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.
Node Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
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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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 | ADSL | adenylosuccinate lyase; Catalyzes two non-sequential steps in de novo AMP synthesis- converts (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate (484 aa) | ||
 | ATP6V1D | ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D; Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity) (247 aa) | ||
 | ATP6V1B1 | ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B1; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (513 aa) | ||
 | ATP6V1E1 | ATPase, H+ transporting, lysosomal 31kDa, V1 subunit E1; Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (226 aa) | ||
 | ATP6V0A4 | ATPase, H+ transporting, lysosomal V0 subunit a4; Part of the proton channel of the V-ATPase that is involved in normal vectorial acid transport into the urine by the kidney (By similarity) (840 aa) | ||
 | ATP6V0A1 | ATPase, H+ transporting, lysosomal V0 subunit a1; Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity) (838 aa) | ||
 | TCIRG1 | T-cell, immune regulator 1, ATPase, H+ transporting, lysosomal V0 subunit A3; Part of the proton channel of V-ATPases (By similarity). Seems to be directly involved in T-cell activation (830 aa) | ||
 | ATP6V1A | ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (617 aa) | ||
 | ATP6V1B2 | ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (511 aa) | ||
 | AASDHPPT | aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase; Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4’- phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN (309 aa) | ||
 | ATP5G3 | ATP synthase, H+ transporting, mitochondrial Fo complex, subunit C3 (subunit 9); Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is c [...] (142 aa) | ||
 | ATP6V0D2 | ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d2; Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity) (350 aa) | ||
 | ATP6V0D1 | ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1; Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity) (351 aa) | ||
 | RRM1 | ribonucleotide reductase M1; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity) (792 aa) | ||
 | ATP6V0C | ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (155 aa) | ||
 | ATP6V0A2 | ATPase, H+ transporting, lysosomal V0 subunit a2; Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (856 aa) | ||
 | PPCDC | phosphopantothenoylcysteine decarboxylase; Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4’- phosphopantotheine (204 aa) | ||
 | ATP5G1 | ATP synthase, H+ transporting, mitochondrial Fo complex, subunit C1 (subunit 9); Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is c [...] (136 aa) | ||
 | ENPP3 | ectonucleotide pyrophosphatase/phosphodiesterase 3; Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity) (875 aa) | ||
 | ENPP1 | ectonucleotide pyrophosphatase/phosphodiesterase 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. In vitro, has a broad specificity, hydrolyzing 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 involved in the regu [...] (925 aa) | ||
 | PPCS | phosphopantothenoylcysteine synthetase; Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4’- phosphopantothenate to form 4-phosphopantothenoylcysteine (311 aa) | ||
 | CLIC4 | chloride intracellular channel 4; Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell- surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical- basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis) (253 aa) | ||
 | ATP5G2 | ATP synthase, H+ transporting, mitochondrial Fo complex, subunit C2 (subunit 9); Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is c [...] (198 aa) | ||
 | ATP6V0B | ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (205 aa) | ||
 | PCYT2 | phosphate cytidylyltransferase 2, ethanolamine; Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine (407 aa) | ||
 | COASY | CoA synthase; Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation (593 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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