Cd79b encodes Ig-beta, a single-pass membrane signaling subunit of the B-cell antigen receptor. It forms a disulfide-linked heterodimer with Ig-alpha and associates with membrane immunoglobulin, which recognizes antigen. The paired ITAM-containing cytoplasmic tails organize intracellular signaling and support B-cell maturation. Isolated Ig-beta domains can self-associate in biochemical preparations, whereas the physiological receptor signaling unit is the Ig-alpha/Ig-beta heterodimer.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002376 immune system process | IEA GO_REF:0000117 | MODIFY | Summary: The broad process can be specified as B-cell receptor signaling. Reason: The chain performs receptor assembly and ITAM-dependent signal transmission in this specific pathway; the refinement assigns neither kinase catalysis nor a generic function to all immune processes. Proposed replacements: B cell receptor signaling pathway Supporting Evidence: |
| GO:0004888 transmembrane signaling receptor activity | IDA PMID:8626447 Reconstitution of B cell antigen receptor-induced signaling ... | ACCEPT | Summary: The CD79 chain contributes transmembrane signaling within the assembled B-cell receptor. Reason: Membrane immunoglobulin supplies antigen recognition, and the Ig-alpha/Ig-beta heterodimer couples receptor engagement to intracellular effectors. Reconstitution in mouse AtT20 cells demonstrates several signaling outputs after Syk expression, without sufficiency for the entire native B-cell network. Any contributes_to flag is retained and assessed as a complex contribution. |
| GO:0004888 transmembrane signaling receptor activity | IEA GO_REF:0000002 | ACCEPT | Summary: The CD79 chain contributes transmembrane signaling within the assembled B-cell receptor. Reason: Membrane immunoglobulin supplies antigen recognition, and the Ig-alpha/Ig-beta heterodimer couples receptor engagement to intracellular effectors. Reconstitution in mouse AtT20 cells demonstrates several signaling outputs after Syk expression, without sufficiency for the entire native B-cell network. Any contributes_to flag is retained and assessed as a complex contribution. |
| GO:0005515 protein binding | IPI PMID:1373499 The membrane IgM-associated proteins MB-1 and Ig-beta are su... | MODIFY | Summary: The CD79 chains heterodimerize to form the receptor signaling module. Reason: Coexpression and assembly experiments establish the Ig-alpha/Ig-beta pair, so the more informative protein heterodimerization activity captures the reported partner interaction. This does not assign antigen recognition to either isolated chain. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:8626447 Reconstitution of B cell antigen receptor-induced signaling ... | MODIFY | Summary: The CD79 chains heterodimerize to form the receptor signaling module. Reason: Coexpression and assembly experiments establish the Ig-alpha/Ig-beta pair, so the more informative protein heterodimerization activity captures the reported partner interaction. This does not assign antigen recognition to either isolated chain. Proposed replacements: protein heterodimerization activity |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The assembled receptor is expressed at the plasma membrane. Reason: Reconstitution establishes surface expression of the membrane-IgM/Ig-alpha/Ig-beta complex. Independent receptor-assembly evidence corroborates the orthology or curated pathway assignment; intracellular receptor trafficking does not contradict cell-surface residence. Supporting Evidence: url:https://pmc.ncbi.nlm.nih.gov/articles/PMC48876/ |
| GO:0005886 plasma membrane | ISO GO_REF:0000119 | ACCEPT | Summary: The assembled receptor is expressed at the plasma membrane. Reason: Reconstitution establishes surface expression of the membrane-IgM/Ig-alpha/Ig-beta complex. Independent receptor-assembly evidence corroborates the orthology or curated pathway assignment; intracellular receptor trafficking does not contradict cell-surface residence. Supporting Evidence: url:https://pmc.ncbi.nlm.nih.gov/articles/PMC48876/ |
| GO:0005886 plasma membrane | ISO GO_REF:0000119 | ACCEPT | Summary: The assembled receptor is expressed at the plasma membrane. Reason: Reconstitution establishes surface expression of the membrane-IgM/Ig-alpha/Ig-beta complex. Independent receptor-assembly evidence corroborates the orthology or curated pathway assignment; intracellular receptor trafficking does not contradict cell-surface residence. Supporting Evidence: url:https://pmc.ncbi.nlm.nih.gov/articles/PMC48876/ |
| GO:0005886 plasma membrane | TAS Reactome:R-MMU-983702 | ACCEPT | Summary: The assembled receptor is expressed at the plasma membrane. Reason: Reconstitution establishes surface expression of the membrane-IgM/Ig-alpha/Ig-beta complex. Independent receptor-assembly evidence corroborates the orthology or curated pathway assignment; intracellular receptor trafficking does not contradict cell-surface residence. Supporting Evidence: Reactome:R-MMU-983702 url:https://pmc.ncbi.nlm.nih.gov/articles/PMC48876/ |
| GO:0007165 signal transduction | IEA GO_REF:0000117 | MODIFY | Summary: The broad process can be specified as B-cell receptor signaling. Reason: The chain performs receptor assembly and ITAM-dependent signal transmission in this specific pathway; the refinement assigns neither kinase catalysis nor a generic function to all immune processes. Proposed replacements: B cell receptor signaling pathway Supporting Evidence: |
| GO:0007166 cell surface receptor signaling pathway | IEA GO_REF:0000002 | MODIFY | Summary: The broad process can be specified as B-cell receptor signaling. Reason: The chain performs receptor assembly and ITAM-dependent signal transmission in this specific pathway; the refinement assigns neither kinase catalysis nor a generic function to all immune processes. Proposed replacements: B cell receptor signaling pathway Supporting Evidence: |
| GO:0009617 response to bacterium | IEP PMID:23012479 Impact of lactobacilli on orally acquired listeriosis. | UNDECIDED | Summary: The target-specific link from ileal expression changes to a bacterial-response role remains unresolved. Reason: The full study profiles host responses to Lactobacillus and Listeria in gnotobiotic mice. The main text does not resolve Cd79b-specific functional work versus altered abundance of B cells or receptor transcripts. The target-level supplementary expression table could not be recovered from the publisher (403). Its established BCR role makes immune participation plausible, but neither expression alone nor failure to locate the row proves or disproves this particular annotation. Supporting Evidence: |
| GO:0009897 external side of plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The extracellular CD79 domain is exposed on the outside of the plasma membrane. Reason: Surface receptor assembly and the extracellular Ig-domain structure establish this topology. The same protein has a transmembrane segment and cytoplasmic ITAM; the annotation concerns its exposed extracellular region and does not move signaling chemistry outside the cell. |
| GO:0009897 external side of plasma membrane | IDA PMID:1373499 The membrane IgM-associated proteins MB-1 and Ig-beta are su... | ACCEPT | Summary: The extracellular CD79 domain is exposed on the outside of the plasma membrane. Reason: Surface receptor assembly and the extracellular Ig-domain structure establish this topology. The same protein has a transmembrane segment and cytoplasmic ITAM; the annotation concerns its exposed extracellular region and does not move signaling chemistry outside the cell. |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Specify the established plasma-membrane location. Reason: The protein is a single-pass component of the surface BCR, so a specific supported location is available. Proposed replacements: plasma membrane Supporting Evidence: url:https://pmc.ncbi.nlm.nih.gov/articles/PMC48876/ |
| GO:0019815 B cell receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0019815 B cell receptor complex | IDA PMID:1373499 The membrane IgM-associated proteins MB-1 and Ig-beta are su... | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0019815 B cell receptor complex | IDA PMID:8626447 Reconstitution of B cell antigen receptor-induced signaling ... | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0019815 B cell receptor complex | IEA GO_REF:0000120 | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0019815 B cell receptor complex | ISO GO_REF:0000119 | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0030183 B cell differentiation | IBA GO_REF:0000033 | ACCEPT | Summary: Receptor-associated signaling supports B-cell developmental checkpoints. Reason: Native mouse deficiency arrests maturation at the progenitor stage while preserving V(D)J recombination. Ig-alpha ITAM mutation and Ig-beta-tail truncation show context-dependent compensation, not dispensability of the receptor signaling module. The proteins do developmental signaling work, not DNA recombination. |
| GO:0042802 identical protein binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Self-association is supported in purified CD79-domain experiments. Reason: Purified cytoplasmic Ig-alpha/Ig-beta domains oligomerize in PMID14967045; PMID20696394 additionally resolves murine and human Ig-beta ectodomain homodimers. These experiments support the biochemical binding capacity, without replacing the physiological Ig-alpha/Ig-beta signaling heterodimer with an obligatory homomer. |
| GO:0042802 identical protein binding | IPI PMID:20696394 Structural and functional studies of Igalphabeta and its ass... | KEEP AS NON CORE | Summary: Self-association is supported in purified CD79-domain experiments. Reason: Purified cytoplasmic Ig-alpha/Ig-beta domains oligomerize in PMID14967045; PMID20696394 additionally resolves murine and human Ig-beta ectodomain homodimers. These experiments support the biochemical binding capacity, without replacing the physiological Ig-alpha/Ig-beta signaling heterodimer with an obligatory homomer. |
| GO:0042802 identical protein binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Self-association is supported in purified CD79-domain experiments. Reason: Purified cytoplasmic Ig-alpha/Ig-beta domains oligomerize in PMID14967045; PMID20696394 additionally resolves murine and human Ig-beta ectodomain homodimers. These experiments support the biochemical binding capacity, without replacing the physiological Ig-alpha/Ig-beta signaling heterodimer with an obligatory homomer. |
| GO:0050853 B cell receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Ig-alpha/Ig-beta supplies the receptor-proximal signaling module. Reason: Reconstitution and effector-association studies show that the cytoplasmic tails transmit antigen-receptor signals. The 1996 AtT20 experiment required active Syk for several outputs and did not reconstitute phosphoinositide signaling; the existing pathway assignment does not assert sufficiency for all downstream branches. |
| GO:0050853 B cell receptor signaling pathway | IDA PMID:1373499 The membrane IgM-associated proteins MB-1 and Ig-beta are su... | ACCEPT | Summary: Ig-alpha/Ig-beta supplies the receptor-proximal signaling module. Reason: Reconstitution and effector-association studies show that the cytoplasmic tails transmit antigen-receptor signals. The 1996 AtT20 experiment required active Syk for several outputs and did not reconstitute phosphoinositide signaling; the existing pathway assignment does not assert sufficiency for all downstream branches. |
| GO:0050853 B cell receptor signaling pathway | IDA PMID:8626447 Reconstitution of B cell antigen receptor-induced signaling ... | ACCEPT | Summary: Ig-alpha/Ig-beta supplies the receptor-proximal signaling module. Reason: Reconstitution and effector-association studies show that the cytoplasmic tails transmit antigen-receptor signals. The 1996 AtT20 experiment required active Syk for several outputs and did not reconstitute phosphoinositide signaling; the existing pathway assignment does not assert sufficiency for all downstream branches. |
| GO:0050853 B cell receptor signaling pathway | IDA PMID:8626447 Reconstitution of B cell antigen receptor-induced signaling ... | ACCEPT | Summary: Ig-alpha/Ig-beta supplies the receptor-proximal signaling module. Reason: Reconstitution and effector-association studies show that the cytoplasmic tails transmit antigen-receptor signals. The 1996 AtT20 experiment required active Syk for several outputs and did not reconstitute phosphoinositide signaling; the existing pathway assignment does not assert sufficiency for all downstream branches. |
| GO:0071755 IgM B cell receptor complex | IEA GO_REF:0000107 | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR containing membrane IgM. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0071755 IgM B cell receptor complex | ISO GO_REF:0000119 | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR containing membrane IgM. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
| GO:0071755 IgM B cell receptor complex | ISS GO_REF:0000024 | ACCEPT | Summary: The CD79 chain is an integral signaling component of the BCR containing membrane IgM. Reason: Mouse receptor reconstitution directly establishes association with membrane IgM and the other CD79 chain. Human/murine ectodomain work independently supports the assembly interface. This is complex membership, not autonomous antigen binding or a claim that all BCRs use the IgM isotype. |
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