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{
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"name": {
"name": "Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit",
"short": "STKc_PhKG1"
},
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{
"text": "<p>STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. [[cite:PUB00098856], [cite:PUB00133181], [cite:PUB00133182], [cite:PUB00134081], [cite:PUB00074290], [cite:PUB00133191], [cite:PUB00133183], [cite:PUB00133184], [cite:PUB00133185], [cite:PUB00133186], [cite:PUB00133187], [cite:PUB00037452], [cite:PUB00133188], [cite:PUB00133189], [cite:PUB00133190], [cite:PUB00032877], [cite:PUB00029859]]</p>",
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"PUB00133186": {
"PMID": 11796107,
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"volume": "10",
"issue": "1",
"year": 2002,
"title": "A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy.",
"URL": null,
"raw_pages": "23-32",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Nadeau OW",
"Carlson GM",
"Gogol EP."
],
"DOI_URL": null
},
"PUB00133184": {
"PMID": 19764815,
"ISBN": null,
"volume": "48",
"issue": "42",
"year": 2009,
"title": "Expressed phosphorylase b kinase and its alphagammadelta subcomplex as regulatory models for the rabbit skeletal muscle holoenzyme.",
"URL": null,
"raw_pages": "10183-91",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Boulatnikov IG",
"Peters JL",
"Nadeau OW",
"Sage JM",
"Daniels PJ",
"Kumar P",
"Walsh DA",
"Carlson GM."
],
"DOI_URL": null
},
"PUB00098856": {
"PMID": 10487978,
"ISBN": null,
"volume": "4",
"issue": null,
"year": 1999,
"title": "Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure.",
"URL": null,
"raw_pages": "D618-41",
"medline_journal": "Front Biosci",
"ISO_journal": "Front Biosci",
"authors": [
"Brushia RJ",
"Walsh DA."
],
"DOI_URL": null
},
"PUB00029859": {
"PMID": 7663944,
"ISBN": null,
"volume": "3",
"issue": "5",
"year": 1995,
"title": "Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.",
"URL": null,
"raw_pages": "467-82",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Owen DJ",
"Noble ME",
"Garman EF",
"Papageorgiou AC",
"Johnson LN."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00180-0"
},
"PUB00133187": {
"PMID": 11448955,
"ISBN": null,
"volume": "276",
"issue": "37",
"year": 2001,
"title": "An inhibitory segment of the catalytic subunit of phosphorylase kinase does not act as a pseudosubstrate.",
"URL": null,
"raw_pages": "34560-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Bartleson C",
"Graves DJ."
],
"DOI_URL": null
},
"PUB00133183": {
"PMID": 20604537,
"ISBN": null,
"volume": "49",
"issue": "31",
"year": 2010,
"title": "The glucoamylase inhibitor acarbose is a direct activator of phosphorylase kinase.",
"URL": null,
"raw_pages": "6505-7",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Nadeau OW",
"Liu W",
"Boulatnikov IG",
"Sage JM",
"Peters JL",
"Carlson GM."
],
"DOI_URL": null
},
"PUB00134081": {
"PMID": 17692548,
"ISBN": null,
"volume": "92",
"issue": "3",
"year": 2007,
"title": "In Silico characterization of phosphorylase kinase: evidence for an alternate intronic polyadenylation site in PHKG1.",
"URL": null,
"raw_pages": "234-42",
"medline_journal": "Mol Genet Metab",
"ISO_journal": "Mol Genet Metab",
"authors": [
"Winchester JS",
"Rouchka EC",
"Rowland NS",
"Rice NA."
],
"DOI_URL": null
},
"PUB00133181": {
"PMID": 19141288,
"ISBN": null,
"volume": "17",
"issue": "1",
"year": 2009,
"title": "The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase.",
"URL": null,
"raw_pages": "117-27",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Venien-Bryan C",
"Jonic S",
"Skamnaki V",
"Brown N",
"Bischler N",
"Oikonomakos NG",
"Boisset N",
"Johnson LN."
],
"DOI_URL": null
},
"PUB00133182": {
"PMID": 22964223,
"ISBN": null,
"volume": "11",
"issue": "12",
"year": 2012,
"title": "Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (αβγδ)4 phosphorylase kinase complex.",
"URL": null,
"raw_pages": "1768-76",
"medline_journal": "Mol Cell Proteomics",
"ISO_journal": "Mol Cell Proteomics",
"authors": [
"Lane LA",
"Nadeau OW",
"Carlson GM",
"Robinson CV."
],
"DOI_URL": null
},
"PUB00032877": {
"PMID": 9362479,
"ISBN": null,
"volume": "16",
"issue": "22",
"year": 1997,
"title": "The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.",
"URL": null,
"raw_pages": "6646-58",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Lowe ED",
"Noble ME",
"Skamnaki VT",
"Oikonomakos NG",
"Owen DJ",
"Johnson LN."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/16.22.6646"
},
"PUB00133190": {
"PMID": 10029550,
"ISBN": null,
"volume": "38",
"issue": "8",
"year": 1999,
"title": "Activators of phosphorylase kinase alter the cross-linking of its catalytic subunit to the C-terminal one-sixth of its regulatory alpha subunit.",
"URL": null,
"raw_pages": "2551-9",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Nadeau OW",
"Traxler KW",
"Fee LR",
"Baldwin BA",
"Carlson GM."
],
"DOI_URL": null
},
"PUB00133185": {
"PMID": 17123541,
"ISBN": null,
"volume": "365",
"issue": "5",
"year": 2007,
"title": "Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides.",
"URL": null,
"raw_pages": "1429-45",
"medline_journal": "J Mol Biol",
"ISO_journal": "J Mol Biol",
"authors": [
"Nadeau OW",
"Anderson DW",
"Yang Q",
"Artigues A",
"Paschall JE",
"Wyckoff GJ",
"McClintock JL",
"Carlson GM."
],
"DOI_URL": null
},
"PUB00133188": {
"PMID": 10443001,
"ISBN": null,
"volume": "30",
"issue": "3",
"year": 1999,
"title": "Detection and mapping of mutations in the porcine phosphoglucomutase 1 (PGM1) and phosphorylase kinase gamma unit (PHKG) genes using F-SSCP-analysis.",
"URL": null,
"raw_pages": "234",
"medline_journal": "Anim Genet",
"ISO_journal": "Anim Genet",
"authors": [
"Looft C",
"Paul S",
"Kalm E."
],
"DOI_URL": null
},
"PUB00133189": {
"PMID": 10375405,
"ISBN": null,
"volume": "367",
"issue": "1",
"year": 1999,
"title": "A recombinant form of the catalytic subunit of phosphorylase kinase that is soluble, monomeric, and includes key C-terminal residues.",
"URL": null,
"raw_pages": "104-14",
"medline_journal": "Arch Biochem Biophys",
"ISO_journal": "Arch Biochem Biophys",
"authors": [
"Pete MJ",
"Liao CX",
"Bartleson C",
"Graves DJ."
],
"DOI_URL": null
},
"PUB00074290": {
"PMID": 12825073,
"ISBN": null,
"volume": "11",
"issue": "7",
"year": 2003,
"title": "Muscle glycogenosis with low phosphorylase kinase activity: mutations in PHKA1, PHKG1 or six other candidate genes explain only a minority of cases.",
"URL": null,
"raw_pages": "516-26",
"medline_journal": "Eur J Hum Genet",
"ISO_journal": "Eur. J. Hum. Genet.",
"authors": [
"Burwinkel B",
"Hu B",
"Schroers A",
"Clemens PR",
"Moses SW",
"Shin YS",
"Pongratz D",
"Vorgerd M",
"Kilimann MW."
],
"DOI_URL": "http://dx.doi.org/10.1038/sj.ejhg.5200996"
},
"PUB00133191": {
"PMID": 8530014,
"ISBN": null,
"volume": "96",
"issue": "5",
"year": 1995,
"title": "Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1).",
"URL": null,
"raw_pages": "616-8",
"medline_journal": "Hum Genet",
"ISO_journal": "Hum Genet",
"authors": [
"Wehner M",
"Kilimann MW."
],
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},
"PUB00037452": {
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"ISBN": null,
"volume": "38",
"issue": "44",
"year": 1999,
"title": "Catalytic mechanism of phosphorylase kinase probed by mutational studies.",
"URL": null,
"raw_pages": "14718-30",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Skamnaki VT",
"Owen DJ",
"Noble ME",
"Lowe ED",
"Lowe G",
"Oikonomakos NG",
"Johnson LN."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi991454f"
}
},
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"name": "PKc_like"
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}
}
