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Prdx4 Prdx4 Egln3 Egln3 Fkbp4 Fkbp4 Ero1a Ero1a Ppig Ppig Fkbp1a Fkbp1a Ppif Ppif Ppwd1 Ppwd1 Cwc27 Cwc27 Ppil4 Ppil4 Ppil3 Ppil3 P3h3 P3h3 Gpr162 Gpr162 Fkbp10 Fkbp10 Ppib Ppib Ppic Ppic Ogfod1 Ogfod1 Egln1 Egln1 P4htm P4htm Pin1 Pin1 Egln2 Egln2 Fkbp2 Fkbp2 Fkbp5 Fkbp5 Ppil2 Ppil2 Ppid Ppid Ntmt1 Ntmt1 P4ha2 P4ha2 P4ha3 P4ha3 P4hb P4hb Ppih Ppih Ppil6 Ppil6 Ranbp2 Ranbp2 P4ha1 P4ha1 Crtap Crtap Nktr Nktr Ppidl1 Ppidl1 Fkbp1b Fkbp1b Ppial4g Ppial4g LOC102555086 LOC102555086 Ppial4d Ppial4d P3h1 P3h1 Ppia Ppia Arf3 Arf3 Ppie Ppie RGD1562814 RGD1562814 P3h2 P3h2 Ero1b Ero1b Ppil1 Ppil1
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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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
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textmining
co-expression
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Prdx4Peroxiredoxin-4; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation. Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (273 aa)
Egln3Egl nine homolog 3; Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both [...] (355 aa)
Fkbp4Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90) (By similarity). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. May have a protective role against oxidative stress in mitochondria (By similarity). Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promo [...] (458 aa)
Ero1aERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins (By similarity). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-tri [...] (464 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. (752 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 (By similarity); Belongs to the FKBP-type PPIase family. FKBP [...] (108 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 [...] (206 aa)
Ppwd1Peptidylprolyl isomerase domain and WD repeat containing 1 (Predicted). (646 aa)
Cwc27Spliceosome-associated protein CWC27 homolog; As part of the spliceosome, plays a role in pre-mRNA splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. (468 aa)
Ppil4Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (492 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 (By similarity). (161 aa)
P3h3Leprecan-like 2 (Predicted), isoform CRA_b. (548 aa)
Gpr162G protein-coupled receptor 162 (Predicted). (588 aa)
Fkbp10Peptidylprolyl isomerase. (581 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; Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. (216 aa)
PpicPeptidyl-prolyl cis-trans isomerase; 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. (212 aa)
Ogfod12-oxoglutarate and iron-dependent oxygenase domain-containing 1. (545 aa)
Egln1Egl nine homolog 1; Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is [...] (222 aa)
P4htmSimilar to prolyl-4-hydroxylase-alpha NE2 CG9720-PA (Predicted). (503 aa)
Pin1Peptidyl-prolyl cis-trans isomerase. (165 aa)
Egln2Egl nine homolog 2; Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is [...] (415 aa)
Fkbp2Peptidylprolyl isomerase. (140 aa)
Fkbp5Peptidylprolyl isomerase. (456 aa)
Ppil2Peptidylprolyl isomerase (Cyclophilin)-like 2. (521 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 co [...] (370 aa)
Ntmt1N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed; Distributive alpha-N-methyltransferase that methylates the N- terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]- Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Catalyzes the trimethylation of the N-terminal Gly [...] (223 aa)
P4ha2Prolyl 4-hydroxylase subunit alpha 2. (535 aa)
P4ha3Prolyl 4-hydroxylase subunit alpha-3; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. (544 aa)
P4hbProtein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] (509 aa)
PpihPeptidyl-prolyl cis-trans isomerase; 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. (176 aa)
Ppil6Peptidylprolyl isomerase-like 6. (313 aa)
Ranbp2RAN-binding protein 2. (3088 aa)
P4ha1Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. (534 aa)
CrtapSimilar to Cartilage-associated protein (Predicted), isoform CRA_a. (209 aa)
NktrNatural killer cell triggering receptor. (1470 aa)
Ppidl1Peptidylprolyl isomerase D-like 1. (407 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)
Ppial4gPeptidyl-prolyl cis-trans isomerase; 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. (164 aa)
LOC102555086Similar to Cartilage-associated protein (Predicted), isoform CRA_b. (403 aa)
Ppial4dPeptidyl-prolyl cis-trans isomerase A, N-terminally processed; 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. PPIase A subfamily. (164 aa)
P3h1Prolyl 3-hydroxylase 1; Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts (By similarity). (739 aa)
PpiaPeptidyl-prolyl cis-trans isomerase; 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. (167 aa)
Arf3Peptidylprolyl isomerase. (201 aa)
PpiePeptidyl-prolyl cis-trans isomerase E; Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins; Belongs to the cyclophilin-type PPIase family. PPIase E subfamily. (301 aa)
RGD1562814Peptidyl-prolyl cis-trans isomerase; 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. (164 aa)
P3h2Prolyl 3-hydroxylase 2; Prolyl 3-hydroxylase that catalyzes the post-translational formation of 3-hydroxyproline on collagens. Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in tendons, the eye sclera and in the eye lens capsule (By similarity). Has high activity with the type IV collagen COL4A1, and lower activity with COL1A1. Catalyzes hydroxylation of the first Pro in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline. Has no activity on substrates that lack 4-hydroxyproline in the third position (By similarity). Belongs to the leprecan family. (702 aa)
Ero1bEndoplasmic reticulum oxidoreductase 1 beta. (467 aa)
Ppil1Peptidyl-prolyl cis-trans isomerase; 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. (166 aa)
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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