HSPA5 (BiP/GRP78, human, P11021) review notes

Deep research: not run (falcon times out in this environment; perplexity-lite unavailable).
Review based on cached GOA-cited publications, the UniProt entry, the rat Hspa5 review
(genes/rat/Hspa5) and the PTHR19375 family review, for consistency.

Key findings

• ATP-dependent Hsp70 cycle structurally characterized for human BiP
  PMID:26655470
• Represses PERK PMID:11907036 and IRE1alpha
  PMID:19538957
• Auxiliary translocation component with Sec62/Sec63 PMID:29719251.
• ERdj4/ERdj5 stimulate BiP ATPase for ERAD of misfolded SP-C PMID:18400946.

Curation decisions

• 107 protein binding rows: co-chaperone/chaperone partners (DNAJB11, DNAJB9, DNAJC10, Dnajc3, SIL1, HYOU1, HSP90B1) MODIFY to GO:0051087 protein-folding chaperone binding; all others REMOVE (UPR sensor interactions are captured by sequestering/kinase inhibitor/regulation terms).
• Proteomics-only locations (focal adhesion, COP9 signalosome, midbody, cadherin binding, bare membrane) marked over-annotated; nucleus/cytoplasm/cell surface kept non-core (consistent with rat Hspa5).
• positive regulation of transcription by RNA polymerase II (TAS) REMOVE.
• ubiquitin protein ligase binding (PMID:8666824, calreticulin paper, abstract only) UNDECIDED.
• NEW: GO:0140662 ATP-dependent protein folding chaperone (MF refinement, as for yeast KAR2).