Manual literature synthesis, 2026-11-06. This is an authored evidence guide, not provider-generated research. Source caches retain their original contents and availability flags.
UniProt P16278 currently describes products of 677, 546 and 647 residues. P16278-2 and legacy P16279-1 identify the same 546-residue sequence. Its canonical 83–244 replacement contains 31 residues; the historical 32-residue description includes the adjacent boundary glycine. The 647-residue product lacks canonical residues 1–30; that sequence fact alone establishes neither localization nor activity. The sterol-isomerase gene EBP is a separate locus.
PMID:2511208(https://pubmed.ncbi.nlm.nih.gov/2511208/) distinguishes active long and inactive short cDNA products. PMID:8383699(https://pubmed.ncbi.nlm.nih.gov/8383699/) supplies the splice-product/elastin-binding crosswalk. Its selected original text and figures were examined; full historical construct sequences were not independently reconstructed.
In PMID:9497360(https://pubmed.ncbi.nlm.nih.gov/9497360/), human fibroblast S-Gal cDNA was expressed in reticulocyte and cell systems. Elastin retention, laminin recovery and collagen controls support matrix association. Figure 2D states that the product “binds to elastin and laminin but not to collagen type I.” These assays do not provide a purified two-component affinity constant. PMID:10841810(https://pubmed.ncbi.nlm.nih.gov/10841810/) connects S-Gal deficiency and cellular rescue with elastic-fiber deposition; it does not isolate every proposed chaperone step.
PMID:22128166(https://pubmed.ncbi.nlm.nih.gov/22128166/) studied processed recombinant human enzyme. Figure 2C describes material that “was eluted at a position corresponding to the dimer.” The preparation, proteolytic processing and unresolved physiological stoichiometry limit extrapolation to endogenous complexes. The original methods, results and discussion were read separately from search summaries.
PMID:31720227(https://pmc.ncbi.nlm.nih.gov/articles/PMC6838976/) combines patient measurements with recombinant-enzyme experiments on deficient-mouse glycans. Its human keratan-sulfate assay uses keratanase II; it is not a purified GLB1 cleavage experiment. PMID:8200356(https://pubmed.ncbi.nlm.nih.gov/8200356/) directly compares GLB1 and GALC in saposin-dependent lipid assays, whose substrate presentation matters.
The actual PTHR23421 tree places the exact 677-residue human sequence at AN156. The catalytic assertion is at AN0/PTN000602923; the vertebrate lysosome assertion is at AN146/PTN002765259. Selected catalytic alignment windows retain E188 and E268. The human target's experimental evidence legitimately contributes to the ancestral inference. No claim is made to have manually inspected every alignment column.
PMID:15498789(https://pubmed.ncbi.nlm.nih.gov/15498789/) tests NGX6 encoded by AF188239 with ezrin. The original construct is distinct from GLB1; the historical GLB1 citation-target assignment therefore needs checking. An empty current IntAct response cannot determine whether a historical error occurred.
PMID:32296183(https://pubmed.ncbi.nlm.nih.gov/32296183/) and its actual interaction records support yeast two-hybrid observations with SLC7A1, SLC10A6, GOLM1 and SLC30A2. The records do not establish a GLB1 isoform or endogenous complex. Generic binding removal does not deny these interactions.
The PMID:19056867 authors' database lists GLB1/NP_000395 and links the study. Its integrated peptide total spans two studies. For PMID:23533145(https://pmc.ncbi.nlm.nih.gov/articles/PMC3773505/), original Supplemental Table 2, sheet SI Table 2 row 530, identifies P16278/GLB1: unique-peptide counts are 7/10 in the cancer pool duplicates and 14/13 in control pool duplicates. Individual spectra and isoform-specific peptides were not examined; the manuscript discusses possible co-isolation.
Actual rat D3ZUM4 annotations trace galactoside binding to PMID:8702598(https://pubmed.ncbi.nlm.nih.gov/8702598/) and galactose catabolism to PMID:6811372(https://pubmed.ncbi.nlm.nih.gov/6811372/). Only their authentic abstracts were recovered. Galactoside hydrolysis releasing galactose does not by itself establish breakdown of galactose. These transfers remain unresolved without alleging a curator error.
PMID:6411136(https://pubmed.ncbi.nlm.nih.gov/6411136/) reports a developmental intestinal activity response to cortisone; PMID:414795(https://pubmed.ncbi.nlm.nih.gov/414795/) reports a fetal intestinal response after maternal T3 treatment. These are contextual enzyme-activity responses, not hormone-binding assays. GO:1904016 currently targets CHEBI:80690, a thyroglobulin-bound group distinguished from free T3 by KEGG C16730. The precise T3 term transfer remains unresolved.
R-HSA-2265534 and R-HSA-9036061 describe failed mutant reactions; their normalReaction links to R-HSA-1630306 and R-HSA-2090079 provide the normal catalytic context. BGAL's confirmed GLB1 dimer component resolves to P16278. NEU1/NEU4 reaction complexes establish GLB1 location without assigning their sialidase chemistry to GLB1. Granule events place P16278 in input and released-cargo sets; cargo membership does not establish exocytosis machinery.