PHKA1

From Wikipedia, the free encyclopedia

Phosphorylase kinase, alpha 1 (muscle)

Identifiers

PHKA1; MGC132604; PHKA

External IDs

OMIM: 311870 MGI: 97576 HomoloGene: 1981

Gene ontology
Molecular Function:	• catalytic activity • phosphorylase kinase activity • calmodulin binding • phosphorylase kinase regulator activity
Cellular Component:	• membrane
Biological Process:	• carbohydrate metabolic process • glycogen catabolic process • generation of precursor metabolites and energy

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_002637 (mRNA)
NP_002628 (protein)

NM_008832 (mRNA)
NP_032858 (protein)

Location

n/a

Chr X: 98.72 - 98.85 Mb

Pubmed search

[1]

[2]

Phosphorylase kinase, alpha 1 (muscle), also known as PHKA1, is a human gene.^[1]

The PHKA1 gene encodes the alpha subunit of muscle phosphorylase kinase (EC 2.7.1.38), a key regulatory enzyme of glycogen metabolism. Phosphorylase kinase consists of 4 copies of an alpha-beta-gamma-delta tetramer. The alpha, beta (PHKB; MIM 172490), and gamma (PHKG1; MIM 172470 and PHKG2; MIM 172471) subunits have several isoforms; the delta subunit is calmodulin (CALM1; MIM 114180). PHKA2 (MIM 306000) encodes the alpha subunit of liver-specific phosphorylase kinase and is also located on the X chromosome.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: PHKA1 phosphorylase kinase, alpha 1 (muscle).

[edit] Further reading

Brushia RJ, Walsh DA (1999). "Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure.". Front. Biosci. 4: D618-41. PMID 10487978.
Daube H, Billich A, Mann K, Schramm HJ (1991). "Cleavage of phosphorylase kinase and calcium-free calmodulin by HIV-1 protease.". Biochem. Biophys. Res. Commun. 178 (3): 892-8. PMID 1872871.
Meyer HE, Meyer GF, Dirks H, Heilmeyer LM (1990). "Localization of phosphoserine residues in the alpha subunit of rabbit skeletal muscle phosphorylase kinase.". Eur. J. Biochem. 188 (2): 367-76. PMID 2108025.
Francke U, Darras BT, Zander NF, Kilimann MW (1989). "Assignment of human genes for phosphorylase kinase subunits alpha (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13.". Am. J. Hum. Genet. 45 (2): 276-82. PMID 2757032.
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.
Wüllrich A, Hamacher C, Schneider A, Kilimann MW (1993). "The multiphosphorylation domain of the phosphorylase kinase alpha M and alpha L subunits is a hotspot of differential mRNA processing and of molecular evolution.". J. Biol. Chem. 268 (31): 23208-14. PMID 8226841.
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.
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.
Pallen MJ (2004). "Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase.". Protein Sci. 12 (8): 1804-7. PMID 12876330.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.