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RASSF5 RASSF5 FKBP1B FKBP1B YTHDF2 YTHDF2 ASPSCR1 ASPSCR1 ENPP1 ENPP1 GYG2 GYG2 ENPP3 ENPP3 UGP2 UGP2 GYG1 GYG1 PGM2L1 PGM2L1 GRHPR GRHPR PGM1 PGM1 FKBP1A FKBP1A AGL AGL PYGB PYGB PGM2 PGM2 GBE1 GBE1 CAT CAT PYGL PYGL PYGM PYGM MGAM MGAM ADSS ADSS LOC93432 LOC93432 GARS GARS LSM2 LSM2 RAN RAN
Nodes:
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
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
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
Your Input:
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)
CATCatalase; Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells; Belongs to the catalase family (527 aa)
AGLGlycogen debranching enzyme; Multifunctional enzyme acting as 1,4-alpha-D-glucan-1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation; Belongs to the glycogen debranching enzyme family (1532 aa)
PGM2L1Glucose 1,6-bisphosphate synthase; Glucose 1,6-bisphosphate synthase using 1,3- bisphosphoglycerate as a phosphate donor and a series of 1- phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1- phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5- bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities (622 aa)
ASPSCR1Tether containing UBX domain for GLUT4; Tethering protein that sequesters GLUT4-containing vesicles in the cytoplasm in the absence of insulin. Modulates the amount of GLUT4 that is available at the cell surface (By similarity). Enhances VCP methylation catalyzed by VCPKMT; UBX domain containing (647 aa)
GRHPRGlyoxylate reductase/hydroxypyruvate reductase; Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate (328 aa)
UGP2UTP--glucose-1-phosphate uridylyltransferase; Plays a central role as a glucosyl donor in cellular metabolic pathways; Belongs to the UDPGP type 1 family (508 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)
ENPP1Ectonucleotide pyrophosphatase/phosphodiesterase family member 1; By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5’ triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3’,5’-cAMP to AMP. May also be [...] (925 aa)
ADSSAdenylosuccinate synthetase isozyme 2; Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (456 aa)
PGM1Phosphoglucomutase-1; This enzyme participates in both the breakdown and synthesis of glucose; Belongs to the phosphohexose mutase family (580 aa)
YTHDF2YTH domain-containing family protein 2; Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates mRNA stability. M6A is a modification present at internal sites of mRNAs and some non- coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability- binding to m6A-containing mRNAs results in the localization to mRNA decay sites, such as processing bodies (P-bodies), leading to mRNA degradation. Required maternally to regulate oocyte maturation- probably acts by binding to m6A-containing mRNAs, thereby regulating mater [...] (579 aa)
LSM2U6 snRNA-associated Sm-like protein LSm2; Binds specifically to the 3’-terminal U-tract of U6 snRNA. May be involved in pre-mRNA splicing; Belongs to the snRNP Sm proteins family (95 aa)
FKBP1BPeptidyl-prolyl cis-trans isomerase FKBP1B; Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the FKBP-type PPIase family. FKBP1 subfamily (108 aa)
GYG2Glycogenin-2; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase; Glycosyltransferase family 8 (501 aa)
PGM2Phosphoglucomutase-2; Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity; Belongs to the phosphohexose mutase family (612 aa)
GARSGlycine--tRNA ligase; Catalyzes the ligation of glycine to the 3’-end of its cognate tRNA. Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs; Belongs to the class-II aminoacyl-tRNA synthetase family (739 aa)
FKBP1APeptidyl-prolyl cis-trans isomerase FKBP1A; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the FKBP-type PPIase family. FKBP1 subfamily (108 aa)
ENPP3Ectonucleotide pyrophosphatase/phosphodiesterase family member 3; Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD; CD molecules (875 aa)
GBE11,4-alpha-glucan-branching enzyme; Required for normal glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule (Probable); Belongs to the glycosyl hydrolase 13 family. GlgB subfamily (702 aa)
RANGTP-binding nuclear protein Ran; GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment a [...] (216 aa)
MGAMMaltase-glucoamylase, intestinal; May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing (1857 aa)
LOC93432Probable maltase-glucoamylase 2; Homo sapiens maltase-glucoamylase (alpha-glucosidase) (LOC93432), mRNA (482 aa)
RASSF5Ras association domain-containing protein 5; Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras [...] (418 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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