Metallothionein 1H-like protein 1 (MT1HL1)

Metallothionein 1H-like protein 1 (MT1HL1) is a member of the metallothionein family of metal-binding proteins, characterized by a high cysteine content, enabling binding of heavy metals such as zinc and copper. MT1HL1 is a protein-coding retrogene, closely related to metallothionein 1H (MT1H), with minor differences at selected metal-binding sites. The protein is assumed to be translated and functional, serving roles in cellular metal homeostasis and protection against oxidative stress through metal detoxification and redox buffering. However, MT1HL1's individual physiological and pathological roles remain poorly characterized, and most biological and clinical insights relate to the broader metallothionein 1 subfamily rather than this specific isoform[2][3][4][1][5]. Currently, MT1HL1 is not recognized as a unique receptor, enzyme, or therapeutic target, and is not associated with direct drug interactions or established biomarker applications.

Other names

Metallothionein 1H-like protein 1MT1HL1MT1P2 (previous HGNC symbol)M1BL1 proteinMT-1H-like protein

None for direct drug targeting. Metallothioneins participate in cell detoxification by chelating metals and regulating their bioavailability, but this is intrinsic protein function, not a pharmacological mechanism[1][5].