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
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
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 | PPP2R5B | protein phosphatase 2, regulatory subunit B’, beta; 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. The phosphorylated form mediates the interaction between AKT1 and PP2A phosphatase leading to dephosphorylation of AKT1 on the ’Thr-308’ and ’Ser-373’ residues (497 aa) | ||
 | CD38 | CD38 molecule; Synthesizes cyclic ADP-ribose, a second messenger for glucose-induced insulin secretion. Also has cADPr hydrolase activity. Also moonlights as a receptor in cells of the immune system (300 aa) | ||
 | NUDT12 | nudix (nucleoside diphosphate linked moiety X)-type motif 12; Hydrolyzes NAD(P)H to NMNH and AMP (2’,5’-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (462 aa) | ||
 | NKTR | natural killer-tumor recognition sequence; Component of a putative tumor-recognition complex. Involved in the function of NK cells (1462 aa) | ||
 | PPIG | peptidylprolyl isomerase G (cyclophilin G); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing (754 aa) | ||
 | PPP2R5A | protein phosphatase 2, regulatory subunit B’, alpha; 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 (486 aa) | ||
 | NNT | nicotinamide nucleotide transhydrogenase; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland (1086 aa) | ||
 | BST1 | bone marrow stromal cell antigen 1; Synthesizes cyclic ADP-ribose, a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth (318 aa) | ||
 | PPIL3 | peptidylprolyl isomerase (cyclophilin)-like 3; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing (165 aa) | ||
 | NMNAT2 | nicotinamide nucleotide adenylyltransferase 2; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides [...] (307 aa) | ||
 | MYO15B | myosin XVB pseudogene (487 aa) | ||
 | PPID | peptidylprolyl isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be i [...] (370 aa) | ||
 | PPIH | peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone (177 aa) | ||
 | NADSYN1 | NAD synthetase 1 (706 aa) | ||
 | PPP2R5E | protein phosphatase 2, regulatory subunit B’, epsilon 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 (467 aa) | ||
 | NMNAT3 | nicotinamide nucleotide adenylyltransferase 3; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as subs [...] (215 aa) | ||
 | NADK | NAD kinase (591 aa) | ||
 | UBC | ubiquitin C (685 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) | ||
 | PPIAL4C | peptidylprolyl isomerase A (cyclophilin A)-like 4C; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (164 aa) | ||
 | CUTC | cutC copper transporter homolog (E. coli); May play a role in copper homeostasis. Can bind one Cu(1+) per subunit (273 aa) | ||
 | MINPP1 | multiple inositol-polyphosphate phosphatase 1; Acts as a phosphoinositide 5- and phosphoinositide 6- phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3- phosphoglycerate. May play a role in bone development (endochondral ossification) (487 aa) | ||
 | NMNAT1 | nicotinamide nucleotide adenylyltransferase 1; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails [...] (279 aa) | ||
 | PPP2R5C | protein phosphatase 2, regulatory subunit B’, gamma; 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. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage- induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation (555 aa) | ||
 | PPP2R5D | protein phosphatase 2, regulatory subunit B’, delta; 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 (602 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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