AFAP1L2 (XB130) is a cytoplasmic adaptor that couples Src-family kinase signaling to downstream phosphorylation, transcriptional responses and cell-cycle progression. Its N-terminal SH2/SH3-binding motifs and pleckstrin homology domains organize interactions with signaling proteins. It promotes Src activation and EGF-linked Akt signaling, with context-dependent effects on epithelial cytokine production.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | ACCEPT | Summary: AFAP1L2 is a cytoplasmic signaling adaptor. Reason: The original characterization and curated localization place XB130 in the cytoplasm, where it engages Src-family signaling. The cytosolic and vocabulary mappings are compatible with that mechanistic role. Supporting Evidence: file:human/AFAP1L2/AFAP1L2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm PMID:17412687 Their co-expression in COS-7 cells resulted in activation of c-Src and elevated tyrosine phosphorylation of multiple proteins, including XB130 itself. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: AFAP1L2 is a cytoplasmic signaling adaptor. Reason: The original characterization and curated localization place XB130 in the cytoplasm, where it engages Src-family signaling. The cytosolic and vocabulary mappings are compatible with that mechanistic role. Supporting Evidence: file:human/AFAP1L2/AFAP1L2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm PMID:17412687 Their co-expression in COS-7 cells resulted in activation of c-Src and elevated tyrosine phosphorylation of multiple proteins, including XB130 itself. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: AFAP1L2 is a cytoplasmic signaling adaptor. Reason: The original characterization and curated localization place XB130 in the cytoplasm, where it engages Src-family signaling. The cytosolic and vocabulary mappings are compatible with that mechanistic role. Supporting Evidence: file:human/AFAP1L2/AFAP1L2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm PMID:17412687 Their co-expression in COS-7 cells resulted in activation of c-Src and elevated tyrosine phosphorylation of multiple proteins, including XB130 itself. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: AFAP1L2 is a cytoplasmic signaling adaptor. Reason: The original characterization and curated localization place XB130 in the cytoplasm, where it engages Src-family signaling. The cytosolic and vocabulary mappings are compatible with that mechanistic role. Supporting Evidence: file:human/AFAP1L2/AFAP1L2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm PMID:17412687 Their co-expression in COS-7 cells resulted in activation of c-Src and elevated tyrosine phosphorylation of multiple proteins, including XB130 itself. |
| GO:0006954 inflammatory response | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: XB130 can regulate epithelial inflammatory outputs. Reason: The primary study measures altered IL-8 and IL-6 release after XB130 depletion. Retain inflammatory-response participation as a context-dependent downstream role rather than the core molecular identity of the adaptor. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. file:human/AFAP1L2/AFAP1L2-Xu2007-excerpt.md In addition to IL-8, the protein level of IL-6 was also reduced by siRNA treatment. |
| GO:0006954 inflammatory response | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | KEEP AS NON CORE | Summary: XB130 can regulate epithelial inflammatory outputs. Reason: The primary study measures altered IL-8 and IL-6 release after XB130 depletion. Retain inflammatory-response participation as a context-dependent downstream role rather than the core molecular identity of the adaptor. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. file:human/AFAP1L2/AFAP1L2-Xu2007-excerpt.md In addition to IL-8, the protein level of IL-6 was also reduced by siRNA treatment. |
| GO:0007346 regulation of mitotic cell cycle | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: XB130 affects cell-cycle progression downstream of growth-factor signaling. Reason: Knockdown changes epithelial cell-cycle distributions alongside reduced Akt signaling. This supports participation in cell-cycle regulation, but does not make AFAP1L2 a core cell-cycle enzyme. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0007346 regulation of mitotic cell cycle | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | KEEP AS NON CORE | Summary: XB130 affects cell-cycle progression downstream of growth-factor signaling. Reason: Knockdown changes epithelial cell-cycle distributions alongside reduced Akt signaling. This supports participation in cell-cycle regulation, but does not make AFAP1L2 a core cell-cycle enzyme. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0017124 SH3 domain binding | IPI PMID:17412687 XB130, a novel adaptor protein for signal transduction. | ACCEPT | Summary: SH2/SH3-binding motifs mediate AFAP1L2 signaling interactions. Reason: The original study characterizes Src interaction and loss of signaling upon deletion of the N-terminal motif-rich region. These specific binding annotations describe the adaptor mechanism; they do not imply AFAP1L2 contains an SH2 or SH3 domain. Supporting Evidence: PMID:17412687 XB130DeltaN, an N-terminal deletion mutant lacking a putative SH3-binding motif and several putative SH2-binding sites, reduced its ability to mediate Src signal transduction. |
| GO:0030296 protein tyrosine kinase activator activity | IBA GO_REF:0000033 | ACCEPT | Summary: AFAP1L2 promotes Src tyrosine kinase activity. Reason: Coexpression increases Src activation and protein tyrosine phosphorylation; depletion reduces endogenous Src activity. The activator term distinguishes this adaptor from a catalytic kinase. Supporting Evidence: PMID:17412687 Their co-expression in COS-7 cells resulted in activation of c-Src and elevated tyrosine phosphorylation of multiple proteins, including XB130 itself. PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0030296 protein tyrosine kinase activator activity | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | ACCEPT | Summary: AFAP1L2 promotes Src tyrosine kinase activity. Reason: Coexpression increases Src activation and protein tyrosine phosphorylation; depletion reduces endogenous Src activity. The activator term distinguishes this adaptor from a catalytic kinase. Supporting Evidence: PMID:17412687 Their co-expression in COS-7 cells resulted in activation of c-Src and elevated tyrosine phosphorylation of multiple proteins, including XB130 itself. PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0032675 regulation of interleukin-6 production | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | KEEP AS NON CORE | Summary: XB130 depletion reduces IL-6 release in airway epithelial cells. Reason: The full Results text reports the IL-6 reduction in the multiplex cytokine assay. This supports regulation of IL-6 production in that context; the abstract-only PMID cache omits this detail, so the inspected source excerpt is recorded separately. Supporting Evidence: file:human/AFAP1L2/AFAP1L2-Xu2007-excerpt.md In addition to IL-8, the protein level of IL-6 was also reduced by siRNA treatment. |
| GO:0032757 positive regulation of interleukin-8 production | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | KEEP AS NON CORE | Summary: XB130 promotes IL-8 output in airway epithelial cells. Reason: The original siRNA experiment reduces IL-8 production, supporting positive regulation in the assayed human epithelial cells. This is a downstream signaling output, not an intrinsic cytokine-producing molecular activity. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0042169 SH2 domain binding | IPI PMID:17412687 XB130, a novel adaptor protein for signal transduction. | ACCEPT | Summary: SH2/SH3-binding motifs mediate AFAP1L2 signaling interactions. Reason: The original study characterizes Src interaction and loss of signaling upon deletion of the N-terminal motif-rich region. These specific binding annotations describe the adaptor mechanism; they do not imply AFAP1L2 contains an SH2 or SH3 domain. Supporting Evidence: PMID:17412687 XB130DeltaN, an N-terminal deletion mutant lacking a putative SH3-binding motif and several putative SH2-binding sites, reduced its ability to mediate Src signal transduction. |
| GO:0045742 positive regulation of epidermal growth factor receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: AFAP1L2 supports EGF-responsive downstream signaling. Reason: XB130 depletion reduces EGF-induced Akt and GSK3beta phosphorylation. Its adaptor activity therefore participates in propagation of receptor signaling without acting as the receptor itself. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0045742 positive regulation of epidermal growth factor receptor signaling pathway | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | ACCEPT | Summary: AFAP1L2 supports EGF-responsive downstream signaling. Reason: XB130 depletion reduces EGF-induced Akt and GSK3beta phosphorylation. Its adaptor activity therefore participates in propagation of receptor signaling without acting as the receptor itself. Supporting Evidence: PMID:17412687 Down-regulation of endogenous XB130 with siRNA reduced c-Src activity, IL-8 production, EGF-induced phosphorylation of Akt and GSK3beta, and altered cell cycles in human lung epithelial cells. |
| GO:0045893 positive regulation of DNA-templated transcription | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: AFAP1L2 enhances Src-dependent transcriptional responses. Reason: The SRE and AP-1 reporter results support positive regulation of transcription as a downstream effect of cytoplasmic signaling. They do not imply DNA binding or direct transcription-factor activity. Supporting Evidence: PMID:17412687 XB130 expression in HEK293 cells enhanced serum response element- and AP-1-dependent transcriptional activation mediated by c-Src. |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:17412687 XB130, a novel adaptor protein for signal transduction. | KEEP AS NON CORE | Summary: AFAP1L2 enhances Src-dependent transcriptional responses. Reason: The SRE and AP-1 reporter results support positive regulation of transcription as a downstream effect of cytoplasmic signaling. They do not imply DNA binding or direct transcription-factor activity. Supporting Evidence: PMID:17412687 XB130 expression in HEK293 cells enhanced serum response element- and AP-1-dependent transcriptional activation mediated by c-Src. |
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