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PYGB PYGB PYGL PYGL PPP5C PPP5C CNOT7 CNOT7 PPEF1 PPEF1 PYGM PYGM PPP1R3B PPP1R3B YY1 YY1 GYS1 GYS1 GYG1 GYG1 GYS2 GYS2 PPP2R2C PPP2R2C PPP1CA PPP1CA PPP3CA PPP3CA PPP1CB PPP1CB PPP3CC PPP3CC PPP1CC PPP1CC PPP2R2A PPP2R2A PPEF2 PPEF2 PPP3CB PPP3CB PPP2R2B PPP2R2B GBAS GBAS PPP2CA PPP2CA PPP2R2D PPP2R2D PPP4C PPP4C PPP2CB PPP2CB
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Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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PPP5CSerine/threonine-protein phosphatase 5; Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Pa [...] (499 aa)
PYGMGlycogen 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)
PYGLGlycogen 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)
PYGBGlycogen phosphorylase, brain form; Glycogen phosphorylase that regulates glycogen mobilization. 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 (843 aa)
PPP2CBSerine/threonine-protein phosphatase 2A catalytic subunit beta isoform; PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase; Protein phosphatase catalytic subunits (309 aa)
GYS2Glycogen [starch] synthase, liver; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan; Glycosyl transferases group 1 domain containing (703 aa)
YY1Transcriptional repressor protein YY1; Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5’-CCGCCATNTT-3’; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activa [...] (414 aa)
PPP4CSerine/threonine-protein phosphatase 4 catalytic subunit; Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C- PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phospho [...] (307 aa)
PPEF2Serine/threonine-protein phosphatase with EF-hands 2; May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission; Belongs to the PPP phosphatase family (753 aa)
PPP1R3BProtein phosphatase 1 regulatory subunit 3B; Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated gl [...] (285 aa)
GBASProtein NipSnap homolog 2; May act as a positive regulator of L-type calcium channels; Belongs to the NipSnap family (286 aa)
GYS1Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan; Glycosyl transferases group 1 domain containing (737 aa)
PPP2R2ASerine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment; Protein phosphatase 2 regulatory subunits (457 aa)
PPP1CASerine/threonine-protein phosphatase PP1-alpha catalytic subunit; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin de [...] (341 aa)
PPP2R2CSerine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment (447 aa)
GYG1Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase; Glycosyltransferase family 8 (350 aa)
PPP1CCSerine/threonine-protein phosphatase PP1-gamma catalytic subunit; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density- asso [...] (337 aa)
PPEF1Serine/threonine-protein phosphatase with EF-hands 1; May have a role in the recovery or adaptation response of photoreceptors. May have a role in development; EF-hand domain containing (653 aa)
CNOT7CCR4-NOT transcription complex subunit 7; Has 3’-5’ poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translationa [...] (285 aa)
PPP2R2BSerine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity (By similarity). Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance (By similarity) (509 aa)
PPP3CBSerine/threonine-protein phosphatase 2B catalytic subunit beta isoform; Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin (525 aa)
PPP3CASerine/threonine-protein phosphatase 2B catalytic subunit alpha isoform; Calcium-dependent, calmodulin-stimulated protein phosphatase. Many of the substrates contain a PxIxIT motif. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1; Belongs to the PPP phosphatase family. PP-2B subfamily (521 aa)
PPP1CBSerine/threonine-protein phosphatase PP1-beta catalytic subunit; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progressi [...] (327 aa)
PPP3CCSerine/threonine-protein phosphatase 2B catalytic subunit gamma isoform; Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin; Belongs to the PPP phosphatase family. PP-2B subfamily (521 aa)
PPP2R2DSerine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform; B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55- delta) fluctuate during the cell cycle- the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and also m [...] (453 aa)
PPP2CASerine/threonine-protein phosphatase 2A catalytic subunit alpha isoform; PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at ’Ser-259’; Belongs to the PPP phosphatase family. PP-1 subfamily (309 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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