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PPIA PPIA PPID PPID EEF1G EEF1G RANBP2 RANBP2 INO80B INO80B NKTR NKTR PPIF PPIF PPIC PPIC PPIG PPIG PNISR PNISR PPIAL4G PPIAL4G LUC7L LUC7L PPIL6 PPIL6 CLK3 CLK3 PPIL1 PPIL1 PPIL3 PPIL3 ZC3H18 ZC3H18 CD2BP2 CD2BP2 PPIL4 PPIL4 PRPF38B PRPF38B PPIH PPIH PPIE PPIE CWC27 CWC27 PPIB PPIB JMJD6 JMJD6 PPIL2 PPIL2
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.
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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:
some 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 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:
PPIFPeptidyl-prolyl cis-trans isomerase F, mitochondrial; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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 in act [...] (207 aa)
NKTRNK-tumor recognition protein; Component of a putative tumor-recognition complex. Involved in the function of NK cells; Cyclophilin peptidylprolyl isomerases (1462 aa)
INO80BINO80 complex subunit B; Induces growth and cell cycle arrests at the G1 phase of the cell cycle; INO80 complex (356 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)
PPIGPeptidyl-prolyl cis-trans isomerase 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; Cyclophilin peptidylprolyl isomerases (754 aa)
RANBP2E3 SUMO-protein ligase RanBP2; E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single- stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at ’Lys-490’ which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore comple [...] (3224 aa)
PPIL3Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (165 aa)
LUC7LPutative RNA-binding protein Luc7-like 1; May bind to RNA via its Arg/Ser-rich domain; Belongs to the Luc7 family (371 aa)
PPIBPeptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (216 aa)
PPICPeptidyl-prolyl cis-trans isomerase C; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (212 aa)
PPIDPeptidyl-prolyl cis-trans 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 complexe [...] (370 aa)
CD2BP2CD2 antigen cytoplasmic tail-binding protein 2; Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly; Protein phosphatase 1 regulatory subunits (341 aa)
PPIHPeptidyl-prolyl cis-trans isomerase 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; Cyclophilin peptidylprolyl isomerases (177 aa)
EEF1GElongation factor 1-gamma; Probably plays a role in anchoring the complex to other cellular components (437 aa)
PPIL2Peptidyl-prolyl cis-trans isomerase-like 2; May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins (By similarity). May also function as a chaperone, playing a role in transport to the cell membrane of BSG for instance. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating ’Lys-48’-linked polyubiquitination of proteins could target them for proteasomal degradation; Cyclo [...] (520 aa)
PNISRArginine/serine-rich protein PNISR; PNN interacting serine and arginine rich protein; Belongs to the splicing factor SR family (805 aa)
PRPF38BPre-mRNA-splicing factor 38B; May be required for pre-mRNA splicing (546 aa)
PPIEPeptidyl-prolyl cis-trans isomerase E; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing; Cyclophilin peptidylprolyl isomerases (314 aa)
PPIL1Peptidyl-prolyl cis-trans isomerase-like 1; 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; Cyclophilin peptidylprolyl isomerases (166 aa)
CWC27Peptidyl-prolyl cis-trans isomerase CWC27 homolog; PPIases accelerate the folding of proteins; Belongs to the cyclophilin-type PPIase family (472 aa)
CLK3Dual specificity protein kinase CLK3; Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells; CDC like kinases (638 aa)
PPIL6Peptidyl-prolyl cis-trans isomerase-like 6; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (337 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)
JMJD6Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an argi [...] (414 aa)
ZC3H18Zinc finger CCCH-type containing 18 (977 aa)
PPIAPeptidyl-prolyl cis-trans isomerase A; 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 (165 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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