PHKG1

Phosphorylase kinase, gamma 1 (muscle)
File:PBB Protein PHKG1 image.jpg PDB rendering based on 1phk.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1phk​, 1ql6​, 2phk​
Identifiers
Symbols	PHKG1 ; PHKG
External IDs	Template:OMIM5 Template:MGI HomoloGene: 68508
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PHKG1 207312 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Phosphorylase kinase, gamma 1 (muscle), also known as PHKG1, is a human gene.

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.

Further reading

• Jones TA, da Cruz e Silva EF, Spurr NK; et al. (1990). "Localisation of the gene encoding the catalytic gamma subunit of phosphorylase kinase to human chromosome bands 7p12-q21". Biochim. Biophys. Acta. 1048 (1): 24–9. PMID 2297530.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Harris WR, Malencik DA, Johnson CM; et al. (1990). "Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain". J. Biol. Chem. 265 (20): 11740–5. PMID 2365696.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Dasgupta M, Honeycutt T, Blumenthal DK (1989). "The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin". J. Biol. Chem. 264 (29): 17156–63. PMID 2507540.CS1 maint: Multiple names: authors list (link)
• Drewes G, Trinczek B, Illenberger S; et al. (1995). "Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262". J. Biol. Chem. 270 (13): 7679–88. PMID 7706316.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wehner M, Clemens PR, Engel AG, Kilimann MW (1995). "Human muscle glycogenosis due to phosphorylase kinase deficiency associated with a nonsense mutation in the muscle isoform of the alpha subunit". Hum. Mol. Genet. 3 (11): 1983–7. PMID 7874115.CS1 maint: Multiple names: authors list (link)
• Yuan CJ, Huang CY, Graves DJ (1994). "Oxidation and site-directed mutagenesis of the sulfhydryl groups of a truncated gamma catalytic subunit of phosphorylase kinase. Functional and structural effects". J. Biol. Chem. 269 (39): 24367–73. PMID 7929096.CS1 maint: Multiple names: authors list (link)
• Malencik DA, Zhao Z, Anderson SR (1994). "Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase". Mol. Cell. Biochem. 127-128: 31–43. PMID 7935360.CS1 maint: Multiple names: authors list (link)
• Wehner M, Kilimann MW (1996). "Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1)". Hum. Genet. 96 (5): 616–8. PMID 8530014.
• Steiner RF, Juminaga D, Albaugh S, Washington H (1996). "A comparison of the properties of the binary and ternary complexes formed by calmodulin and troponin C with two regulatory peptides of phosphorylase kinase". Biophys. Chem. 59 (3): 277–88. PMID 8672716.CS1 maint: Multiple names: authors list (link)
• Paudel HK (1997). "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase". J. Biol. Chem. 272 (3): 1777–85. PMID 8999860.
• Lowe ED, Noble ME, Skamnaki VT; et al. (1998). "The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition". EMBO J. 16 (22): 6646–58. doi:10.1093/emboj/16.22.6646. PMID 9362479.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sengupta A, Kabat J, Novak M; et al. (1998). "Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules". Arch. Biochem. Biophys. 357 (2): 299–309. doi:10.1006/abbi.1998.0813. PMID 9735171.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wang JZ, Wu Q, Smith A; et al. (1998). "Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase". FEBS Lett. 436 (1): 28–34. PMID 9771888.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hanger DP, Betts JC, Loviny TL; et al. (1998). "New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry". J. Neurochem. 71 (6): 2465–76. PMID 9832145.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Schneider A, Biernat J, von Bergen M; et al. (1999). "Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments". Biochemistry. 38 (12): 3549–58. doi:10.1021/bi981874p. PMID 10090741.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Reynolds CH, Betts JC, Blackstock WP; et al. (2000). "Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta". J. Neurochem. 74 (4): 1587–95. PMID 10737616.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Liu F, Iqbal K, Grundke-Iqbal I, Gong CX (2002). "Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta". FEBS Lett. 530 (1–3): 209–14. PMID 12387894.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Burwinkel B, Hu B, Schroers A; et al. (2004). "Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases". Eur. J. Hum. Genet. 11 (7): 516–26. doi:10.1038/sj.ejhg.5200996. PMID 12825073.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)