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PHKG1

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	7p11.2	Start	56,080,283bp^[1]
Band	7p11.2	End	56,092,996bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5 G1.3\|5 68.26 cM	Start	129,892,262bp^[2]
Band	5 G1.3\|5 68.26 cM	End	129,927,390bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

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

BioGPS


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

Species

Human

Mouse

Entrez


5260


18682

Ensembl


ENSG00000164776


ENSMUSG00000025537

UniProt


Q16816


P07934

RefSeq (mRNA)


NM_001258459 NM_001258460 NM_006213


NM_011079

RefSeq (protein)


NP_001245388 NP_001245389 NP_006204


NP_035209

Location (UCSC)

Chr 7: 56.08 – 56.09 Mb

Chr 5: 129.89 – 129.93 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is anenzyme that in humans is encoded by thePHKG1gene.^[5]^[6]

This gene is a member of theSer/Thr protein kinase family and encodes a protein with one protein kinase domain and twocalmodulin-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 crucialglycogenolytic regulatory enzyme. This gene has twopseudogenes at chromosome 7q11.21 and one at chromosome 11p11.12.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000164776 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000025537 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.S2CID 3257867.
^^a ^b"Entrez Gene: PHKG1 phosphorylase kinase, gamma 1 (muscle)".

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 PDB gallery
1phk: TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH NUCLEOTIDE, SUBSTRATE-ANALOGUE AND PRODUCT 1ql6: THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES 2phk: THE CRYSTAL STRUCTURE OF A PHOSPHORYLASE KINASE PEPTIDE SUBSTRATE COMPLEX: KINASE SUBSTRATE RECOGNITION

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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