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FKBP1C FKBP1C FKBP1B FKBP1B FKBP11 FKBP11 FKBP9 FKBP9 FKBP7 FKBP7 FKBP8 FKBP8 FKBP3 FKBP3 FKBP15 FKBP15 FKBP6 FKBP6 ANK1 ANK1 FKBP2 FKBP2 FKBP14 FKBP14 FKBP1A FKBP1A NSF NSF FKBP10 FKBP10 FKBP4 FKBP4 TMPRSS15 TMPRSS15 FKBP5 FKBP5 AHCY AHCY SLC4A3 SLC4A3 AHCYL2 AHCYL2 AHCYL1 AHCYL1 CA4 CA4 CA2 CA2 CFTR CFTR PRKCE PRKCE
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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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FKBP4Peptidyl-prolyl cis-trans isomerase FKBP4; Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role a [...] (459 aa)
CFTRCystic fibrosis transmembrane conductance regulator; Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. Mediates the transport of chloride ions across the cell membrane. Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Plays an important role in airway fluid homeostasis. Contributes to the regulation of the pH [...] (1480 aa)
FKBP3Peptidyl-prolyl cis-trans isomerase FKBP3; FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins; FKBP prolyl isomerases (224 aa)
AHCYAdenosylhomocysteinase; Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (432 aa)
FKBP14Peptidyl-prolyl cis-trans isomerase FKBP14; PPIases accelerate the folding of proteins during protein synthesis; EF-hand domain containing (211 aa)
FKBP15FK506-binding protein 15; May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule- based movement; FKBP prolyl isomerases (1219 aa)
FKBP6Inactive peptidyl-prolyl cis-trans isomerase FKBP6; Co-chaperone required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis. May be re [...] (327 aa)
ANK1Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions (1897 aa)
SLC4A3Anion exchange protein 3; Plasma membrane anion exchange protein of wide distribution. Mediates at least a part of the Cl(-)/HCO3(-) exchange in cardiac myocytes. Both BAE3 and CAE3 forms transport Cl(-); Belongs to the anion exchanger (TC 2.A.31) family (1259 aa)
TMPRSS15Enteropeptidase; Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases; Scavenger receptor cysteine rich domain containing (1019 aa)
CA2Carbonic anhydrase 2; Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6; Carbonic anhydrases (260 aa)
CA4Carbonic anhydrase 4; Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid; Belongs to the alpha-carbonic anhydrase family (312 aa)
PRKCEProtein kinase C epsilon type; Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 [...] (737 aa)
AHCYL2Adenosylhomocysteinase 3; May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate; Belongs to the adenosylhomocysteinase family (611 aa)
FKBP10Peptidyl-prolyl cis-trans isomerase FKBP10; PPIases accelerate the folding of proteins during protein synthesis; EF-hand domain containing (582 aa)
AHCYL1S-adenosylhomocysteine hydrolase-like protein 1; Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5- trisphosphate competing for the common binding site and acting as endogenous ’pseudoligand’ whose inhibitory activity can be modulated by its phosphorylation status. In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5- trisphosphate-induced calcium release by interacting with I [...] (530 aa)
FKBP1CPeptidylprolyl isomerase; FK506 binding protein 1C; FKBP prolyl isomerases (108 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)
FKBP2Peptidyl-prolyl cis-trans isomerase FKBP2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; FKBP prolyl isomerases (142 aa)
NSFVesicle-fusing ATPase; Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling (By similarity); Belongs to the AAA ATPase family (744 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)
FKBP7Peptidylprolyl isomerase; EF-hand domain containing (222 aa)
FKBP9Peptidyl-prolyl cis-trans isomerase FKBP9; PPIases accelerate the folding of proteins during protein synthesis; EF-hand domain containing (623 aa)
FKBP5Peptidyl-prolyl cis-trans isomerase FKBP5; Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded; FKBP prolyl isomerases (457 aa)
FKBP11Peptidyl-prolyl cis-trans isomerase FKBP11; PPIases accelerate the folding of proteins during protein synthesis; FKBP prolyl isomerases (201 aa)
FKBP8Peptidyl-prolyl cis-trans isomerase FKBP8; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis; FKBP prolyl isomerases (413 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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