STRINGSTRING
AIPL1 AIPL1 FKBP2 FKBP2 FKBP1A FKBP1A FKBP7 FKBP7 FKBP15 FKBP15 FKBP9 FKBP9 FKBP5 FKBP5 FKBP11 FKBP11 FKBP8 FKBP8 LOC114841035 LOC114841035 FKBP4 FKBP4 FKBP3 FKBP3 FKBP14 FKBP14 FKBP6 FKBP6 AIP AIP FKBP10 FKBP10 FKBP1C FKBP1C FKBP1B FKBP1B
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 Color
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:
a 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 to 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:
AIPL1Aryl-hydrocarbon-interacting protein-like 1; May be important in protein trafficking and/or protein folding and stabilization. (384 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. (142 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)
FKBP7Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. (222 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. (1219 aa)
FKBP9Peptidyl-prolyl cis-trans isomerase FKBP9; PPIases accelerate the folding of proteins during protein synthesis. (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. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. (457 aa)
FKBP11Peptidyl-prolyl cis-trans isomerase FKBP11; PPIases accelerate the folding of proteins during protein synthesis. (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. (413 aa)
LOC114841035Uncharacterized protein LOC114841035. (142 aa)
FKBP4Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; 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 [...] (459 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. (224 aa)
FKBP14Peptidyl-prolyl cis-trans isomerase FKBP14; PPIase which accelerates the folding of proteins during protein synthesis. Has a preference for substrates containing 4- hydroxylproline modifications, including type III collagen. May also target type VI and type X collagens. (211 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)
AIPAH receptor-interacting protein; May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting. (330 aa)
FKBP10Peptidyl-prolyl cis-trans isomerase FKBP10; PPIases accelerate the folding of proteins during protein synthesis. (582 aa)
FKBP1CFKBP prolyl isomerase 1C. (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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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