Protein Phosphatase 6, Catalytic Subunit (PPP6C)

PPP6; Serine/threonine-protein phosphatase 6 catalytic subunit

SPN	S745
HGNC	9323
MGI	1915107
PubMed	21481188
RGD	708460
UniProt	O00743
Wiki	PPP6C

Reversible phosphorylation of proteins on serine and threonine residues is an important biochemical event that regulates a broad variety of intracellular processes. The phosphorylation state is determined by the well-controlled balance of activities of serine/threonine-specific protein kinases and protein phosphatases. PPP6C is the catalytic subunit of human serine/threonine protein phosphatase-6.

Northern blot analysis showed that PPP6C was expressed as 3 transcripts of 1.8 kb, 4.2 kb, and 4.7 kb in all 16 human tissues examined. Expression levels were highest in testis, heart, and skeletal muscle and lowest in placenta, lung, and kidney. Immunoblot analysis detected a 35-kD PPP6C protein in lysates from human heart muscle and bull testis.

Reference

"The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation."
J. Cell Sci. 109:2865-2874(1996) [PubMed] [Europe PMC] [Abstract]

"Identification of a type 6 protein Ser/Thr phosphatase regulated by interleukin-2 stimulation."
J. Cell. Biochem. 73:153-163(1999) [PubMed] [Europe PMC] [Abstract]

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Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]

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