Recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP1A (FKBP1A)

1. These findings of this study suggested that FKBP12 is linked to the accumulation of alpha-SYN and phosphorylated tau protein in alpha-synucleinopathies. FKBP12 may play important roles in the pathogenesis of alpha-synucleinopathies. PMID: 29246765
2. FKBP12 binding is required for full Met activation and everolimus can inhibit Met PMID: 27223077
3. Specifically tested on two model systems, the power of iSPOT is demonstrated to accurately predict the structures of a large protein-protein complex (TGFbeta-FKBP12) and a multidomain nuclear receptor homodimer (HNF-4alpha), based on the structures of individual components of the complexes. PMID: 27496803
4. These results identify a novel function for FKBP12 in downregulating MDM2, which directly enhances sensitivity of cancer cells to chemotherapy and nutlin-3 treatment. PMID: 27617579
5. Data show that FKBP12 (FK506 binding protein 1A)conformational transition Is coupled to histidine tautomerization. PMID: 27936610
6. Electrostatic effects on the folding stability of FKBP12 PMID: 27381026
7. Findings indicate that mutant huntingtin (mHTT) aggregates can be transformed into benign species by isomerase FKBP12. PMID: 26450664
8. RyRs have been identified as important targets of FKBP12 and FKBP12.6, members of the immunophilin family PMID: 26009182
9. How phosphorylation of RyR affects channel activity and whether proteins such as the FK-506 binding proteins (FKBP12 and FKBP12.6) are involved in heart failure PMID: 26009186
10. Ultra-fast Shape Recognition with Atom Types--the discovery of novel bioactive small molecular scaffolds for FKBP12 and 11betaHSD1. PMID: 25659145
11. Selectivity within the FKBP family, in particular selective inhibition of FKBP12 or FKBP51, is possible. FKBP51 is a pharmacologically tractable target for stress-related disorders. PMID: 25615537
12. peptidyl prolyl cis-trans isomerase activity of FKBP12 probably plays a role in inhibition of receptor phosphorylation. PMID: 24607931
13. FKBP12 inhibits RyR1 and FKBP12 E31Q/D32N/W59F mutant activates RyR1 in vitro. PMID: 24559985
14. FKBP12 regulates the localization and processing of amyloid precursor protein in human cell lines. PMID: 24499793
15. Enhanced plasticity in the active site of FKBP12.6 is likely to contribute to marked attenuation in the spatial extent of the residues that exhibit doubling of their amide resonances compared with those of the homologous FKBP12. PMID: 24598733
16. the structural basis of the slow resonance doubling transition of FKBP12 and the more rapid conformational linebroadening transition in the 80's loop to gain insight into how these effects are propagated through the protein structure PMID: 24405377
17. the association of FKBP12 with OPRM1 attenuates the phosphorylation of the receptor and triggers the recruitment and activation of PKCepsilon. PMID: 24113748
18. The K44V mutation selectively reduces the line-broadening in the 40's loop, verifying that at least three distinct conformational transitions underlie the line-broadening processes of FKBP12. PMID: 23688288
19. N-terminal and central domain elements are closely apposed near the FKBP12 binding site within the RyR1 three-dimensional structure. PMID: 23585572
20. These data corroborate other studies suggesting that mutations in FKBP12 and FKBP12.6 genes are not commonly related to cardiac diseases. PMID: 22236651
21. The study provides biochemical evidence of the interaction between FKBP12 and RYR1, RYR3 and IP3R. PMID: 22100703
22. Results suggest that FKBP12 forms an endogenous inhibitor of EGFR phosphorylation directly involved in control of cellular EGFR activity (as in carcinoma). PMID: 22103444
23. FKBP12 is the most important PPIase modulating alpha-SYN aggregation and validate the protein as an interesting drug target for Parkinson disease PMID: 21652707
24. It is likely that in FKBP12-ligand complexes, tryptophan 59 provides added binding energy at the active site at the expense of protein stability, a characteristic common to other proteins. PMID: 12600203
25. folding and kinetics of human FKBP12 PMID: 12850152
26. the central binding site for the 12 kDa FK506-binding protein of type-3 ryanodine receptor, encompassing the critical valine proline motif, plays a crucial role in the modulation of the Ca2+ release properties PMID: 14970260
27. experimental data on the stability of FKBP12 are reported for the effects of three environmental variables: pH, salt, and macromolecular crowding PMID: 15992823
28. The spinal horn neurons stained with anti-FKBP 12 antibody was significantly decreased in the motor neuron disease cases compared to that in controls. PMID: 16036432
29. FKBP12 accelerated the aggregation of alpha-synuclein in vitro. PMID: 16410343
30. These findings indicate a new inhibitory function of FKBP12 as an adaptor molecule for the Smad7-Smurf1 complex to regulate the duration of the activin signal through activin type I receptors. PMID: 16720724
31. characterization of the stability, binding and enzymatic properties of three FK506 binding proteins (FKBP-12) differing only by the length and sequence of their N-terminus PMID: 16908189
32. Data show that insertion of a chaperone domain from E. coli SlyD converts human FKBP12 into a powerful catalyst of protein folding. PMID: 17397867
33. FKBP12.0-RyR2 interaction can regulate the gain of excitation-contraction coupling in cardiomyocytes PMID: 17872463
34. FKBP12 is predominantly present during early neointima formation, while mature neointimal atheromas show a relatively low expression without confinement to luminal areas. PMID: 17962721
35. fndings suggest that the peptidyl-prolyl isomerase activity requires only the hydrophobic cavity that captures the Pro-containing peptide PMID: 18029417
36. We investigated in detail the effect of FKBP12 on early aggregation and on fibril formation of wild-type, A53T and A30P alpha-SYN. FKBP12 has a much smaller effect on the fibril formation of these two clinical mutants of alpha-SYN. PMID: 18346205
37. CCI-779 inhibits mTOR signaling through an FKBP12-independent mechanism that leads to profound translational repression in cancer cells. PMID: 18413763
38. our results suggest that FKBP12 may be involved in neuronal or astrocytic cytoskeletal organization and in the abnormal metabolism of tau protein in Alzheimer's disease damaged neurons PMID: 19414059

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HGNC: 3711

OMIM: 186945

KEGG: hsa:2280

STRING: 9606.ENSP00000371138

UniGene: Hs.471933