Huntingtin-interacting protein K (HYPK)

Huntingtin-interacting protein K (HYPK) is a small, intrinsically disordered protein found in higher eukaryotes that acts as a chaperone-like regulator involved in several essential cellular processes, including protein folding, negative regulation of apoptosis, and co-translational N-terminal acetylation as a modulator of the NatA N-terminal acetyltransferase complex[1][4][5][6]. HYPK was originally identified as a binding partner of the huntingtin protein (HTT) and has the ability to suppress the aggregation and toxicity of mutant huntingtin, a key mechanism associated with Huntington's disease[1][3]. It interacts with a wide array of proteins involved in protein folding, response to unfolded proteins, anti-apoptosis, cell cycle arrest, and transcription regulation, mostly through its intrinsically disordered and flexible structure[1][2][4]. HYPK also regulates the heat shock response by repressing the transcriptional activity of heat shock factor 1 (HSF1) and is itself downregulated in Huntington's disease, further implicating its significance in neurodegeneration[3]. HYPK is not currently considered a primary therapeutic target (such as a receptor, enzyme, or transporter), nor are there approved drugs specifically targeting it.

Other names

C15orf63HSPC136FLJ20431Huntingtin yeast partner Khuntingtin yeast partner Khuntingtin-interacting protein K