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Literature summary for 5.2.1.8 extracted from

  • Buschdorf, J.P.; Chew, L.L.; Soh, U.J.; Liou, Y.C.; Low, B.C.
    Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons (2008), PLoS ONE, 3, e2686.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in 293-T cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
C113A mutation in isomerase domain, catalytically inert. Mutation diminishes binding to brain-specifc protein BNIP-H Homo sapiens
S16A mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H Homo sapiens
S16E mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H Homo sapiens
W34A mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Subunits

Subunits Comment Organism
More isoform Pin1 interacts with brain-specifc protein BNIP-H after nerve growth factor stimulation. Both proteins co-localize in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Expression of Pin1 disrupts the BNIP-H/glutaminase complex formation in PC-12 cells under nerve growth factor-stimulation Homo sapiens