JavaScript is disabled in your browser. Please enable JavaScript to view this website.

PHKB

Function

Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation.

Involvement in disease

Glycogen storage disease 9B

GSD9B

A metabolic disorder characterized by hepatomegaly, only slightly elevated transaminases and plasma lipids, clinical improvement with increasing age, and remarkably no clinical muscle involvement. Biochemical observations suggest that this mild phenotype is caused by an incomplete holoenzyme that lacks the beta subunit, but that may possess residual activity.

None

The disease is caused by variants affecting the gene represented in this entry.

Pathway

Glycan biosynthesis; glycogen metabolism.

Post-translational modifications

Ser-701 is probably phosphorylated by PKA.

Although the final Cys may be farnesylated, the terminal tripeptide is probably not removed, and the C-terminus is not methylated.

Sequence Similarities

Belongs to the phosphorylase b kinase regulatory chain family.

Cellular localization

Alternative names

Phosphorylase b kinase regulatory subunit beta, Phosphorylase kinase subunit beta, PHKB

swissprot:Q93100 omim:172490 entrezGene:5257