BMP10

Summary: BMP10 is an extracellular TGF-beta-superfamily signaling ligand.

Reason: The PAINT cytokine assertion is consistent with BMP10 activating receptor complexes and downstream SMAD signaling (PMID:16049014; PMID:17068149). This is an inherited ligand activity; neither the number of donor proteins nor the presence of target-specific evidence challenges the ancestral-node inference. The PAINT tree itself was not independently re-curated.

Summary: Secreted BMP10 can transmit a regulatory signal to responding cardiomyocytes.

Reason: The PMID:17921333 abstract reports extracellular secretion and hypertrophic activity of conditioned medium on rat neonatal cardiomyocytes. This supports the existing hormone-activity assertion at the level of a secreted regulatory ligand. It does not independently establish physiological circulating concentrations or a specific endocrine route. The narrower core summary uses growth-factor activity.

Summary: The BMP10 interaction with ACVRL1/ALK1 is functionally a receptor-binding interaction.

Reason: The PMID:17068149 abstract explicitly identifies BMP10 as a potent ALK1 ligand. The source partner P37023 is the ALK1 receptor, and the seeded receptor serine/threonine kinase binding term already captures this mechanism more informatively than generic protein binding. BMP9-specific quantitative experiments are not transferred to BMP10. The selected binary/ternary receptor-complex Results in PMID:35504921 independently resolve BMP10 contacts with ALK1 and BMPRII. This evidence supports the proposed receptor-binding specificity.

Proposed replacements: receptor serine/threonine kinase binding

Summary: BMP10 binding to telethonin is supported and has an existing specific term.

Reason: The PMID:17921333 abstract explicitly reports BMP10 interaction with titin-cap/telethonin and reduced binding by a human BMP10 variant. Replace the generic binding description with telethonin binding, already present among the seeded annotations. This does not turn the interaction into a second core ligand activity.

Proposed replacements: telethonin binding

Summary: The BMP10 prodomain docks to fibrillin-1 in an extracellular targeting interaction.

Reason: PMID:18339631 reports BMP10 prodomain binding to the N-terminal region of fibrillin-1, an extracellular matrix component. GO:0050840 captures that binding specificity more informatively than generic protein binding. PMID:39921464 section 3.8 further measures binding of the processed prodomain-growth-factor complex to a fibrillin-1 fragment, with no detected binding by the unprocessed precursor in that assay. The refinement describes extracellular targeting, not receptor activation or a new core function; it does not assert an independently established in-vivo latent conformation.

Proposed replacements: extracellular matrix binding

Summary: BMP10 prodomain binding to fibrillin-2 is supported by recombinant binding measurements.

Reason: Selected Table 3 and Discussion of PMID:18339631 identify binding of the BMP10 prodomain to recombinant fibrillin-2 fragment rF86. Fibrillin-2 is an extracellular matrix component, so GO:0050840 refines the existing physical interaction without assigning an additional signaling activity. The experiment used a fibrillin fragment; binding to an assembled microfibril is not asserted by this refinement.

Proposed replacements: extracellular matrix binding

Summary: HuRI reports BMP10 binding to BSCL2 (UniProtKB:J3KQ12); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names BSCL2 (UniProtKB:J3KQ12), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For BSCL2, the membrane-localization concern requires the actual interaction domain and its orientation to be established; an ER-associated label alone does not exclude contact with a BMP10 precursor in the secretory pathway. The J3KQ12 construct itself has not been inspected. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to MGST3 (UniProtKB:O14880); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names MGST3 (UniProtKB:O14880), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For MGST3, a proposed microsomal location raises the question of which membrane face and construct were assayed. Neither the binding surface nor contact with the BMP10 precursor or mature ligand has been established here. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TMPRSS2 (UniProtKB:O15393-2); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TMPRSS2 (UniProtKB:O15393-2), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. The assertion specifically names TMPRSS2 isoform O15393-2. Its isoform-specific sequence, assayed region and orientation must be checked rather than substituted with the canonical protein or interpreted as a BMP10-processing mechanism. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to FFAR2 (UniProtKB:O15552); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names FFAR2 (UniProtKB:O15552), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For FFAR2, receptor classification alone does not identify which surface the BMP10 construct contacted. An extracellularly accessible receptor domain would not be excluded solely because the receptor spans a membrane; the actual BMP10-binding surface has not been mapped here. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TNFSF14 (UniProtKB:O43557); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TNFSF14 (UniProtKB:O43557), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TNFSF14 (O43557), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to COQ9 (UniProtKB:O75208); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names COQ9 (UniProtKB:O75208), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. The cached COQ9 record annotates mitochondrial localization, creating a substantial compartment concern for a normally secreted BMP10 ligand. It does not establish that this particular binary-screen result is false: construct boundaries, targeting sequences and a physiological encounter remain unverified. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to DEXI (UniProtKB:O95424); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names DEXI (UniProtKB:O95424), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For DEXI (O95424), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to CLDN7 (UniProtKB:O95471); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names CLDN7 (UniProtKB:O95471), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For CLDN7 (O95471), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SLC4A1 (UniProtKB:P02730); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SLC4A1 (UniProtKB:P02730), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For SLC4A1 (P02730), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to GJB1 (UniProtKB:P08034); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names GJB1 (UniProtKB:P08034), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For GJB1 (P08034), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to FCGR1A (UniProtKB:P12314); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names FCGR1A (UniProtKB:P12314), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For FCGR1A (P12314), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to CD33 (UniProtKB:P20138); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names CD33 (UniProtKB:P20138), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For CD33 (P20138), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to KLRC1 (UniProtKB:P26715); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names KLRC1 (UniProtKB:P26715), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For KLRC1, the exact receptor fragment, membrane orientation and BMP10 species in the assay need to be checked. The receptor name is neither proof of a BMP10 signaling role nor sufficient evidence that an interaction is impossible. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to IL3RA (UniProtKB:P26951); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names IL3RA (UniProtKB:P26951), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For IL3RA (P26951), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to ERP29 (UniProtKB:P30040); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names ERP29 (UniProtKB:P30040), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For ERP29 (P30040), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TNFSF8 (UniProtKB:P32971); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TNFSF8 (UniProtKB:P32971), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TNFSF8 (P32971), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to KIR2DL3 (UniProtKB:P43628); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names KIR2DL3 (UniProtKB:P43628), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. The UniProt P43628 topology record includes an extracellular domain, so a universal compartment-impossibility argument is inappropriate for KIR2DL3. Whether the HuRI construct contains that domain and whether BMP10 binds it physiologically remain unresolved. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to KIR3DL1 (UniProtKB:P43629); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names KIR3DL1 (UniProtKB:P43629), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For KIR3DL1 (P43629), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TCTA (UniProtKB:P57738); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TCTA (UniProtKB:P57738), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TCTA (P57738), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TSPAN31 (UniProtKB:Q12999); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TSPAN31 (UniProtKB:Q12999), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TSPAN31 (Q12999), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to BIK (UniProtKB:Q13323); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names BIK (UniProtKB:Q13323), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For BIK (Q13323), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to AQP6 (UniProtKB:Q13520); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names AQP6 (UniProtKB:Q13520), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For AQP6 (Q13520), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SLC10A1 (UniProtKB:Q14973); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SLC10A1 (UniProtKB:Q14973), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For SLC10A1 (Q14973), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to EBP (UniProtKB:Q15125); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names EBP (UniProtKB:Q15125), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For EBP (Q15125), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SLC10A6 (UniProtKB:Q3KNW5); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SLC10A6 (UniProtKB:Q3KNW5), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For SLC10A6 (Q3KNW5), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to ARL13B (UniProtKB:Q3SXY8); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names ARL13B (UniProtKB:Q3SXY8), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For ARL13B (Q3SXY8), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to FAM209A (UniProtKB:Q5JX71); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names FAM209A (UniProtKB:Q5JX71), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For FAM209A (Q5JX71), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to PLPP4 (UniProtKB:Q5VZY2); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names PLPP4 (UniProtKB:Q5VZY2), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For PLPP4 (Q5VZY2), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to CCDC70 (UniProtKB:Q6NSX1); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names CCDC70 (UniProtKB:Q6NSX1), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For CCDC70 (Q6NSX1), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to GGT6 (UniProtKB:Q6P531); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names GGT6 (UniProtKB:Q6P531), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For GGT6 (Q6P531), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to APOA5 (UniProtKB:Q6Q788); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names APOA5 (UniProtKB:Q6Q788), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For APOA5 (Q6Q788), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to LRRC25 (UniProtKB:Q8N386); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names LRRC25 (UniProtKB:Q8N386), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For LRRC25 (Q8N386), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to CISD2 (UniProtKB:Q8N5K1); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names CISD2 (UniProtKB:Q8N5K1), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For CISD2 (Q8N5K1), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to JAGN1 (UniProtKB:Q8N5M9); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names JAGN1 (UniProtKB:Q8N5M9), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For JAGN1 (Q8N5M9), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TMEM86B (UniProtKB:Q8N661); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TMEM86B (UniProtKB:Q8N661), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TMEM86B (Q8N661), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to FNDC9 (UniProtKB:Q8TBE3); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names FNDC9 (UniProtKB:Q8TBE3), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For FNDC9 (Q8TBE3), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to GPR152 (UniProtKB:Q8TDT2); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names GPR152 (UniProtKB:Q8TDT2), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For GPR152 (Q8TDT2), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to GPX8 (UniProtKB:Q8TED1); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names GPX8 (UniProtKB:Q8TED1), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For GPX8 (Q8TED1), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to BSND (UniProtKB:Q8WZ55); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names BSND (UniProtKB:Q8WZ55), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For BSND (Q8WZ55), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TMEM45B (UniProtKB:Q96B21); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TMEM45B (UniProtKB:Q96B21), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TMEM45B (Q96B21), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to CREB3L1 (UniProtKB:Q96BA8); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names CREB3L1 (UniProtKB:Q96BA8), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For CREB3L1 (Q96BA8), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to MS4A3 (UniProtKB:Q96HJ5); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names MS4A3 (UniProtKB:Q96HJ5), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For MS4A3 (Q96HJ5), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to FCRL4 (UniProtKB:Q96PJ5); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names FCRL4 (UniProtKB:Q96PJ5), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For FCRL4 (Q96PJ5), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SLC38A1 (UniProtKB:Q9H2H9); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SLC38A1 (UniProtKB:Q9H2H9), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For SLC38A1 (Q9H2H9), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to MTIF3 (UniProtKB:Q9H2K0); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names MTIF3 (UniProtKB:Q9H2K0), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. The MTIF3 mitochondrial-translation context raised in the review warrants a construct and compartment check. The assayed targeting sequence and BMP10 species have not been inspected, and the screen alone does not demonstrate a physiological interaction or prove an artifact. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to REEP4 (UniProtKB:Q9H6H4); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names REEP4 (UniProtKB:Q9H6H4), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For REEP4 (Q9H6H4), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to VSIR (UniProtKB:Q9H7M9); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names VSIR (UniProtKB:Q9H7M9), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For VSIR (Q9H7M9), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to LRRC4C (UniProtKB:Q9HCJ2); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names LRRC4C (UniProtKB:Q9HCJ2), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For LRRC4C (Q9HCJ2), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SPAG4 (UniProtKB:Q9NPE6); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SPAG4 (UniProtKB:Q9NPE6), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For SPAG4 (Q9NPE6), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SLC35C2 (UniProtKB:Q9NQQ7-3); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SLC35C2 (UniProtKB:Q9NQQ7-3), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. The assertion specifically names SLC35C2 isoform Q9NQQ7-3. Its construct and isoform-specific topology have not been inspected; the canonical protein cannot silently substitute for this partner. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to TMEM14B (UniProtKB:Q9NUH8); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names TMEM14B (UniProtKB:Q9NUH8), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For TMEM14B (Q9NUH8), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to SIT1 (UniProtKB:Q9Y3P8); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names SIT1 (UniProtKB:Q9Y3P8), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For SIT1 (Q9Y3P8), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to MRPS18B (UniProtKB:Q9Y676); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names MRPS18B (UniProtKB:Q9Y676), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. The MRPS18B mitochondrial-ribosome context raises a compartment concern for secreted BMP10. Neither the tested construct boundaries nor a physiological route of encounter were established in the material examined; this is a reason for uncertainty, not a demonstrated false interaction. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: HuRI reports BMP10 binding to FKBP7 (UniProtKB:Q9Y680); interpretation of the specific assay remains unresolved.

Reason: The source IPI tuple names FKBP7 (UniProtKB:Q9Y680), also recorded in the cached BMP10 UniProt interaction list. Those records can share HuRI provenance and are not independent confirmation. For FKBP7 (Q9Y680), neither the exact assayed region nor its accessibility to the BMP10 precursor, prodomain or processed growth-factor chain has been independently established. No partner-specific physiological interaction or signaling role is inferred from the database match. The HuRI methods describe binary screening, retesting and sequence confirmation, but the exact BMP10/partner constructs, pair-specific supplementary record and any orthogonal validation have not been independently read. It is therefore unclear how the assay relates to the processed extracellular BMP10 species. UNDECIDED records that evidence limit; generic wording and topology alone do not justify REMOVE.

Summary: BMP10 acts as a secreted extracellular ligand.

Reason: The inherited/electronic extracellular localization agrees with BMP10 secretion and extracellular activity in PMID:17921333, receptor activation in PMID:16049014 and PMID:17068149, and the secreted precursor architecture in UniProt. Target inclusion in the PAINT evidence is expected and is not circular.

Summary: The cited study detects extracellular secretion of BMP10.

Reason: PMID:17921333 explicitly reports extracellular secretion and an effect of BMP10-containing conditioned medium. Extracellular location is central to the ligand activity; detailed intracellular localization is considered separately.

Summary: BMP10 acts as a secreted extracellular ligand.

Reason: The inherited/electronic extracellular localization agrees with BMP10 secretion and extracellular activity in PMID:17921333, receptor activation in PMID:16049014 and PMID:17068149, and the secreted precursor architecture in UniProt. Target inclusion in the PAINT evidence is expected and is not circular.

Summary: Fibrillin-associated BMP10 is present in the extracellular environment.

Reason: Reactome:R-HSA-2396399 describes binding of BMP10 prodomain by fibrillins as extracellular targeting. The PMID:18339631 abstract independently supports BMP10 prodomain–fibrillin-1 binding. Retain the extracellular location without inferring a distinct splice isoform.

Summary: BMP10 binds the extracellular portion of its receptor complex.

Reason: Reactome:R-HSA-8858369 records BMP10 binding to ACVRL1 and an activin type-II receptor. This ligand–receptor event takes place extracellularly and agrees with PMID:17068149. Statements explicitly limited to BMP9 in the Reactome summary are not attributed to BMP10.

Summary: Human heart immunostaining supports contextual cytoplasmic BMP10 localization.

Reason: PMID:17921333 Figure 1 reports striated cytoplasmic staining. Finer localization lacked ultrastructural or fractionation confirmation; retain the broad experimental location as non-core.

Summary: The detailed adult heart development assertion is not established by the accessible expression-study abstract.

Reason: The original PMID:10072785 abstract supplies expression context. PMID:16798733 establishes a postnatal hypertrophic-growth effect, but the precise developmental interval and donor experiment intended by this adult-heart assertion remain unresolved. Retain UNDECIDED without claiming that postnatal growth has no relationship to adult heart development.

Summary: The detailed adult heart development assertion is not established by the accessible expression-study abstract.

Reason: The original PMID:10072785 abstract supplies expression context. PMID:16798733 establishes a postnatal hypertrophic-growth effect, but the precise developmental interval and donor experiment intended by this adult-heart assertion remain unresolved. Retain UNDECIDED without claiming that postnatal growth has no relationship to adult heart development.

Summary: BMP10 possesses growth-factor activity as a secreted receptor agonist.

Reason: The PMID:19903896 abstract establishes the ALK1-ligand signaling context but does not identify every ligand-specific experiment. The activity itself is well supported by BMP10 receptor activation in PMID:16049014 and conditioned-medium hypertrophy in PMID:17921333, so retain the existing activity while deferring to the original curator on this experiment. Endothelial growth inhibition does not negate context-dependent growth-factor activity. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: The growth-factor family mapping is consistent with direct BMP10 activity.

Reason: The TGF-beta growth-factor domain mapping agrees with receptor/SMAD activation by recombinant BMP10 (PMID:16049014) and the cardiomyocyte response to secreted BMP10 (PMID:17921333). This describes the core extracellular ligand activity rather than an enzymatic reaction. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: Cell-surface BMP10 was reported in the telethonin/cardiomyocyte study.

Reason: The PMID:17921333 abstract explicitly reports BMP10 at the cardiomyocyte cell surface. Retain this experimental location as contextual localization; it does not establish that BMP10 is an integral membrane protein.

Summary: BMP10 inhibits endothelial wound closure in the reported migration assay.

Reason: PMID:17068149 Figure 6D follows wound closure of HMVEC-d endothelial monolayers exposed to BMP10 under low-serum conditions. This directly supports the authors' migration interpretation and the existing endothelial-specific annotation, while wound closure can also be affected by cell abundance. Retain this contextual response as non-core. The separate Figure 6E WST-1 measurement does not by itself establish a change in individual-cell size or isolate a proliferation mechanism. No BMP9-only receptor-depletion experiment is transferred.

Summary: BMP10 signaling can regulate cardiac hypertrophic responses.

Reason: The broad ARBA prediction is consistent with the BMP10-dependent conditioned-medium hypertrophy described in PMID:17921333. Retain the contextual cardiac process without expanding the electronic assertion to every form of hypertrophy.

Summary: BMP10 promotes hypertrophy of rat neonatal cardiomyocytes in the cited context.

Reason: PMID:17921333 reports that medium from BMP10-expressing cells induces hypertrophy in rat neonatal cardiomyocytes and that increased secretion by a human BMP10 variant enhances the effect. This supports the specific positive-regulation context. The rat donor assertion is not treated as a direct in vivo human experiment.

Summary: BMP10 promotes hypertrophy of rat neonatal cardiomyocytes in the cited context.

Reason: PMID:17921333 reports that medium from BMP10-expressing cells induces hypertrophy in rat neonatal cardiomyocytes and that increased secretion by a human BMP10 variant enhances the effect. This supports the specific positive-regulation context. The rat donor assertion is not treated as a direct in vivo human experiment.

Summary: BMP10 can limit postnatal cardiomyocyte enlargement.

Reason: Myocardial overexpression in mice reduced developmental hypertrophy while load-induced responses remained intact. Retain this context-dependent signaling outcome as non-core. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: BMP10 can limit postnatal cardiomyocyte enlargement.

Reason: Myocardial overexpression in mice reduced developmental hypertrophy while load-induced responses remained intact. Retain this context-dependent signaling outcome as non-core. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: BMP10 localization at the cardiomyocyte Z disc was reported with telethonin binding.

Reason: The PMID:17921333 abstract explicitly places BMP10 at the stretch-sensing Z disc. Preserve this contextual localization without asserting that BMP10 itself supplies the structural scaffold of the sarcomere.

Summary: BMP10 reduces the endothelial growth readout, but the measured endpoint does not resolve cell enlargement versus proliferation or survival.

Reason: PMID:17068149 describes inhibition of endothelial growth; Figure 6E measures WST-1 absorbance as viable-cell abundance after 24 and 48 hours of BMP10 treatment. This supports the reported growth phenotype but does not measure individual-cell enlargement, which GO:0030308 regulates, or distinguish cell proliferation from survival and metabolic changes. The suggestion to replace it with GO:0001937 is plausible but not established by that endpoint alone. Retain UNDECIDED because the interpretation and appropriate replacement remain uncertain, not because the caption was inaccessible. Figure 6D separately measures wound closure, so accepting its migration interpretation does not require treating WST-1 as a division assay.

Summary: The reported migration response is specifically measured in endothelial cells.

Reason: PMID:17068149 Figure 6D measures reduced wound closure in BMP10-treated HMVEC-d endothelial monolayers under low-serum conditions. Refine the generic migration-regulation term to GO:0010596, which is already represented by an existing assertion from this paper. This preserves the source assertion while naming the tested cell context; it does not add an independent experiment or a new process. Wound closure is a migration proxy rather than an isolated measurement of motility unaffected by cell abundance.

Proposed replacements: negative regulation of endothelial cell migration

Summary: The phylogenetic BMP-signaling assignment agrees with direct BMP10 ligand experiments.

Reason: PMID:16049014 and PMID:17068149 demonstrate BMP10 receptor activation and BMP/SMAD responses. BMP10 performs the extracellular ligand step of this pathway. The target is legitimately among the evidence sources for the PAINT ancestral assertion; this is not circular transfer. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: Recombinant BMP10 activates BMP receptors and downstream SMAD1 signaling.

Reason: The PMID:16049014 abstract describes BMP10 activity in MC3T3 cells and receptor-transfected COS7 cells, including SMAD1/5/8-responsive reporters, SMAD1 phosphorylation, and receptor perturbations. BMP10 contributes the activating ligand step of BMP signaling. Both seeded assertions are preserved as provided. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: Recombinant BMP10 activates BMP receptors and downstream SMAD1 signaling.

Reason: The PMID:16049014 abstract describes BMP10 activity in MC3T3 cells and receptor-transfected COS7 cells, including SMAD1/5/8-responsive reporters, SMAD1 phosphorylation, and receptor perturbations. BMP10 contributes the activating ligand step of BMP signaling. Both seeded assertions are preserved as provided. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: BMP10 is an ALK1 ligand that initiates BMP-pathway signaling.

Reason: The PMID:17068149 abstract directly identifies BMP10 as a potent ALK1 ligand and describes shared endothelial responses. The pathway is central to BMP10 function. The detailed BMP9 time course and potency measurements are not asserted for BMP10. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: BMP10 ligand activity is consistent with the cited ALK1 signaling study.

Reason: PMID:19903896 describes ALK1-ligand stimulation of lymphatic endothelial cells. The accessible abstract does not resolve every BMP10-specific experiment, but the BMP-signaling function is independently established by PMID:16049014 and PMID:17068149. Retain the correct function and defer to the original experimental curation rather than infer misattribution. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: The mouse-to-human BMP-signaling transfer is independently supported in BMP10 receptor assays.

Reason: The ortholog inference is consistent with BMP10 functioning as a BMP ligand in PMID:16049014 and PMID:17068149; no target-specific loss of this signaling function is apparent. PMID:39921464 section3.2 independently shows SMAD1/5/9 responses to processed BMP10 in HUVEC and C2C12 cells, whereas the unprocessed precursor did not signal above baseline in those assays.

Summary: BMP10 binds telethonin in a cardiac secretion/hypertrophy context.

Reason: PMID:17921333 directly reports BMP10–Tcap interaction, reduced interaction by a human variant, and altered secretion. Retain the specific binding activity as non-core regulatory context. It does not establish contractile or sarcomere-structural activity of BMP10 itself.

Summary: BMP10 signaling uses an activin type-II receptor in the reported receptor assays.

Reason: PMID:16049014 reports suppression of BMP10 signaling after ActRIIA depletion. GO:0032924 describes signaling initiated by a ligand binding an activin receptor, rather than requiring an activin-named ligand or SMAD2/3. The existing pathway assertion therefore agrees with the receptor context.

Summary: Independent BMP10 ActRIIA-depletion evidence supports the activin-receptor pathway annotation.

Reason: PMID:17068149 establishes BMP10 activation of ALK1, but the BMPRII/ActRIIA depletion result described there concerns BMP9. ALK1's historical name alone is not evidence for this pathway. The separate PMID:16049014 reports suppression of BMP10 signaling by ActRIIA shRNA in MC3T3 cells, providing BMP10-specific type-II-receptor support for GO:0032924. Retain ACCEPT on that independent functional evidence while preserving the original PMID:17068149 source field; the term does not require an activin-named ligand or SMAD2/3 signaling.

Summary: BMP10 binds a receptor serine/threonine kinase as its extracellular ligand.

Reason: PMID:17068149 identifies BMP10 as a ligand of ACVRL1/ALK1, and Reactome:R-HSA-8858369 records the corresponding binding event. This is receptor binding by BMP10, not kinase activity of BMP10. PMID:35504921 directly resolves binary BMP10:BMPRII and ternary ALK1:BMP10:BMPRII complexes. The receptor components carry kinase activity; BMP10 supplies ligand-binding surfaces.

Summary: BMP10-conditioned medium promoted sarcomeric maturation in cultured cardiomyocytes.

Reason: PMID:17921333 Figure 3 reports sarcomeric maturation in neonatal rat cardiomyocytes exposed to human BMP10-conditioned medium. This contextual outcome does not establish a structural role for BMP10; an indirect secreted mediator remains possible.

Summary: BMP10-conditioned medium promoted sarcomeric maturation in cultured cardiomyocytes.

Reason: PMID:17921333 Figure 3 reports sarcomeric maturation in neonatal rat cardiomyocytes exposed to human BMP10-conditioned medium. This contextual outcome does not establish a structural role for BMP10; an indirect secreted mediator remains possible.

Summary: BMP10 receptor signaling activates transcriptional reporter responses.

Reason: PMID:16049014 explicitly reports activation of SMAD-responsive promoter constructs by BMP10. Retain the downstream transcriptional regulatory outcome as non-core. The evidence does not confer DNA-binding or transcription-factor activity on the secreted BMP10 protein. Independent developmental context comes from PMID:15073151, where BMP10 is required to maintain normal NKX2-5 and MEF2C expression in mouse myocardium. This corroborates signaling-dependent endogenous gene regulation without changing what the original paper measured or making BMP10 a DNA-binding protein.

Summary: BMP10 signaling changes endothelial gene expression.

Reason: PMID:17068149 reports stimulation of an endothelial gene panel by BMP9 and BMP10. Retain this signaling-dependent transcriptional outcome as non-core; BMP10 is the extracellular ligand rather than a DNA-binding transcription factor. Independent developmental context comes from PMID:15073151, where BMP10 is required to maintain normal NKX2-5 and MEF2C expression in mouse myocardium. This corroborates signaling-dependent endogenous gene regulation without changing what the original paper measured or making BMP10 a DNA-binding protein.

Summary: The broad organismal-process regulation term can be refined to the supported cardiac hypertrophic response.

Reason: The near-root ARBA term does not identify which organismal response BMP10 regulates. PMID:17921333 provides independent support for a cardiac hypertrophic response to BMP10-containing conditioned medium in neonatal rat cardiomyocytes. Refine to GO:0010613, already present among the reviewed assertions, without claiming reconstruction of the ARBA training provenance. This contextual effect is not a universal BMP10 response: PMID:16798733 reports reduced postnatal cardiomyocyte enlargement under myocardial overexpression. The refinement preserves a supported specific outcome rather than treating broadness as biological falsity.

Proposed replacements: positive regulation of cardiac muscle hypertrophy

Summary: The detailed atrial cardiac muscle tissue morphogenesis assertion is not established by the accessible expression-study abstract.

Reason: The inspected PMID:15073151 knockout/rescue material establishes ventricular growth and general chamber maturation. Atrial expression alone does not resolve this atrial-specific morphogenetic assertion, and the exact donor experiment remains unverified. Retain UNDECIDED without inferring that BMP10 lacks an atrial role.

Summary: The detailed atrial cardiac muscle tissue morphogenesis assertion is not established by the accessible expression-study abstract.

Reason: The inspected PMID:15073151 knockout/rescue material establishes ventricular growth and general chamber maturation. Atrial expression alone does not resolve this atrial-specific morphogenetic assertion, and the exact donor experiment remains unverified. Retain UNDECIDED without inferring that BMP10 lacks an atrial role.

Summary: Mouse evidence supports BMP10-dependent ventricular tissue growth.

Reason: Knockout histology showed thin ventricular walls and defective trabecular expansion. Ligand rescue supports a signaling contribution; retain the developmental outcome as non-core. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: Mouse evidence supports BMP10-dependent ventricular tissue growth.

Reason: Knockout histology showed thin ventricular walls and defective trabecular expansion. Ligand rescue supports a signaling contribution; retain the developmental outcome as non-core. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: BMP10 signaling modulates ventricular cardiomyocyte maturation.

Reason: Postnatal ventricular overexpression altered cardiomyocyte enlargement without reactivating division. This supports a developmental signaling role, not BMP10 performing contractile-cell differentiation. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: BMP10 signaling modulates ventricular cardiomyocyte maturation.

Reason: Postnatal ventricular overexpression altered cardiomyocyte enlargement without reactivating division. This supports a developmental signaling role, not BMP10 performing contractile-cell differentiation. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: The specific BMP10 effect on cardiac contraction has not been verified.

Reason: The PMID:17921333 abstract describes hypertrophy, secretion, localization and telethonin binding, but not the contraction assay behind this annotation. A change in hypertrophy is not by itself a measurement of contraction. Preserve the experimental assertion as unresolved pending full-text review.

Summary: BMP10 signaling supports embryonic cardiomyocyte proliferation.

Reason: Mouse knockout and conditioned-medium rescue support proliferative activity. Retain the broad process as non-core; the ligand provides signaling rather than division machinery. This is independent corroboration; the original donor-reference edge remains unverified. PMID:15073151 also links the mouse knockout phenotype to ectopic/elevated CDKN1C/p57KIP2 and reduced maintenance of NKX2-5 and MEF2C expression at mid-gestation. These observations connect BMP10 signaling to cell-cycle restraint and cardiogenic gene expression; they do not establish direct promoter binding by BMP10 or prove that any one expression change alone mediates the entire phenotype.

Summary: BMP10 signaling supports embryonic cardiomyocyte proliferation.

Reason: Mouse knockout and conditioned-medium rescue support proliferative activity. Retain the broad process as non-core; the ligand provides signaling rather than division machinery. This is independent corroboration; the original donor-reference edge remains unverified. PMID:15073151 also links the mouse knockout phenotype to ectopic/elevated CDKN1C/p57KIP2 and reduced maintenance of NKX2-5 and MEF2C expression at mid-gestation. These observations connect BMP10 signaling to cell-cycle restraint and cardiogenic gene expression; they do not establish direct promoter binding by BMP10 or prove that any one expression change alone mediates the entire phenotype.

Summary: BMP10 promotes embryonic cardiomyocyte proliferation.

Reason: Conditioned medium and feeder-cell assays increased thymidine labeling; knockout reduced proliferation. Retain this downstream developmental signaling effect as non-core. This is independent corroboration; the original donor-reference edge remains unverified. PMID:15073151 also links the mouse knockout phenotype to ectopic/elevated CDKN1C/p57KIP2 and reduced maintenance of NKX2-5 and MEF2C expression at mid-gestation. These observations connect BMP10 signaling to cell-cycle restraint and cardiogenic gene expression; they do not establish direct promoter binding by BMP10 or prove that any one expression change alone mediates the entire phenotype.

Summary: BMP10 promotes embryonic cardiomyocyte proliferation.

Reason: Conditioned medium and feeder-cell assays increased thymidine labeling; knockout reduced proliferation. Retain this downstream developmental signaling effect as non-core. This is independent corroboration; the original donor-reference edge remains unverified. PMID:15073151 also links the mouse knockout phenotype to ectopic/elevated CDKN1C/p57KIP2 and reduced maintenance of NKX2-5 and MEF2C expression at mid-gestation. These observations connect BMP10 signaling to cell-cycle restraint and cardiogenic gene expression; they do not establish direct promoter binding by BMP10 or prove that any one expression change alone mediates the entire phenotype.

Summary: BMP10-conditioned medium promoted sarcomeric maturation in cultured cardiomyocytes.

Reason: PMID:17921333 Figure 3 reports sarcomeric maturation in neonatal rat cardiomyocytes exposed to human BMP10-conditioned medium. This contextual outcome does not establish a structural role for BMP10; an indirect secreted mediator remains possible.

Summary: BMP10 supports expansion of cardiac trabecular myocardium.

Reason: Selected Results and Figures 3-4 distinguish defective trabecular growth from preserved primitive initiation. Retain the morphogenetic signaling contribution as non-core. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: BMP10 supports expansion of cardiac trabecular myocardium.

Reason: Selected Results and Figures 3-4 distinguish defective trabecular growth from preserved primitive initiation. Retain the morphogenetic signaling contribution as non-core. This is independent corroboration; the original donor-reference edge remains unverified.

Summary: BMP10 increases SMAD pathway activity following receptor engagement.

Reason: PMID:16049014 reports SMAD1 phosphorylation and activation of SMAD1/5/8-responsive promoters by BMP10. This is the downstream effect of the core BMP10 ligand activity, not direct phosphorylation catalyzed by BMP10.

Summary: BMP10 ALK1 signaling is consistent with activation of the BMP/SMAD pathway.

Reason: The PMID:17068149 abstract explicitly identifies BMP10 as an ALK1 ligand, while much of its detailed SMAD time-course description concerns BMP9. BMP10-dependent SMAD activation is independently supported by PMID:16049014; retain the correct function while deferring to the original curator on the BMP10-specific assay in the cited paper.

Summary: BMP10-dependent receptor signaling activates the SMAD pathway.

Reason: The PMID:19903896 abstract describes ALK1-ligand responsiveness but does not give every ligand-specific SMAD experiment. The function is independently supported by PMID:16049014, so retain the existing annotation without representing the abstract as a complete experiment-level verification.

Summary: The ortholog SMAD-signaling transfer is corroborated by direct BMP10 ligand experiments.

Reason: PMID:16049014 directly demonstrates SMAD1 phosphorylation and SMAD-responsive transcription following BMP10 stimulation. This independently supports the biological function inferred from mouse Bmp10.

Summary: The ortholog SMAD-signaling transfer is corroborated by direct BMP10 ligand experiments.

Reason: PMID:16049014 directly demonstrates SMAD1 phosphorylation and SMAD-responsive transcription following BMP10 stimulation. This independently supports the biological function inferred from mouse Bmp10.

Summary: The mouse-source cartilage-development assertion has not been evaluated.

Reason: The source is the mouse BMP10 ortholog Q9R229, but the corresponding cartilage experiment was not available in the examined material. Membership in the BMP family or evidence from other BMP paralogs cannot independently establish this BMP10-specific process. There is no direct contradictory evidence warranting removal.

Summary: BMP10 ligand binding regulates receptor serine/threonine kinase signaling.

Reason: The broad electronic annotation agrees with direct receptor-dependent BMP10 responses in PMID:16049014 and PMID:17068149. This refers to regulation of a receptor pathway and does not assign protein kinase activity to the ligand.

Summary: BMP10 has a reported role in hypertrophic responses under hypertensive stress.

Reason: PMID:17921333 reports increased BMP10 expression in hypertensive rat ventricles and BMP10-dependent hypertrophy in neonatal cardiomyocyte assays. Retain this defined contextual response as non-core, without claiming that the abstract establishes every in vivo stress-response mechanism.

Summary: BMP10 promotes proliferation during embryonic heart morphogenesis.

Reason: Knockout and ligand-rescue experiments connect cardiomyocyte proliferation with chamber growth. Retain this developmental signaling outcome as non-core. This is independent corroboration; the original donor-reference edge remains unverified. PMID:15073151 also links the mouse knockout phenotype to ectopic/elevated CDKN1C/p57KIP2 and reduced maintenance of NKX2-5 and MEF2C expression at mid-gestation. These observations connect BMP10 signaling to cell-cycle restraint and cardiogenic gene expression; they do not establish direct promoter binding by BMP10 or prove that any one expression change alone mediates the entire phenotype.

Summary: BMP10 promotes proliferation during embryonic heart morphogenesis.

Reason: Knockout and ligand-rescue experiments connect cardiomyocyte proliferation with chamber growth. Retain this developmental signaling outcome as non-core. This is independent corroboration; the original donor-reference edge remains unverified. PMID:15073151 also links the mouse knockout phenotype to ectopic/elevated CDKN1C/p57KIP2 and reduced maintenance of NKX2-5 and MEF2C expression at mid-gestation. These observations connect BMP10 signaling to cell-cycle restraint and cardiogenic gene expression; they do not establish direct promoter binding by BMP10 or prove that any one expression change alone mediates the entire phenotype.