CABP2

Summary: CaBP2 regulates calcium-channel inactivation in sensory cells.

Reason: Human CaBP2 suppresses CaV1.3 calcium-dependent inactivation in the 2012 heterologous assay, and the 2017 native mouse study finds increased channel inactivation after Cabp2 disruption. The latter room-temperature analysis primarily resolves increased voltage-dependent inactivation; its CDI trend was not significant. Together these experiments support the existing broad calcium-channel regulator activity. The refined 2017 cell assay did not reproduce the earlier decrease in peak current density, and native current density was unchanged. The conserved assertion is retained with human construct, rat channel and native mouse boundaries distinguished.

Summary: CaBP2 regulates calcium-channel inactivation in sensory cells.

Reason: Human CaBP2 suppresses CaV1.3 calcium-dependent inactivation in the 2012 heterologous assay, and the 2017 native mouse study finds increased channel inactivation after Cabp2 disruption. The latter room-temperature analysis primarily resolves increased voltage-dependent inactivation; its CDI trend was not significant. Together these experiments support the existing broad calcium-channel regulator activity. The refined 2017 cell assay did not reproduce the earlier decrease in peak current density, and native current density was unchanged. The conserved assertion is retained with human construct, rat channel and native mouse boundaries distinguished.

Summary: Calcium binding is an intrinsic feature of the CaBP2 sensory regulator.

Reason: Calcium binding is supported by target recombinant-protein isothermal titration calorimetry in PMID:22981119 and PMID:28183797, independently of the earlier calcium-sensitive purification behavior in PMID:10625670. The 2012 WT protein and truncation surrogate had different binding thermodynamics. No exact physiological affinity or equivalence of the two normal human splice products is inferred. Calcium sensing is part of the same channel-regulatory unit.

Summary: Calcium binding is an intrinsic feature of the CaBP2 sensory regulator.

Reason: Calcium binding is supported by target recombinant-protein isothermal titration calorimetry in PMID:22981119 and PMID:28183797, independently of the earlier calcium-sensitive purification behavior in PMID:10625670. The 2012 WT protein and truncation surrogate had different binding thermodynamics. No exact physiological affinity or equivalence of the two normal human splice products is inferred. Calcium sensing is part of the same channel-regulatory unit.

Summary: CABP2 has a curated binary interaction with DPEP2NB (A0A0U1RQF7).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact A0A0U1RQF7 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with GOLGA6L9 (A6NEM1).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact A6NEM1 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with ZNF785 (A8K8V0).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact A8K8V0 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with NME4 (O00746).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact O00746 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with SNAI2 (O43623).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact O43623 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with TNNI1 (P19237).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact P19237 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with HOXD12 (P35452-2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact P35452-2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform P35452-2 is retained.

Summary: CABP2 has a curated binary interaction with ZNF140 (P52738).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact P52738 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with PRR20D (P86480).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact P86480 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with TLE5 (Q08117-2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q08117-2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform Q08117-2 is retained.

Summary: CABP2 has a curated binary interaction with EFHC2 (Q5JST6).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q5JST6 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with COA6 (Q5JTJ3).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q5JTJ3 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with AVPI1 (Q5T686).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q5T686 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with ZNF57 (Q68EA5).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q68EA5 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with ZNF774 (Q6NX45).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q6NX45 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with C22orf39 (Q6P5X5).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q6P5X5 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with RD3 (Q7Z3Z2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q7Z3Z2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with ADGRF5 (Q8IZF2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q8IZF2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with ANKRD29 (Q8N6D5).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q8N6D5 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with SPMIP6 (Q8NCR6).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q8NCR6 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with VXN (Q8TAG6).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q8TAG6 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with THAP6 (Q8TBB0).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q8TBB0 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with HOOK2 (Q96ED9-2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q96ED9-2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform Q96ED9-2 is retained.

Summary: CABP2 has a curated binary interaction with TEKT5 (Q96M29).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q96M29 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with NUDT16L1 (Q9BRJ7).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9BRJ7 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with MXRA8 (Q9BRK3).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9BRK3 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with NDUFAF3 (Q9BU61).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9BU61 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with SPATC1L (Q9H0A9-2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9H0A9-2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform Q9H0A9-2 is retained.

Summary: CABP2 has a curated binary interaction with CIMIP1 (Q9H1P6).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9H1P6 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with CARD9 (Q9H257-2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9H257-2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform Q9H257-2 is retained.

Summary: CABP2 has a curated binary interaction with UNKL (Q9H9P5-5).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9H9P5-5 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform Q9H9P5-5 is retained.

Summary: CABP2 has a curated binary interaction with NOP10 (Q9NPE3).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9NPE3 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2.

Summary: CABP2 has a curated binary interaction with TRIM35 (Q9UPQ4-2).

Reason: The HuRI human-protein interaction study uses systematic yeast two-hybrid screening with pairwise retesting and sequence confirmation. The exact Q9UPQ4-2 edge is present in both the source GOA record and the UniProt IntAct interaction list. Retain the curator-supported physical interaction as non-core; the individual target supplementary record was not independently inspected and no partner-specific orthogonal validation is claimed. This edge alone does not establish a channel-regulatory role or transfer the partner's biochemical function to CABP2. The exact partner isoform Q9UPQ4-2 is retained.

Summary: Tagged human CaBP2 shows perinuclear Golgi-like localization in the tested neuronal cell model.

Reason: PMID:19338761 includes human CaBP2 among the fluorescent constructs expressed in differentiated Neuro2A cells and reports a perinuclear region resembling the Golgi apparatus. This supports retaining the curated Golgi assignment with model and morphology limits. The stronger syntaxin-6/VSVG TGN colocalization assays in that paper concern CaBP7/8, not CaBP2; no TGN-specific or endogenous human localization is inferred.

Summary: Tagged human CaBP2 shows perinuclear Golgi-like localization in the tested neuronal cell model.

Reason: PMID:19338761 includes human CaBP2 among the fluorescent constructs expressed in differentiated Neuro2A cells and reports a perinuclear region resembling the Golgi apparatus. This supports retaining the curated Golgi assignment with model and morphology limits. The stronger syntaxin-6/VSVG TGN colocalization assays in that paper concern CaBP7/8, not CaBP2; no TGN-specific or endogenous human localization is inferred.

Summary: CaBP2 can associate with the plasma membrane, consistent with its membrane-channel regulatory role.

Reason: The exact tagged human CaBP2 construct was examined in PMID:19338761, whose Results report membrane association and plasma-membrane localization in differentiated Neuro2A cells. UniProt independently curates membrane association. This supports its location at the membrane where it regulates channels, with the tagged-protein model distinguished from endogenous sensory-cell localization. The IBA target self-source is legitimate descendant experimental evidence, not circularity.

Summary: CaBP2 can associate with the plasma membrane, consistent with its membrane-channel regulatory role.

Reason: The exact tagged human CaBP2 construct was examined in PMID:19338761, whose Results report membrane association and plasma-membrane localization in differentiated Neuro2A cells. UniProt independently curates membrane association. This supports its location at the membrane where it regulates channels, with the tagged-protein model distinguished from endogenous sensory-cell localization.

Summary: CaBP2 can associate with the plasma membrane, consistent with its membrane-channel regulatory role.

Reason: The exact tagged human CaBP2 construct was examined in PMID:19338761, whose Results report membrane association and plasma-membrane localization in differentiated Neuro2A cells. UniProt independently curates membrane association. This supports its location at the membrane where it regulates channels, with the tagged-protein model distinguished from endogenous sensory-cell localization.

Summary: CaBP2 modulates calcium-dependent signal transmission.

Reason: PMID:10625670 reports CaBP2 calcium sensitivity and in-vitro effector modulation, including CaMKII stimulation, while explicitly leaving physiological target colocalization unresolved. The broad signal-transduction assignment is compatible with later calcium-channel regulation. It is retained as broad context without inventing a kinase, a physiological GRK5-inhibitor core, or a separate generic signaling core.

Summary: Mouse CaBP2 physiology supports the conserved retinal signal-transmission annotation.

Reason: UniProt retains the retinal function by similarity to mouse CaBP2/Q9JLK4. PMID:27822497 directly records light-evoked excitatory currents in mouse retinal whole mounts: Cabp2 loss reduced ON-alpha ganglion-cell response amplitude and modestly slowed its kinetics under cone-dominated stimulation. This supports the broad visual-perception assertion by ortholog and curator deference, without claiming that human retinal physiology was tested. The precise CaBP2 target and presynaptic mechanism in the retinal circuit remain unresolved. Apparently intact scotopic electroretinograms in PMID:28183797 are a neutral contextual result, not positive support; PMID:27822497 also reports unchanged ERG b-waves in its Discussion (data not shown). Different readouts can reveal different circuit effects, and these findings do not establish a direct phototransduction step.

Summary: Mouse CaBP2 physiology supports the conserved retinal signal-transmission annotation.

Reason: UniProt retains the retinal function by similarity to mouse CaBP2/Q9JLK4. PMID:27822497 directly records light-evoked excitatory currents in mouse retinal whole mounts: Cabp2 loss reduced ON-alpha ganglion-cell response amplitude and modestly slowed its kinetics under cone-dominated stimulation. This supports the broad visual-perception assertion by ortholog and curator deference, without claiming that human retinal physiology was tested. The precise CaBP2 target and presynaptic mechanism in the retinal circuit remain unresolved. Apparently intact scotopic electroretinograms in PMID:28183797 are a neutral contextual result, not positive support; PMID:27822497 also reports unchanged ERG b-waves in its Discussion (data not shown). Different readouts can reveal different circuit effects, and these findings do not establish a direct phototransduction step.

Summary: Direct participation in phototransduction remains less resolved than retinal signal transmission.

Reason: Official GO:0007602 describes intracellular conversion of absorbed photons into a molecular signal, under detection of light stimulus and signal transduction. The inspected CaBP2 evidence establishes retinal expression and downstream light-response transmission but does not resolve its step in photon conversion. The PAINT node PTN000550340 and its Cabp4 descendant evidence are preserved; a different paralog or a short donor list is not evidence that the node placement is wrong. Pending target-step and phylogenetic adjudication, retain uncertainty rather than declaring this conserved assertion false.

Summary: CaBP2 supports sound encoding through calcium-channel regulation at inner-hair-cell synapses.

Reason: Human CABP2 variants cause hearing impairment, while mouse Cabp2 disruption increases IHC calcium-channel inactivation and reduces spontaneous and sound-evoked SGN firing without loss of cochlear amplification. Presynaptic calcium-channel regulation therefore supports synaptic sound encoding. The 2017 capacitance measurements did not directly show reduced exocytosis; impaired channel availability is a proposed explanation of the neural phenotype. Human genetics and heterologous assays are distinguished from native mouse physiology.

Summary: CaBP2 supports sound encoding through calcium-channel regulation at inner-hair-cell synapses.

Reason: Human CABP2 variants cause hearing impairment, while mouse Cabp2 disruption increases IHC calcium-channel inactivation and reduces spontaneous and sound-evoked SGN firing without loss of cochlear amplification. Presynaptic calcium-channel regulation therefore supports synaptic sound encoding. The 2017 capacitance measurements did not directly show reduced exocytosis; impaired channel availability is a proposed explanation of the neural phenotype. Human genetics and heterologous assays are distinguished from native mouse physiology.

Summary: A perinuclear CaBP2 pool is reported in a tagged-protein cell model.

Reason: The normal UniProt mapping is consistent with PMID:19338761, whose Results explicitly include human CaBP2 in differentiated Neuro2A cells. Retain this contextual localization without assuming an endogenous human perinuclear organelle pool or transferring CaBP7/8-specific TGN marker results.