STAMBP
STAMBP (STAM binding protein, also known as AMSH) is a zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. It acts in endosomal receptor sorting and in cytokine and growth factor signalling. Browse Assay Genie's current range of STAMBP research reagents below, or read on for the biology behind the target.
STAMBP is a zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains and does not cleave 'Lys-48'-linked chains. This selectivity separates its role from degradation signals targeted to the proteasome. It has a key role in regulating cell surface receptor-mediated endocytosis and the ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localisation of STAMBP is required for efficient EGFR degradation, but not for EGFR internalisation.
The STAMBP protein also contributes to signal transduction. It plays a role in cell growth and MYC induction mediated by IL-2 and GM-CSF, and it potentiates BMP (bone morphogenetic protein) signalling by antagonising the inhibitory action of SMAD6 and SMAD7. It is also involved in the negative regulation of the PI3K-AKT-mTOR and RAS-MAP signalling pathways. UniProt places it in the peptidase M67C family, and HGNC classifies it in the JAMM/MPN+ metallopeptidase family. Reported subcellular locations include the nucleus, membrane, cytoplasm and early endosome.
The name reflects its interaction with a signal-transducing adaptor molecule (STAM). In cytokine signalling through the JAK-STAT cascade, adaptor molecules are required, and one contains an SH3 domain needed for MYC induction and cell growth. The protein encoded by the STAMBP gene binds to this SH3 domain and plays a critical role in cytokine-mediated signalling for MYC induction and cell cycle progression. Multiple alternatively spliced transcript variants encode the same protein isoform. AMSH is the commonly used alias, and mouse and rat orthologues are both named Stambp.
STAMBP cleaves Lys-63-linked polyubiquitin chains but not Lys-48-linked chains, making it a useful model of linkage-specific deubiquitination.
It regulates receptor-mediated endocytosis and the sorting of receptors to lysosomes, and endosomal STAMBP is required for efficient EGFR degradation.
STAMBP binds the STAM SH3 domain and supports IL-2 and GM-CSF signalling that drives MYC induction and cell cycle progression.
It potentiates BMP signalling against SMAD6 and SMAD7 and negatively regulates PI3K-AKT-mTOR and RAS-MAP signalling.
STAMBP is a zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. It regulates receptor endocytosis and sorting to lysosomes, supports IL-2 and GM-CSF signalling for MYC induction, potentiates BMP signalling, and negatively regulates PI3K-AKT-mTOR and RAS-MAP pathways.
Yes. AMSH is an alias of STAMBP, whose approved HGNC name is STAM binding protein. The name refers to its binding to the SH3 domain of the signal-transducing adaptor molecule STAM. Multiple splice variants of the gene encode the same protein isoform.
Orthologues exist in mouse and rat, and both are named Stambp. Researchers should check the datasheet of any product for its validated reactivity before using it in a given species.
Receptors, signalling regulators and pathway partners connected to STAMBP function in endosomal sorting and cytokine signalling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O95630; product specifications from Assay Genie datasheets.