Target intelligence / Profile preview

Kyphoscoliosis peptidase (KY)

Target
KY
Molecular classification
Transglutaminase-like superfamily, Z-disk protein, Structural protein (skeletal muscle), Other (not an active enzyme based on current evidence)
01

Overview

Kyphoscoliosis peptidase (KY) is a structural protein localized to the Z-disk of skeletal muscle, where it interacts with other sarcomeric and immunoglobulin-like proteins (e.g., FLNC, IGFN1, myosin binding protein C) to maintain normal protein organization and muscle integrity[2]. The protein belongs to the transglutaminase-like superfamily and contains a conserved transglutaminase/protease domain, but biochemical assays indicate the domain is not enzymatically active in humans. Instead, KY is required for normal maturation, stabilization, and response to mechanical stress in muscle, and its dysfunction provokes severe myopathies with muscle weakness, protein aggregation (notably filamin C), and impaired muscle hypertrophy responses[1][2][3][4]. KY may also have nuclear localization in human cells, possibly reflecting evolved functions in primates[2]. While suggested as a candidate biomarker for some muscle and cancer diseases, KY is not an established therapeutic target and no drugs directly modulate its activity[1][2][4].

Other names
Kyphoscoliosis peptidaseKYFLJ33207MFM7
02

Biological functions

Myofibrillar assembly and integrityMuscle fiber maturation and stabilizationNeuromuscular junction formation and maintenanceProtein-protein interactions at the sarcomeric Z-diskRegulation of muscle growth and response to mechanical stress
03

Disease associations

Myofibrillar myopathyMuscle weaknessKyphoscoliosis (mouse; possible relevance to human disease)Protein aggregation disorders involving skeletal muscle
04

Safety considerations

Genetic deficiency (KY mutations) may cause early-onset neuromuscular disorders and myofibrillar myopathyNo therapeutic or drug safety concerns are documented, given the lack of targeted therapeutics
05

Biomarkers

Altered expression in muscle tissue (potential, not validated for clinical use)Dysregulation in muscle disease (suggested candidate biomarker in muscle and possibly prostate cancer panels)

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