Beta-tubulin 97EF is a tissue-regulated beta-tubulin subunit that contributes to cytoplasmic microtubule structure. Its major exon-4B form is induced at low temperature and promotes microtubule stability, particularly in gut and hemocytes. The minor exon-4C form has a different temperature response and greater overexpression toxicity. Both forms retain the conserved guanine-nucleotide-binding tubulin architecture.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Paralog-specific primary immunolabeling detects betaTub97EF in mitotic spindles of wing imaginal discs. This supports mitotic participation, retained as noncore relative to the structural microtubule role; it does not demonstrate an essential cell-cycle requirement or distinguish the internal splice variants.
Reason: Paralog-specific primary immunolabeling detects betaTub97EF in mitotic spindles of wing imaginal discs. This supports mitotic participation, retained as noncore relative to the structural microtubule role; it does not demonstrate an essential cell-cycle requirement or distinguish the internal splice variants.
Summary: The selected protein contains the conserved beta-tubulin GTPase domain and demonstrably functions in microtubules. Conserved tubulin nucleotide chemistry supports GTP hydrolysis at the exchangeable beta-subunit site, in the polymer/heterodimer context. This is family-based inference, not a claim of a measured isolated betaTub97EF kinetic rate.
Reason: The selected protein contains the conserved beta-tubulin GTPase domain and demonstrably functions in microtubules. Conserved tubulin nucleotide chemistry supports GTP hydrolysis at the exchangeable beta-subunit site, in the polymer/heterodimer context. This is family-based inference, not a claim of a measured isolated betaTub97EF kinetic rate.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Beta-tubulin carries the exchangeable guanine-nucleotide site of the alpha/beta dimer. The intact target GTPase fold and demonstrated microtubule function support conserved GTP binding.
Reason: Beta-tubulin carries the exchangeable guanine-nucleotide site of the alpha/beta dimer. The intact target GTPase fold and demonstrated microtubule function support conserved GTP binding.
Each tubulin monomer binds a guanine nucleotide, which is nonexchangeable when it is bound in the alpha subunit, or N site, and exchangeable when bound in the beta subunit, or E site.
Summary: Beta-tubulin carries the exchangeable guanine-nucleotide site of the alpha/beta dimer. The intact target GTPase fold and demonstrated microtubule function support conserved GTP binding.
Reason: Beta-tubulin carries the exchangeable guanine-nucleotide site of the alpha/beta dimer. The intact target GTPase fold and demonstrated microtubule function support conserved GTP binding.
Each tubulin monomer binds a guanine nucleotide, which is nonexchangeable when it is bound in the alpha subunit, or N site, and exchangeable when bound in the beta subunit, or E site.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Reason: Gene-specific experiments show incorporation into the microtubule system and increased microtubule stability in hemocytes and gut. This supports a structural beta-tubulin role in cytoplasmic microtubule organization rather than merely relying on a generic family annotation.
Summary: The protein supports developing tissues through microtubule stabilization and temperature adaptation. Retain the broad developmental consequence as noncore relative to its structural microtubule role; automated wording does not establish a separate developmental mechanism.
Reason: The protein supports developing tissues through microtubule stabilization and temperature adaptation. Retain the broad developmental consequence as noncore relative to its structural microtubule role; automated wording does not establish a separate developmental mechanism.
Summary: The protein supports developing tissues through microtubule stabilization and temperature adaptation. Retain the broad developmental consequence as noncore relative to its structural microtubule role; automated wording does not establish a separate developmental mechanism.
Reason: The protein supports developing tissues through microtubule stabilization and temperature adaptation. Retain the broad developmental consequence as noncore relative to its structural microtubule role; automated wording does not establish a separate developmental mechanism.
their sensitivity within the well-tolerated range was slightly enhanced during embryogenesis specifically at low temperatures.
GO:0160108 animal gross anatomical part developmental process
IEA GO_REF:0000117
KEEP AS NON CORE
Summary: The protein supports developing tissues through microtubule stabilization and temperature adaptation. Retain the broad developmental consequence as noncore relative to its structural microtubule role; automated wording does not establish a separate developmental mechanism.
Reason: The protein supports developing tissues through microtubule stabilization and temperature adaptation. Retain the broad developmental consequence as noncore relative to its structural microtubule role; automated wording does not establish a separate developmental mechanism.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
A broad microtubule role is supported for both internal splice variants; microtubule-based process is less precise than the supported organization annotation.
Review rationale: A microtubule-based process is supported by the intact beta-tubulin architecture and primary experiments on both internal splice variants. Both forms partially rescue loss of the major betaTub56D paralog; the detailed stabilization and cold-induction results specifically concern the major exon-4B form. Exact correspondence of Q8MST5 to the paper’s exon names remains unresolved, but this does not undermine the broad structural microtubule role. Existing microtubule-cytoskeleton organization is a more precise supported process, so the prediction is LSP.
Supporting Evidence:
PMID:29084803: "Changing β-tubulin isoform ratios in hemocytes demonstrated that β-Tubulin 97EF has a pronounced microtubule stabilizing effect."
PMID:29084803: "βTub97EF is required for normal microtubule stability in the gut."
Selected Q8MST5 is 457 residues and is identical to UniProt E1JIZ8 and the RefSeq translation NP_001163753.1 from NM_001170282.2, labeled transcript variant B. Alternate Q9VAX7 is also 457 residues and differs at 13 positions, from 177 through 223, with identical sequence outside that region. Individual differences are retained in results.json.
The 2017 primary paper distinguishes major exon-4B and minor exon-4C forms with different cold responses and overexpression toxicity. RefSeq transcript variant B is not automatically exon 4B, and the exact exon-name correspondence has not been independently established here. Thus cold-induced expression is assigned only to the paper’s major 4B transcript and the gene-level dominant response. Both tested forms retain tubulin function, including partial rescue of betaTub56D loss; their differing toxicity does not refute the broad microtubule-process prediction.