Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Biology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone.
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HSP47 is a collagen-specific ER molecular chaperone with a serpin fold but no serine protease inhibitory activity.
"belongs to the serpin family and has the serpin fold; however, it has no serine protease inhibitory activity"
Hsp47 as a collagen-specific molecular chaperone.
Inhibition of cysteine proteinases by autolytic digestion is mediated by CBP2/Hsp47.
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The paper states that CBP2/Hsp47 does not appear to inhibit serine proteinases, even though it reports a separate cysteine proteinase interaction.
"this protein does not appear to inhibit serine proteinases"
Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47.
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HSP47 preferentially recognizes collagenous Gly-X-Y repeats in triple-helical conformation
"our results suggest that HSP47 preferentially recognizes collagenous Gly-X-Y repeats in triple-helical conformation"
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Temperature-dependent binding indicates importance of substrate triple helix conformation
"Some peptides interacted with HSP47 at a lowered assay temperature at 24 degrees C but not at 30 degrees C, indicating the importance of conformational change of the substrate peptides"
Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis.
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Hsp47 knockout causes embryonic lethality before 11.5 dpc
"Homozygosity for the Hsp47 mutation resulted in embryonic lethality"
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Mature propeptide-cleaved alpha1(I) collagen is absent in knockout mice
"the mature, propeptide-cleaved α1(I) chain"
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Collagen secreted from Hsp47-/- cells has abnormal triple helix (protease-sensitive)
"collagens with an abnormal triple helix are secreted"
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Transfection of Hsp47 cDNA restores collagen triple helix formation
"the secreted collagen became resistant to protease treatment"
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HSP47 is the first substrate-specific molecular chaperone identified in mammals
"Hsp47 is the first substrate-specific molecular chaperone to be identified in mammals"
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Collagen fibrils and basement membranes are severely deficient in knockout mice
"Collagen fibers and basement membranes were hardly detected in knockout mice"
Global defects in collagen secretion in a Mia3/TANGO1 knockout mouse.
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HSP47 confirmed as ER-resident by immunofluorescence colocalization with calnexin in primary chondrocytes and MEFs
"Mia3 is present in regions demarcated by the ER-resident proteins calnexin and HSP47"
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HSP47 used as ER marker in colocalization studies
"Immunofluorescent colocalization analyses of α-Mia3 SH3 with antibodies against calnexin, Hsp47 (SerpinH1), ERGIC-53 (Lman1), and GM130 in primary chondrocytes reveals an Mia3 protein within punctate structures on the ER membrane"
The matrisome: in silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices.
The molecular chaperone Hsp47 is essential for cartilage and endochondral bone formation.
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Conditional Hsp47 knockout in chondrocytes causes severe chondrodysplasia
"Hsp47 conditional null mutant mice died just before or shortly after birth, and exhibited severe generalized chondrodysplasia and bone deformities with lower levels of type II and type XI collagen"
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Type II and XI collagen levels reduced in conditional knockout
"exhibited severe generalized chondrodysplasia and bone deformities with lower levels of type II and type XI collagen"
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Misaligned type I collagen molecules accumulate
"Second-harmonic generation (SHG) analysis and electron microscopy revealed the accumulation of misaligned type I collagen molecules in the intervertebral discs"
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Endochondral bones severely twisted and shortened
"the endochondral bones were severely twisted and shortened"
Role for phospholipid flippase complex of ATP8A1 and CDC50A proteins in cell migration.
Quantitative proteomic profiling of the extracellular matrix of pancreatic islets during the angiogenic switch and insulinoma progression.
Dynamic variations in the expression of type I collagen and its molecular chaperone Hsp47 in cells of the mouse dental follicle during tooth eruption.
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HSP47 expression correlates with type I collagen production in dental follicle
"The production of type I collagen and Hsp47 in the follicle varied with the stage of dental development and eruption"
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Immunolocalization shows HSP47 in cytoplasm of dental follicle cells
"Immunological probes were used here to investigate in vivo and in vitro the temporal and spatial expression of type I collagen and its molecular chaperone Hsp47 in the dental follicle during eruption"
Serpinh1 GOA annotation snapshot
Serpinh1 Falcon deep research report
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SERPINH1/HSP47 is an ER-resident collagen-specific molecular chaperone, not an inhibitory serpin.
"SERPINH1 encodes **HSP47**, an **ER-resident, collagen-specific molecular chaperone** that adopts a **serpin fold** but **lacks serine protease inhibitory activity**."
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HSP47 binds and stabilizes triple-helical procollagen in the ER.
"HSP47 binds **triple-helical procollagen** in the ER and **stabilizes the triple helix**"
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SERPINH1/HSP47 functions predominantly in the ER lumen with transient early secretory pathway transit.
"The dominant functional localization of SERPINH1/HSP47 is the **ER lumen**."
OpenScientist hypothesis review of Serpinh1 GO:0004867
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OpenScientist concluded that the Serpinh1 GO:0004867 annotation should be removed.
"The current GO:0004867 (serine-type endopeptidase inhibitor activity) annotation for mouse Serpinh1 should be **removed**."
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OpenScientist traced the IBA annotation to PANTHER node PTN000156127 and found that the tree does not resolve non-inhibitory HSP47 from inhibitory serpins.
"Source of the IBA annotation | IBA from PANTHER tree PTN000156127; "with/from" lists 12 inhibitory serpins; tree does not resolve non-inhibitory members"
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OpenScientist identified the InterPro IEA as a parallel broad-family mapping problem.
"An additional IEA annotation exists from InterPro domain IPR000215 (Serpin family), which similarly does not distinguish inhibitory from non-inhibitory members."