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  • 11.0 [archived version]
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PHKB PHKB PHKG1 PHKG1 PHKA2 PHKA2 CALML5 CALML5 PYGL PYGL CALML4 CALML4 PYGM PYGM CALM1 CALM1 PHKA1 PHKA1 PHKG2 PHKG2 PRKAG1 PRKAG1
"PHKG2" - Phosphorylase b kinase gamma catalytic chain, liver/testis isoform in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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PHKG2Phosphorylase b kinase gamma catalytic chain, liver/testis isoform; Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity); Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family (406 aa)    
Predicted Functional Partners:
PHKA2
Phosphorylase b kinase regulatory subunit alpha, liver isoform; Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin (1235 aa)
     
  0.999
PHKB
Phosphorylase b kinase regulatory subunit beta; Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation (1093 aa)
     
  0.997
PHKA1
Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform; Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin (1223 aa)
     
  0.993
PYGL
Glycogen phosphorylase, liver form; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (847 aa)
     
  0.970
CALM1
Calmodulin-1; Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2 (149 aa)
     
  0.963
PHKG1
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform; Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity) (419 aa)
   
 
0.876
PRKAG1
5’-AMP-activated protein kinase subunit gamma-1; AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes- inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a [...] (340 aa)
     
 
  0.844
PYGM
Glycogen phosphorylase, muscle form; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (842 aa)
     
  0.839
CALML4
Calmodulin-like protein 4; EF-hand domain containing; Belongs to the calmodulin family (196 aa)
     
    0.827
CALML5
Calmodulin-like protein 5; Binds calcium. May be involved in terminal differentiation of keratinocytes; EF-hand domain containing (146 aa)
     
    0.827
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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