PHKG1: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform''' is an [[enzyme]] that in humans is encoded by the ''PHKG1'' [[gene]].<ref name="pmid8530014">{{cite journal |vauthors=Wehner M, Kilimann MW | title = Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1) | journal = Hum Genet | volume = 96 | issue = 5 | pages = 616–8 |date=Jan 1996 | pmid = 8530014 | pmc =  | doi = 10.1007/bf00197422}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PHKG1 phosphorylase kinase, gamma 1 (muscle)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5260| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PHKG1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1phk.
| PDB = {{PDB2|1phk}}, {{PDB2|1ql6}}, {{PDB2|2phk}}
| Name = Phosphorylase kinase, gamma 1 (muscle)
| HGNCid = 8930
| Symbol = PHKG1
| AltSymbols =; PHKG
| OMIM = 172470
| ECnumber =
| Homologene = 68508
| MGIid = 97579
  | GeneAtlas_image1 = PBB_GE_PHKG1_207312_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004689 |text = phosphorylase kinase activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005964 |text = phosphorylase kinase complex}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0005978 |text = glycogen biosynthetic process}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5260
    | Hs_Ensembl = ENSG00000164776
    | Hs_RefseqProtein = NP_006204
    | Hs_RefseqmRNA = NM_006213
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 56115471
    | Hs_GenLoc_end = 56128121
    | Hs_Uniprot = Q16816
    | Mm_EntrezGene = 18682
    | Mm_Ensembl = ENSMUSG00000025537
    | Mm_RefseqmRNA = XM_993479
    | Mm_RefseqProtein = XP_998573
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 130148130
    | Mm_GenLoc_end = 130163787
    | Mm_Uniprot = P07934
  }}
}}
'''Phosphorylase kinase, gamma 1 (muscle)''', also known as '''PHKG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PHKG1 phosphorylase kinase, gamma 1 (muscle)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5260| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PHKG1 phosphorylase kinase, gamma 1 (muscle)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5260| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Jones TA, da Cruz e Silva EF, Spurr NK, ''et al.'' |title=Localisation of the gene encoding the catalytic gamma subunit of phosphorylase kinase to human chromosome bands 7p12-q21. |journal=Biochim. Biophys. Acta |volume=1048 |issue= 1 |pages= 24-9 |year= 1990 |pmid= 2297530 |doi=  }}
*{{cite journal  | author=Jones TA |title=Localisation of the gene encoding the catalytic gamma subunit of phosphorylase kinase to human chromosome bands 7p12-q21 |journal=Biochim. Biophys. Acta |volume=1048 |issue= 1 |pages= 24–9 |year= 1990 |pmid= 2297530 |doi=  10.1016/0167-4781(90)90017-V|name-list-format=vanc| author2=da Cruz e Silva EF  | author3=Spurr NK  | display-authors=| last4=Sheer  | first4=| last5=Cohen  | first5=PT }}
*{{cite journal  | author=Harris WR, Malencik DA, Johnson CM, ''et al.'' |title=Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain. |journal=J. Biol. Chem. |volume=265 |issue= 20 |pages= 11740-5 |year= 1990 |pmid= 2365696 |doi=  }}
*{{cite journal  | author=Harris WR |title=Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain |journal=J. Biol. Chem. |volume=265 |issue= 20 |pages= 11740–5 |year= 1990 |pmid= 2365696 |doi=  |name-list-format=vanc| author2=Malencik DA | author3=Johnson CM  | display-authors=3  | last4=Carr  | first4=SA  | last5=Roberts  | first5=GD  | last6=Byles  | first6=CA  | last7=Anderson  | first7=SR  | last8=Heilmeyer Jr  | first8=LM  | last9=Fischer  | first9=EH }}
*{{cite journal  | author=Dasgupta M, Honeycutt T, Blumenthal DK |title=The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin. |journal=J. Biol. Chem. |volume=264 |issue= 29 |pages= 17156-63 |year= 1989 |pmid= 2507540 |doi=  }}
*{{cite journal  |vauthors=Dasgupta M, Honeycutt T, Blumenthal DK |title=The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin |journal=J. Biol. Chem. |volume=264 |issue= 29 |pages= 17156–63 |year= 1989 |pmid= 2507540 |doi=  }}
*{{cite journal | author=Drewes G, Trinczek B, Illenberger S, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7679-88 |year= 1995 |pmid= 7706316 |doi=  }}
*{{cite journal  | author=Drewes G |title=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 |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7679–88 |year= 1995 |pmid= 7706316 |doi=  10.1074/jbc.270.13.7679 |name-list-format=vanc| author2=Trinczek B  | author3=Illenberger S  | display-authors=| last4=Biernat  | first4=J | last5=Schmitt-Ulms  | first5=G  | last6=Meyer  | first6=HE  | last7=Mandelkow  | first7=EM  | last8=Mandelkow | first8=E}}
*{{cite journal  | author=Wehner M, Clemens PR, Engel AG, Kilimann MW |title=Human muscle glycogenosis due to phosphorylase kinase deficiency associated with a nonsense mutation in the muscle isoform of the alpha subunit. |journal=Hum. Mol. Genet. |volume=3 |issue= 11 |pages= 1983-7 |year= 1995 |pmid= 7874115 |doi=  }}
*{{cite journal  |vauthors=Wehner M, Clemens PR, Engel AG, Kilimann MW |title=Human muscle glycogenosis due to phosphorylase kinase deficiency associated with a nonsense mutation in the muscle isoform of the alpha subunit |journal=Hum. Mol. Genet. |volume=3 |issue= 11 |pages= 1983–7 |year= 1995 |pmid= 7874115 |doi=  10.1093/hmg/3.11.1983}}
*{{cite journal  | author=Yuan CJ, Huang CY, Graves DJ |title=Oxidation and site-directed mutagenesis of the sulfhydryl groups of a truncated gamma catalytic subunit of phosphorylase kinase. Functional and structural effects. |journal=J. Biol. Chem. |volume=269 |issue= 39 |pages= 24367-73 |year= 1994 |pmid= 7929096 |doi=  }}
*{{cite journal  |vauthors=Yuan CJ, Huang CY, Graves DJ |title=Oxidation and site-directed mutagenesis of the sulfhydryl groups of a truncated gamma catalytic subunit of phosphorylase kinase. Functional and structural effects |journal=J. Biol. Chem. |volume=269 |issue= 39 |pages= 24367–73 |year= 1994 |pmid= 7929096 |doi=  }}
*{{cite journal | author=Malencik DA, Zhao Z, Anderson SR |title=Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase. |journal=Mol. Cell. Biochem. |volume=127-128 |issue=  |pages= 31-43 |year= 1994 |pmid= 7935360 |doi=  }}
*{{cite journal  |vauthors=Malencik DA, Zhao Z, Anderson SR |title=Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase |journal=Mol. Cell. Biochem. |volume=127-128 |issue= |pages= 31–43 |year= 1994 |pmid= 7935360 |doi=10.1007/BF01076755 }}
*{{cite journal  | author=Wehner M, Kilimann MW |title=Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1). |journal=Hum. Genet. |volume=96 |issue= 5 |pages= 616-8 |year= 1996 |pmid= 8530014 |doi=  }}
*{{cite journal  |vauthors=Steiner RF, Juminaga D, Albaugh S, Washington H |title=A comparison of the properties of the binary and ternary complexes formed by calmodulin and troponin C with two regulatory peptides of phosphorylase kinase |journal=Biophys. Chem. |volume=59 |issue= 3 |pages= 277–88 |year= 1996 |pmid= 8672716 |doi=10.1016/0301-4622(95)00125-5  }}
*{{cite journal  | author=Steiner RF, Juminaga D, Albaugh S, Washington H |title=A comparison of the properties of the binary and ternary complexes formed by calmodulin and troponin C with two regulatory peptides of phosphorylase kinase. |journal=Biophys. Chem. |volume=59 |issue= 3 |pages= 277-88 |year= 1996 |pmid= 8672716 |doi=  }}
*{{cite journal  | author=Paudel HK |title=The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1777–85 |year= 1997 |pmid= 8999860 |doi= 10.1074/jbc.272.3.1777}}
*{{cite journal  | author=Paudel HK |title=The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1777-85 |year= 1997 |pmid= 8999860 |doi=  }}
*{{cite journal  | author=Lowe ED |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 |name-list-format=vanc| author2=Noble ME  | author3=Skamnaki VT  | display-authors=| last4=Oikonomakos  | first4=NG  | last5=Owen  | first5=DJ  | last6=Johnson | first6=LN }}
*{{cite journal  | author=Lowe ED, Noble ME, Skamnaki VT, ''et al.'' |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 }}
*{{cite journal  | author=Sengupta A |title=Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules |journal=Arch. Biochem. Biophys. |volume=357 |issue= 2 |pages= 299–309 |year= 1998 |pmid= 9735171 |doi= 10.1006/abbi.1998.0813 |name-list-format=vanc| author2=Kabat J  | author3=Novak M  | display-authors=3  | last4=Wu  | first4=Q  | last5=Grundke-Iqbal  | first5=| last6=Iqbal  | first6=K }}
*{{cite journal  | author=Sengupta A, Kabat J, Novak M, ''et al.'' |title=Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. |journal=Arch. Biochem. Biophys. |volume=357 |issue= 2 |pages= 299-309 |year= 1998 |pmid= 9735171 |doi= 10.1006/abbi.1998.0813 }}
*{{cite journal  | author=Wang JZ |title=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 |journal=FEBS Lett. |volume=436 |issue= 1 |pages= 28–34 |year= 1998 |pmid= 9771888 |doi=10.1016/S0014-5793(98)01090-4 |name-list-format=vanc| author2=Wu Q | author3=Smith A  | display-authors=3  | last4=Grundke-Iqbal  | first4=I  | last5=Iqbal  | first5=K  }}
*{{cite journal  | author=Wang JZ, Wu Q, Smith A, ''et al.'' |title=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. |journal=FEBS Lett. |volume=436 |issue= 1 |pages= 28-34 |year= 1998 |pmid= 9771888 |doi=  }}
*{{cite journal  | author=Hanger DP |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465–76 |year= 1998 |pmid= 9832145 |doi=10.1046/j.1471-4159.1998.71062465.x |name-list-format=vanc| author2=Betts JC  | author3=Loviny TL  | display-authors=3  | last4=Blackstock  | first4=Walter P.  | last5=Anderton  | first5=Brian H. }}
*{{cite journal | author=Hanger DP, Betts JC, Loviny TL, ''et al.'' |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465-76 |year= 1998 |pmid= 9832145 |doi=  }}
*{{cite journal  | author=Schneider A |title=Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments |journal=Biochemistry |volume=38 |issue= 12 |pages= 3549–58 |year= 1999 |pmid= 10090741 |doi= 10.1021/bi981874p  |name-list-format=vanc| author2=Biernat J  | author3=von Bergen M  | display-authors=3  | last4=Mandelkow  | first4=E.  | last5=Mandelkow  | first5=E.-M. }}
*{{cite journal  | author=Schneider A, Biernat J, von Bergen M, ''et al.'' |title=Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. |journal=Biochemistry |volume=38 |issue= 12 |pages= 3549-58 |year= 1999 |pmid= 10090741 |doi= 10.1021/bi981874p }}
*{{cite journal  | author=Reynolds CH |title=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 |journal=J. Neurochem. |volume=74 |issue= 4 |pages= 1587–95 |year= 2000 |pmid= 10737616 |doi=10.1046/j.1471-4159.2000.0741587.x  |name-list-format=vanc| author2=Betts JC  | author3=Blackstock WP  | display-authors=3  | last4=Nebreda  | first4=Angel R.  | last5=Anderton  | first5=Brian H.  }}
*{{cite journal | author=Reynolds CH, Betts JC, Blackstock WP, ''et al.'' |title=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. |journal=J. Neurochem. |volume=74 |issue= 4 |pages= 1587-95 |year= 2000 |pmid= 10737616 |doi=  }}
*{{cite journal  |vauthors=Liu F, Iqbal K, Grundke-Iqbal I, Gong CX |title=Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta |journal=FEBS Lett. |volume=530 |issue= 1–3 |pages= 209–14 |year= 2002 |pmid= 12387894 |doi=10.1016/S0014-5793(02)03487-7  }}
*{{cite journal  | author=Liu F, Iqbal K, Grundke-Iqbal I, Gong CX |title=Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. |journal=FEBS Lett. |volume=530 |issue= 1-3 |pages= 209-14 |year= 2002 |pmid= 12387894 |doi=  }}
*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  | author=Gevaert K |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810  |name-list-format=vanc| author2=Goethals M  | author3=Martens L  | display-authors=3  | last4=Van Damme  | first4=Jozef  | last5=Staes  | first5=An  | last6=Thomas  | first6=Grégoire R.  | last7=Vandekerckhove  | first7=Joël }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal  | author=Burwinkel B |title=Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases |journal=Eur. J. Hum. Genet. |volume=11 |issue= 7 |pages= 516–26 |year= 2004 |pmid= 12825073 |doi= 10.1038/sj.ejhg.5200996  |name-list-format=vanc| author2=Hu B  | author3=Schroers A  | display-authors=3  | last4=Clemens  | first4=Paula R  | last5=Moses  | first5=Shimon W  | last6=Shin  | first6=Yoon S  | last7=Pongratz  | first7=Dieter  | last8=Vorgerd  | first8=Matthias  | last9=Kilimann  | first9=Manfred W }}
*{{cite journal  | author=Burwinkel B, Hu B, Schroers A, ''et al.'' |title=Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases. |journal=Eur. J. Hum. Genet. |volume=11 |issue= 7 |pages= 516-26 |year= 2004 |pmid= 12825073 |doi= 10.1038/sj.ejhg.5200996 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=5260}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
[[Category:EC 2.7.11]]


{{protein-stub}}
{{gene-7-stub}}
{{WikiDoc Sources}}

Latest revision as of 18:04, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.[1][2]

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.[2]

References

  1. Wehner M, Kilimann MW (Jan 1996). "Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1)". Hum Genet. 96 (5): 616–8. doi:10.1007/bf00197422. PMID 8530014.
  2. 2.0 2.1 "Entrez Gene: PHKG1 phosphorylase kinase, gamma 1 (muscle)".

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. 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. 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. 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.
  • 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. 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.
  • 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:10.1074/jbc.272.3.1777. 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.
  • 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.
  • 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.
  • 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.
  • 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. 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.
  • 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.