PHKG1

PHKG1
Identifiers
Aliases	PHKG1, PHKG, phosphorylase kinase catalytic subunit gamma 1
External IDs	OMIM: 172470; MGI: 97579; HomoloGene: 68508; GeneCards: PHKG1; OMA:PHKG1 - orthologs
EC number	2.7.11.26
Gene location (Human)
Chr.	Chromosome 7 (human)
End	56,092,996 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	129,927,390 bp
RNA expression pattern
	Top expressed in
	gastrocnemius muscle; ; muscle of thigh; ; triceps brachii muscle; ; Skeletal muscle tissue of rectus abdominis; ; biceps brachii; ; glutes; ; Skeletal muscle tissue of biceps brachii; ; apex of heart; ; quadriceps femoris muscle; ; vastus lateralis muscle;
	Top expressed in
	muscle of thigh; ; extensor digitorum longus muscle; ; triceps brachii muscle; ; gastrocnemius muscle; ; masseter muscle; ; medial head of gastrocnemius muscle; ; tibialis anterior muscle; ; vastus lateralis muscle; ; sternocleidomastoid muscle; ; temporal muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	enzyme binding; nucleotide binding; protein kinase activity; protein serine/threonine kinase activity; transferase activity; tau-protein kinase activity; ATP binding; calmodulin binding; kinase activity; phosphorylase kinase activity; calmodulin-dependent protein kinase activity;
Cellular component	cytosol; phosphorylase kinase complex;
Biological process	protein phosphorylation; glycogen biosynthetic process; phosphorylation; glycogen metabolic process; peptidyl-serine phosphorylation; peptidyl-threonine phosphorylation; intracellular signal transduction; carbohydrate metabolic process; glycogen catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	5260
	18682
	ENSG00000164776
	ENSMUSG00000025537
	Q16816
	P07934
	NM_001258459; NM_001258460; NM_006213
	NM_011079
	NP_001245388; NP_001245389; NP_006204
	NP_035209
	Wikidata
View/Edit Human	View/Edit Mouse

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.^[5]^[6]

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.^[6]

References

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. doi:10.1016/0167-4781(90)90017-V. PMID 2297530.
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. doi:10.1016/S0021-9258(19)38460-1. PMID 2365696.
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. doi:10.1016/S0021-9258(18)71472-5. PMID 2507540.
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. doi:10.1074/jbc.270.13.7679. PMID 7706316. S2CID 2039456.
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. doi:10.1093/hmg/3.11.1983. PMID 7874115.
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. doi:10.1016/S0021-9258(19)51092-4. PMID 7929096.
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. doi:10.1007/BF01076755. PMID 7935360. S2CID 6202717.
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. doi:10.1016/0301-4622(95)00125-5. PMID 8672716.
Paudel HK (1997). "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase". J. Biol. Chem. 272 (3): 1777–85. doi:10.1016/S0021-9258(19)67481-8. 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. PMC 1170269. PMID 9362479.
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.
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. doi:10.1016/S0014-5793(98)01090-4. PMID 9771888. S2CID 6430192.
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. doi:10.1046/j.1471-4159.1998.71062465.x. PMID 9832145. S2CID 45602824.
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.
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. doi:10.1046/j.1471-4159.2000.0741587.x. PMID 10737616. S2CID 25661250.
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. doi:10.1016/S0014-5793(02)03487-7. PMID 12387894. S2CID 29065525.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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. S2CID 23783563.
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. S2CID 44579006.

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

PHKG1

References

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