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Phosphorylase kinase, gamma 1

PHKG1, Phkg
This gene is a member of the Ser/Thr protein kinase family and encodes a protein with one protein kinase domain and two calmodulin-binding domains. This protein is the catalytic member of a 16 subunit protein kinase complex which contains equimolar ratios of 4 subunit types. The complex is a crucial glycogenolytic regulatory enzyme. This gene has two pseudogenes at chromosome 7q11.21 and one at chromosome 11p11.12. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, PHKB, Akt, en-1, TGF-beta type II receptor
Papers on PHKG1
A splice mutation in the PHKG1 gene causes high glycogen content and low meat quality in pig skeletal muscle.
Huang et al., Nanchang, China. In Plos Genet, 2014
Within the QTL interval, only one gene (PHKG1) has a cis-eQTL that was colocolizated with pQTL peaked at the same SNP.
Prediction of kinase inhibitor response using activity profiling, in vitro screening, and elastic net regression.
Piermarocchi et al., United States. In Bmc Syst Biol, 2013
The method was applied to the A549 lung cancer cell line, and we identified specific kinases known to have an important role in this type of cancer (TGFBR2, EGFR, PHKG1 and CDK4).
CpG island methylation profiling in human salivary gland adenoid cystic carcinoma.
El-Naggar et al., Jackson, United States. In Cancer, 2011
Hypomethylation was identified in CpG islands near FBXO17, PHKG1, LOXL1, DOCK1, and PARVG.
In Silico characterization of phosphorylase kinase: evidence for an alternate intronic polyadenylation site in PHKG1.
Rice et al., Bowling Green, United States. In Mol Genet Metab, 2007
In particular, we have identified exon 6 of PHKG1 as a 3' composite terminal exon due to the presence of a weak polyadenylation and cleavage site in intron 6.
Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases.
Kilimann et al., Bochum, Germany. In Eur J Hum Genet, 2003
No mutations have been identified in the muscle isoform of the Phk gamma subunit (PHKG1).
Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene structure and mutations associated with cirrhosis.
Kilimann et al., Bochum, Germany. In Hum Mol Genet, 1998
The gene extends over 9.5 kilonucleotides and is divided into 10 exons; positions of introns are highly conserved between PHKG2 and the gene of the muscle isoform of the gamma subunit, PHKG1.
Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1).
Kilimann et al., Bochum, Germany. In Hum Genet, 1995
Muscle glycogenosis caused by phosphorylase kinase (Phk) deficiency may lead to exercise intolerance, weakness and musculatur atrophy.
The gamma phosphorylase kinase gene, Phkg, maps to mouse chromosome 5 near Gus.
Chamberlain et al., Ann Arbor, United States. In Mamm Genome, 1994
We report the mapping of the catalytic gamma subunit gene, Phkg, to mouse Chromosome (Chr) 5 near beta-glucuronidase (Gus), between alpha fetoprotein (Afp) and erythropoietin (Epo).
A B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene.
Chamberlain et al., Ann Arbor, United States. In Genomics, 1993
The murine gene for Phk-gamma M (Phkg) exhibits multiple transcription start sites that are identical in skeletal muscle, cardiac muscle, and brain.
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