ProtNLM2 External predictions
View prediction review YAML Β· B7FXQ8-protnlm-predictions-review.yaml Β· Review status: COMPLETE
HSP20A (B7FXQ8) of Phaeodactylum tricornutum is a full-length small heat-shock protein of PANTHER family PTHR11527 with no GOA annotations. Protein complex oligomerization, response to heat and unfolded protein binding (an obsolete term) are supported by transfer from the family-root PAINT node and characterised sHSP biology. Protein folding, response to salt stress and response to hydrogen peroxide remain uncertain.
Source documents: genes/PHATC/B7FXQ8/B7FXQ8-uniprot.txt Β· genes/PHATC/B7FXQ8/B7FXQ8-ai-review.yaml Β· genes/PHATC/B7FXQ8/B7FXQ8-bioinformatics/RESULTS.md Β· interpro/panther/PTHR11527/PTHR11527-review.yaml Β· genes/PHATC/B7FXQ8/B7FXQ8-goa.tsv Β· publications/PMID_29983375.md Β· genes/PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md
Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.
- file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt: "ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP""
- file:PHATC/B7FXQ8/B7FXQ8-bioinformatics/RESULTS.md: "The PTHR11527 tree root is PTN000163021 (species LUCA). Its PAINT IBDs are protein folding (GO:0006457), response to heat (GO:0009408), response to salt stress (GO:0009651), response to hydrogen peroxide (GO:0042542) and protein complex oligomerization (GO:0051259). ... In the NJ tree, B7FXQ8 groups with the T. pseudonana SF175 protein B8CD87."
- PMID:29983375: "Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers"
- file:PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md: "the salt and peroxide predictions are outliers even relative to the family's own conservative InterPro2GO mapping"
- file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt: "ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP""
- file:PHATC/B7FXQ8/B7FXQ8-bioinformatics/RESULTS.md: "The PTHR11527 tree root is PTN000163021 (species LUCA). Its PAINT IBDs are protein folding (GO:0006457), response to heat (GO:0009408), response to salt stress (GO:0009651), response to hydrogen peroxide (GO:0042542) and protein complex oligomerization (GO:0051259). ... The C-terminal I-X-I motif, which sHSPs use for oligomer assembly, is present in the target as IAI at residues 150-152."
- PMID:29983375: "Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers"
- file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt: "ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP""
- file:PHATC/B7FXQ8/B7FXQ8-bioinformatics/RESULTS.md: "Functions that can be transferred are therefore limited to the family-root IBD set: client holdase behaviour of sHSPs, oligomerization and response to heat."
- PMID:29983375: "Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers"
- file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt: "ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP""
- file:PHATC/B7FXQ8/B7FXQ8-bioinformatics/RESULTS.md: "The PTHR11527 tree root is PTN000163021 (species LUCA). Its PAINT IBDs are protein folding (GO:0006457), response to heat (GO:0009408), response to salt stress (GO:0009651), response to hydrogen peroxide (GO:0042542) and protein complex oligomerization (GO:0051259). ... In the NJ tree, B7FXQ8 groups with the T. pseudonana SF175 protein B8CD87. ... Functions that can be transferred are therefore limited to the family-root IBD set: client holdase behaviour of sHSPs, oligomerization and response to heat."
- PMID:29983375: "Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers"
- file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt: "ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP""
- file:PHATC/B7FXQ8/B7FXQ8-bioinformatics/RESULTS.md: "The PTHR11527 tree root is PTN000163021 (species LUCA). Its PAINT IBDs are protein folding (GO:0006457), response to heat (GO:0009408), response to salt stress (GO:0009651), response to hydrogen peroxide (GO:0042542) and protein complex oligomerization (GO:0051259). ... In the NJ tree, B7FXQ8 groups with the T. pseudonana SF175 protein B8CD87."
- file:PHATC/B7FXQ8/B7FXQ8-hypotheses/prediction-salt-and-peroxide-stress/openscientist.md: "the salt and peroxide predictions are outliers even relative to the family's own conservative InterPro2GO mapping"
- file:PHATC/B7FXQ8/B7FXQ8-uniprot.txt: "ID B7FXQ8_PHATC Unreviewed; 163 AA. ... DR InterPro; IPR002068; A-crystallin/Hsp20_dom. ... DR InterPro; IPR008978; HSP20-like_chaperone. ... DR InterPro; IPR031107; Small_HSP. ... FT DOMAIN 47..155 ... FT /note="SHSP""
- PMID:29983375: "Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. ... the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers"