding another subunit. Reason: The cited reviews discuss calcium-channel organization, but the evidence needed to assign a T-tubule location specifically to beta3 has not been isolated here. This is not a rejection based on a paper foregrounding another subunit. |
| GO:0030315 T-tubule | NAS PMID:27273705 Voltage-gated calcium channels and their auxiliary subunits:... | UNDECIDED | Summary: The cited reviews discuss calcium-channel organization, but the evidence needed to assign a T-tubule location specifically to beta3 has not been isolated here. This is not a rejection based on a paper foregrounding another subunit. Reason: The cited reviews discuss calcium-channel organization, but the evidence needed to assign a T-tubule location specifically to beta3 has not been isolated here. This is not a rejection based on a paper foregrounding another subunit. |
| GO:0045933 positive regulation of muscle contraction | NAS PMID:22982493 Ca(V)1.1: The atypical prototypical voltage-gated CaΒ²βΊ chann... | KEEP AS NON CORE | Summary: Regulation of calcium entry can affect contraction. This physiological outcome is contextual and does not replace channel regulation as the core molecular role. Reason: Regulation of calcium entry can affect contraction. This physiological outcome is contextual and does not replace channel regulation as the core molecular role. |
| GO:0045933 positive regulation of muscle contraction | NAS PMID:34072954 Mechanisms and Regulation of Cardiac Ca(V)1.2 Trafficking. | KEEP AS NON CORE | Summary: Regulation of calcium entry can affect contraction. This physiological outcome is contextual and does not replace channel regulation as the core molecular role. Reason: Regulation of calcium entry can affect contraction. This physiological outcome is contextual and does not replace channel regulation as the core molecular role. |
| GO:0060402 calcium ion transport into cytosol | ISS PMID:25527503 Functional characterization of CaVΞ±2Ξ΄ mutations associated w... | ACCEPT | Summary: Beta3-containing channel complexes support calcium entry into the cytosol; the subunit participates by regulating channel function. Reason: Beta3-containing channel complexes support calcium entry into the cytosol; the subunit participates by regulating channel function. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0061577 calcium ion transmembrane transport via high voltage-gated calcium channel | ISS GO_REF:0000024 | ACCEPT | Summary: Functional beta3-containing high-voltage-activated channel complexes support this calcium-transport process. Reason: Functional beta3-containing high-voltage-activated channel complexes support this calcium-transport process. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0061577 calcium ion transmembrane transport via high voltage-gated calcium channel | ISS PMID:25527503 Functional characterization of CaVΞ±2Ξ΄ mutations associated w... | ACCEPT | Summary: Functional beta3-containing high-voltage-activated channel complexes support this calcium-transport process. Reason: Functional beta3-containing high-voltage-activated channel complexes support this calcium-transport process. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0070588 calcium ion transmembrane transport | IDA PMID:27481713 The Ξ±2Ξ΄-1 subunit remodels CaV1.2 voltage sensors and allows... | ACCEPT | Summary: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Reason: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0070588 calcium ion transmembrane transport | IEA GO_REF:0000002 | ACCEPT | Summary: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Reason: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0070588 calcium ion transmembrane transport | NAS PMID:22982493 Ca(V)1.1: The atypical prototypical voltage-gated CaΒ²βΊ chann... | ACCEPT | Summary: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Reason: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0070588 calcium ion transmembrane transport | NAS PMID:27273705 Voltage-gated calcium channels and their auxiliary subunits:... | ACCEPT | Summary: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Reason: Coexpression and electrophysiology establish participation of beta3 in functional transmembrane calcium transport. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0072659 protein localization to plasma membrane | ISS PMID:25527503 Functional characterization of CaVΞ±2Ξ΄ mutations associated w... | ACCEPT | Summary: CaV beta-subunit association supports channel surface expression, consistent with the conserved trafficking role of the SH3βGK module. Reason: CaV beta-subunit association supports channel surface expression, consistent with the conserved trafficking role of the SH3βGK module. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:0098903 regulation of membrane repolarization during action potential | ISS PMID:25527503 Functional characterization of CaVΞ±2Ξ΄ mutations associated w... | KEEP AS NON CORE | Summary: Calcium-channel regulation can influence action-potential repolarization in excitable cells, but the particular tissue and channel partner determine the effect. Reason: Calcium-channel regulation can influence action-potential repolarization in excitable cells, but the particular tissue and channel partner determine the effect. |
| GO:1901843 positive regulation of high voltage-gated calcium channel activity | ISS GO_REF:0000024 | ACCEPT | Summary: The beta3 regulatory subunit supports functional high-voltage-activated channel activity in coexpression systems. Reason: The beta3 regulatory subunit supports functional high-voltage-activated channel activity in coexpression systems. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:1990454 L-type voltage-gated calcium channel complex | IPI PMID:27481713 The Ξ±2Ξ΄-1 subunit remodels CaV1.2 voltage sensors and allows... | ACCEPT | Summary: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Reason: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:1990454 L-type voltage-gated calcium channel complex | ISS GO_REF:0000024 | ACCEPT | Summary: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Reason: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:1990454 L-type voltage-gated calcium channel complex | ISS GO_REF:0000114 | ACCEPT | Summary: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Reason: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
| GO:1990454 L-type voltage-gated calcium channel complex | ISS PMID:25527503 Functional characterization of CaVΞ±2Ξ΄ mutations associated w... | ACCEPT | Summary: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Reason: Human beta3 was included in functional L-type channel assemblies in the cited coexpression experiments. Supporting Evidence: PMID:8119293 The cloned H beta 3 subunit was further expressed in Xenopus oocytes to demonstrate its ability to modulate VDCC activity. |
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)The human reference supplies mechanistic evidence for the corresponding selected horse protein; the human conclusion alone is not validation of the horse sequence. The exact horse comparison is in genes/HORSE/CACNB3/CACNB3-bioinformatics/RESULTS.md. Research reports are source leads; annotation decisions cite the underlying publication or experimentally supported UniProt passages. Unresolved source-specific results retain UNDECIDED.
Loading supporting contentβ¦
Download this section (compressed HTML)