View source for Biology:PHKG2

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Phosphorylase b kinase gamma catalytic chain, testis/liver isoform''' is an [[Biology:Enzyme|enzyme]] that in humans is encoded by the ''PHKG2'' [[Biology:Gene|gene]].<ref name="pmid2915644">{{cite journal | author = Hanks SK | title = Messenger ribonucleic acid encoding an apparent isoform of phosphorylase kinase catalytic subunit is abundant in the adult testis | journal = Mol Endocrinol | volume = 3 | issue = 1 | pages = 110–6 |date=Mar 1989 | pmid = 2915644 | doi =10.1210/mend-3-1-110  | doi-access = free }}</ref><ref name="pmid8020963">{{cite journal |vauthors=Whitmore SA, Apostolou S, Lane S, Nancarrow JK, Phillips HA, Richards RI, Sutherland GR, Callen DF |  title = Isolation and characterization of transcribed sequences from a chromosome 16 hn-cDNA library and the physical mapping of genes and transcribed sequences using a high-resolution somatic cell panel of human chromosome 16 | journal = Genomics | volume = 20 | issue = 2 | pages = 169–75 |date=Aug 1994 | pmid = 8020963 | doi = 10.1006/geno.1994.1150 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PHKG2 phosphorylase kinase, gamma 2 (testis)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5261}}</ref>

The PHKG2 gene provides instructions for making one piece, the gamma subunit, of the phosphorylase b kinase enzyme. This enzyme is made up of 16 subunits, four each of the alpha, beta, gamma, and delta subunits. (Each subunit is produced from a different gene.) The gamma subunit performs the function of phosphorylase b kinase enzyme, and the other subunits help regulate its activity. This enzyme is found in various [[Biology:Tissue|tissues]], although it is most abundant in the liver and muscles. One version of the enzyme is found in [[Biology:Liver|liver]] cells and another in [[Biology:Muscle|muscle]] cells. The gamma-2 subunit produced from the PHKG2 gene is part of the enzyme found in the liver.<ref name="auto">{{cite web |title=PHKG2 gene |url=https://ghr.nlm.nih.gov/gene/PHKG2#normalfunction |website=ghr.nlm.nih.gov |publisher=Genetics home reference |access-date=9 October 2018}} {{PD-notice}}</ref>

Phosphorylase b kinase plays an important role in providing energy for cells. The main source of cellular energy is a simple sugar called [[Chemistry:Glucose|glucose]]. Glucose is stored in muscle and liver cells in a form called [[Biology:Glycogen|glycogen]]. Glycogen can be broken down rapidly when glucose is needed, for instance to maintain normal levels of glucose in the blood between meals. Phosphorylase b kinase turns on (activates) another enzyme called glycogen phosphorylase b by converting it to the more active form, glycogen phosphorylase a. When active, this enzyme breaks down glycogen.<ref name="auto"/>

==References==
{{reflist}}

==Further reading==
{{refbegin|30em}}
*{{cite journal  | author=Hanks SK |title=Homology probing: identification of cDNA clones encoding members of the protein-serine kinase family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 388–92 |year= 1987 |pmid= 2948189 |doi=10.1073/pnas.84.2.388  | pmc=304212  |doi-access=free |bibcode=1987PNAS...84..388H }}
*{{cite journal  |vauthors=Søvik O, deBarsy T, Maehle B |title=Phosphorylase kinase deficiency: severe glycogen storage disease with evidence of autosomal recessive mode of inheritance. |journal=Eur. J. Pediatr. |volume=139 |issue= 3 |pages= 210 |year= 1983 |pmid= 6962066 |doi=10.1007/BF01377363  |s2cid=21587211 }}
*{{cite journal  |vauthors=Huang CY, Yuan CJ, Livanova NB, Graves DJ |title=Expression, purification, characterization, and deletion mutations of phosphorylase kinase gamma subunit: identification of an inhibitory domain in the gamma subunit. |journal=Mol. Cell. Biochem. |volume=127-128 |pages= 7–18 |year= 1994 |pmid= 7935363 |doi=10.1007/BF01076753  |s2cid=22905953 }}
*{{cite journal   |vauthors=Maichele AJ, Burwinkel B, Maire I, etal |title=Mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit (PHKG2) cause autosomal liver glycogenosis in the gsd rat and in humans. |journal=Nat. Genet. |volume=14 |issue= 3 |pages= 337–40 |year= 1996 |pmid= 8896567 |doi= 10.1038/ng1196-337 |s2cid=2663835 }}
*{{cite journal   |vauthors=Lowe ED, Noble ME, Skamnaki VT, etal |title=The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition. |journal=EMBO J. |volume=16 |issue= 22 |pages= 6646–58 |year= 1998 |pmid= 9362479 |doi= 10.1093/emboj/16.22.6646  | pmc=1170269 }}
*{{cite journal  |vauthors=Burwinkel B, Shiomi S, Al Zaben A, Kilimann MW |title=Liver glycogenosis due to phosphorylase kinase deficiency: PHKG2 gene structure and mutations associated with cirrhosis. |journal=Hum. Mol. Genet. |volume=7 |issue= 1 |pages= 149–54 |year= 1998 |pmid= 9384616 |doi=10.1093/hmg/7.1.149  |doi-access=free }}
*{{cite journal  |vauthors=Burwinkel B, Tanner MS, Kilimann MW |title=Phosphorylase kinase deficient liver glycogenosis: progression to cirrhosis in infancy associated with PHKG2 mutations (H144Y and L225R) |journal=J. Med. Genet. |volume=37 |issue= 5 |pages= 376–7 |year= 2000 |pmid= 10905889 |doi=10.1136/jmg.37.5.376  | pmc=1734590  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal   |vauthors=Burwinkel B, Rootwelt T, Kvittingen EA, etal |title=Severe phenotype of phosphorylase kinase-deficient liver glycogenosis with mutations in the PHKG2 gene. |journal=Pediatr. Res. |volume=54 |issue= 6 |pages= 834–9 |year= 2004 |pmid= 12930917 |doi= 10.1203/01.PDR.0000088069.09275.10 |doi-access= free }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal   |vauthors=Beauchamp NJ, Dalton A, Ramaswami U, etal |title=Glycogen storage disease type IX: High variability in clinical phenotype. |journal=Mol. Genet. Metab. |volume=92 |issue= 1–2 |pages= 88–99 |year= 2007 |pmid= 17689125 |doi= 10.1016/j.ymgme.2007.06.007 }}
{{refend}}

==External links==
* [https://www.ncbi.nlm.nih.gov/books/NBK55061/  GeneReviews/NCBI/NIH/UW entry on Phosphorylase Kinase Deficiency, Glycogen Storage Disease Type IX]

{{Serine/threonine-specific protein kinases}}
{{Enzymes}}

[[Category:EC 2.7.11]]



{{Sourceattribution|PHKG2}}