basic FUNCTION
| having a peptidylprolyl cis-trans-isomerase activity |
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able to interact with triple helical collagen, and acts as a collagen chaperone |
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may act as an elastin chaperone by controlling both the coacervation and the maturation stages of its self-assembly into fibrils |
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tumor suppressor function of the FKBP65 protein in ovarian carcinogenesis |
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is likely required for lysyl hydroxylase activity or access to type I collagen telopeptide lysines, perhaps through its function as a peptidylprolyl isomerase |
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FKBP10, PLOD2 and SERPINH1, acts during procollagen maturation to contribute to molecular stability and post-translational modification of type I procollagen, without which bone mass and quality are abnormal and fractures and contractures result |
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ability of FKBP10 to modulate the self-assembly of tropoelastin (ELN) is independent of its enzymatic activity to promote the cis-trans isomerization of proline residues in proteins |
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requirement for FKBP10 function during embryonic connective tissue development in mice, but the restricted expression postnatally in bone, ligaments and tendons correlates with the bone fragility and contracture phenotype in humans |
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SERPINH1 and FKBP10 act cooperatively during posttranslational maturation of type I procollagen but fail to properly interact in mutant SERPINH1 cells |