STRINGSTRING
NKTR NKTR FKBP14 FKBP14 FKBP3 FKBP3 FKBP4 FKBP4 PPIF PPIF FKBP11 FKBP11 FKBP8 FKBP8 PPIAL4A PPIAL4A PIN4 PIN4 PPIAL4C PPIAL4C PPIAL4E PPIAL4E PPIAL4H PPIAL4H FKBP5 FKBP5 PPIAL4D PPIAL4D FKBP9 FKBP9 PPIA PPIA FKBP7 FKBP7 PPIAL4G PPIAL4G FKBP1A FKBP1A FKBP2 FKBP2 PTPA PTPA FKBP1B FKBP1B PPIL1 PPIL1 PPIE PPIE FKBP1C FKBP1C FKBP10 FKBP10 PPIH PPIH PPID PPID PPIC PPIC PPIB PPIB PPIL3 PPIL3 PPWD1 PPWD1 PPIG PPIG PPIL4 PPIL4 PIN1 PIN1
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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:
a 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 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
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NKTRNK-tumor recognition protein; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Component of a putative tumor-recognition complex involved in the function of NK cells. (1462 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)
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)
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)
PPIFPeptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved [...] (207 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)
PPIAL4APeptidyl-prolyl cis-trans isomerase A-like 4A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). (164 aa)
PIN4Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4; Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double- stranded DNA. (156 aa)
PPIAL4CPeptidyl-prolyl cis-trans isomerase A-like 4C; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. (164 aa)
PPIAL4EPeptidyl-prolyl cis-trans isomerase A-like 4E; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. (164 aa)
PPIAL4HPeptidyl-prolyl cis-trans isomerase A-like 4H; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. (164 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)
PPIAL4DPeptidyl-prolyl cis-trans isomerase A-like 4D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. (164 aa)
FKBP9Peptidyl-prolyl cis-trans isomerase FKBP9; PPIases accelerate the folding of proteins during protein synthesis. (623 aa)
PPIAPeptidyl-prolyl cis-trans isomerase A, N-terminally processed; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (165 aa)
FKBP7Peptidyl-prolyl cis-trans isomerase FKBP7; PPIases accelerate the folding of proteins during protein synthesis. (222 aa)
PPIAL4GPeptidyl-prolyl cis-trans isomerase A-like 4G; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. (164 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)
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)
PTPASerine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the var [...] (323 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)
PPIL1Peptidyl-prolyl cis-trans isomerase-like 1; Involved in pre-mRNA splicing as component of the spliceosome. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. (166 aa)
PPIEPeptidyl-prolyl cis-trans isomerase E; Involved in pre-mRNA splicing as component of the spliceosome. Combines RNA-binding and PPIase activities. Binds mRNA and has a preference for single-stranded RNA molecules with poly-A and poly-U stretches, suggesting it binds to the poly(A)-region in the 3'-UTR of mRNA molecules. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins. Inhibits KMT2A activity; this requires proline isomerase activity. (314 aa)
FKBP1CFKBP prolyl isomerase 1C. (108 aa)
FKBP10Peptidyl-prolyl cis-trans isomerase FKBP10; PPIases accelerate the folding of proteins during protein synthesis. (582 aa)
PPIHPeptidyl-prolyl cis-trans isomerase H; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. 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)
PPIDPeptidyl-prolyl cis-trans isomerase D; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. 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 [...] (370 aa)
PPICPeptidyl-prolyl cis-trans isomerase C; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding; Belongs to the cyclophilin-type PPIase family. (212 aa)
PPIBPeptidyl-prolyl cis-trans isomerase B; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. (216 aa)
PPIL3Peptidyl-prolyl cis-trans isomerase-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; Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily. (165 aa)
PPWD1Peptidylprolyl isomerase domain and WD repeat-containing protein 1; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be involved in pre-mRNA splicing ; Belongs to the cyclophilin-type PPIase family. PPIL1 subfamily. (646 aa)
PPIGPeptidyl-prolyl cis-trans isomerase G; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. 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)
PPIL4Peptidyl-prolyl cis-trans isomerase-like 4; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily. (492 aa)
PIN1Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] (163 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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