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histidine triad nucleotide binding protein 1

Den HINT1 gene provides instructions for making a protein called histidine triad nucleotide-binding protein 1 (HINT1). The function of this protein is not clear. Laboratory studies show that the HINT1 protein has the ability to attach (bind) to certain types of molecules called nucleotides. HINT1 breaks down particular nucleotides through a process called hydrolysis. However, it is not known if the HINT1 protein performs the same reaction in the body or what effects it has.

Normal function

Den HINT1 gene provides instructions for making a protein called histidine triad nucleotide-binding protein 1 (HINT1). The function of this protein is not clear. Laboratory studies show that the HINT1 protein has the ability to attach (bind) to certain types of molecules called nucleotides. HINT1 breaks down particular nucleotides through a process called hydrolysis. However, it is not known if the HINT1 protein performs the same reaction in the body or what effects it has.

Although the mechanisms are not completely understood, the HINT1 protein is involved in the nervous system. In nerve cells (neurons), HINT1 binds to signaling proteins called receptors that relay signals affecting nervous system function. HINT1 appears to stabilize the interaction of different receptors and regulate the effects of their signaling.

The HINT1 protein is also involved in programmed cell death (apoptosis), which occurs when cells are no longer needed. In addition, by blocking the activity of certain genes, HINT1 acts as a tumour suppressor, which means that it keeps cells from growing and dividing too rapidly or in an uncontrolled way.

Conditions referring to this gene or chromosome

Other names

adenosine 5'-monophosphoramidase

HINT

histidine triad nucleotide-binding protein 1

NMAN

PKCI-1

PRKCNH1

protein kinase C inhibitor 1

protein kinase C-interacting protein 1

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Informationen på denna sida är skriven och granskad av kvalificerade kliniker.
  • 18 aug 2020 | Senaste versionen
  • 1 Aug 2014 | Ursprungligen publicerad

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