STRINGSTRING
Calr4 Calr4 Selenof Selenof Vtn Vtn Cyp2w1 Cyp2w1 Rnaset2 Rnaset2 Ache Ache Ngf Ngf Clu Clu Rdh5 Rdh5 Resp18 Resp18 Jmjd8 Jmjd8 Pdia6 Pdia6 Tor1a Tor1a Tor1b Tor1b Slc27a2 Slc27a2 Tgfa Tgfa P4hb P4hb Os9 Os9 Erlec1 Erlec1 Poglut1 Poglut1 Entpd5 Entpd5 Rdh16 Rdh16 Hyou1 Hyou1 Gbf1 Gbf1 Cln6 Cln6 Hsp90b1 Hsp90b1 Mzb1 Mzb1 Tor2a Tor2a Marchf6 Marchf6 Hspa5 Hspa5 Colgalt1 Colgalt1 Ces1c Ces1c H6pd H6pd Serpinh1 Serpinh1 Cd4 Cd4 Casq2 Casq2 Rcn2 Rcn2 Ces1d Ces1d Uggt1 Uggt1 Pdia3 Pdia3 Edn1 Edn1 Manf Manf Txndc5 Txndc5 Calr3 Calr3 Edem3 Edem3 Poglut2 Poglut2 Dnajc3 Dnajc3 Erap1 Erap1 Bche Bche Lrpap1 Lrpap1 Tmem43 Tmem43 Txndc12 Txndc12 Dnajc10 Dnajc10 Casq1 Casq1 Pdia4 Pdia4 Txndc16 Txndc16 Calu Calu Lyz2 Lyz2 Erp44 Erp44 Foxred2 Foxred2 Ptprn2 Ptprn2 Tor3a Tor3a Dnajb9 Dnajb9 Calr Calr Txndc11 Txndc11 Erp29 Erp29
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:
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:
Calr4Calreticulin. (439 aa)
SelenofSelenoprotein F; May be involved in redox reactions associated with the formation of disulfide bonds. May contribute to the quality control of protein folding in the endoplasmic reticulum. May regulate protein folding by enhancing the catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (By similarity). Belongs to the selenoprotein M/F family. (161 aa)
VtnVitronectin. (490 aa)
Cyp2w1Cytochrome P450, family 2, subfamily w, polypeptide 1; Belongs to the cytochrome P450 family. (492 aa)
Rnaset2Ribonuclease T2; Belongs to the RNase T2 family. (330 aa)
AcheAcetylcholinesterase; Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft; Belongs to the type-B carboxylesterase/lipase family. (614 aa)
NgfBeta-nerve growth factor; Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (By similarity). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone colla [...] (293 aa)
CluClusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysos [...] (447 aa)
Rdh5Retinol dehydrogenase 5; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (318 aa)
Resp18Regulated endocrine-specific protein 18; May play an important regulatory role in corticotrophs. (206 aa)
Jmjd8JmjC domain-containing protein 8; Functions as a positive regulator of TNF-induced NF-kappaB signaling. Regulates angiogenesis and cellular metabolism through interaction with PKM. (291 aa)
Pdia6Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. Belongs to the protein disulfide isomerase family. (445 aa)
Tor1aTorsin-1A; Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular traffickin [...] (333 aa)
Tor1bTorsin. (336 aa)
Slc27a2Very long-chain acyl-CoA synthetase; Acyl CoA synthetase that activates long-chain and very long- chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl- CoA. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (By similarity). Does not activate C24 bile acids, cholate and chenodeoxycholate (By similarity). In vitro, activates 3-alpha,7-alpha,12-alpha- trihydroxy- 5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (By similarity). Exhibits long-chain fatty acids (LCFA) transpo [...] (618 aa)
TgfaProtransforming growth factor alpha; TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar. (159 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)
Os9Protein OS-9; Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4 (By similarity). (666 aa)
Erlec1Endoplasmic reticulum lectin 1. (482 aa)
Poglut1Protein O-glucosyltransferase 1; Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C- X-S-X-P-C. Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2 (By similarity). Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development (By similarity). Notch glucosylation does not affect Notch ligand binding (By similarity). Required during early developmen [...] (454 aa)
Entpd5Ectonucleoside triphosphate diphosphohydrolase 5; Uridine diphosphatase (UDPase) that promotes protein N- glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP > IDP > UDP, but not any other nucleoside di-, mono- or triphosphates, nor thia [...] (427 aa)
Rdh16Retinol dehydrogenase 16; Oxidoreductase with a preference for NAD. Oxidizes all-trans- retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol (By similarity). Oxidizes 3- alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction (By similarity); Belongs to the short-chain dehydrogenases/reductases (SDR) family. (317 aa)
Hyou1Hypoxia up-regulated protein 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (By similarity). (998 aa)
Gbf1Golgi brefeldin A-resistant guanine nucleotide exchange factor 1. (1861 aa)
Cln6CLN6, transmembrane ER protein. (308 aa)
Hsp90b1Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. (804 aa)
Mzb1Marginal zone B- and B1-cell-specific protein; Associates with immunoglobulin M (IgM) heavy and light chains and promotes IgM assembly and secretion. May exert its effect by acting as a molecular chaperone or as an oxidoreductase as it displays a low level of oxidoreductase activity (By similarity). Helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion, and integrin activation. (188 aa)
Tor2aTorsin-2A. (321 aa)
Marchf6Membrane associated ring-CH-type finger 6. (909 aa)
Hspa5Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] (654 aa)
Colgalt1Glycosyltransferase 25 domain containing 1 (Predicted). (617 aa)
Ces1cCarboxylesterase 1C; Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Involved in the extracellular metabolism of lung surfactant (By similarity); Belongs to the type-B carboxylesterase/lipase family. (584 aa)
H6pdHexose-6-phosphate dehydrogenase (Glucose 1-dehydrogenase) (Predicted), isoform CRA_b. (797 aa)
Serpinh1Serpin H1; Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. (417 aa)
Cd4T-cell surface glycoprotein CD4; Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kina [...] (457 aa)
Casq2Calsequestrin-2; Calsequestrin is a high-capacity, moderate affinity, calcium- binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats (By similarity). (427 aa)
Rcn2Reticulocalbin-2; Not known. Binds calcium; Belongs to the CREC family. (320 aa)
Ces1dCarboxylesterase 1D; Major lipase in white adipose tissue (By similarity). Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters; Belongs to the type-B carboxylesterase/lipase family. (564 aa)
Uggt1UDP-glucose:glycoprotein glucosyltransferase 1; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Belongs to the glycosyltransferase 8 family. (1551 aa)
Pdia3Protein disulfide-isomerase A3. (510 aa)
Edn1Big endothelin-1; Endothelins are endothelium-derived vasoconstrictor peptides (By similarity). Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells (By similarity). Belongs to the endothelin/sarafotoxin family. (202 aa)
ManfMesencephalic astrocyte-derived neurotrophic factor; Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain (By similarity). Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress- induced cell death (By similarity). Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal condit [...] (179 aa)
Txndc5Thioredoxin domain-containing 5; Belongs to the protein disulfide isomerase family. (417 aa)
Calr3Calreticulin. (379 aa)
Edem3alpha-1,2-Mannosidase; Belongs to the glycosyl hydrolase 47 family. (893 aa)
Poglut2KDEL (Lys-Asp-Glu-Leu) containing 1, isoform CRA_a. (502 aa)
Dnajc3DnaJ homolog subfamily C member 3; Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (By similarity). (504 aa)
Erap1Endoplasmic reticulum aminopeptidase 1; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play [...] (930 aa)
BcheCarboxylic ester hydrolase; Belongs to the type-B carboxylesterase/lipase family. (597 aa)
Lrpap1Alpha-2-macroglobulin receptor-associated protein; Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway. (360 aa)
Tmem43Transmembrane protein 43; May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). (400 aa)
Txndc12Thioredoxin domain-containing protein 12; Possesses significant protein thiol-disulfide oxidase activity. (170 aa)
Dnajc10DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] (793 aa)
Casq1Calsequestrin-1; Calsequestrin is a high-capacity, moderate affinity, calcium- binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction (By similarity). Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity). (406 aa)
Pdia4Protein disulfide-isomerase A4; Belongs to the protein disulfide isomerase family. (643 aa)
Txndc16Thioredoxin domain-containing 16. (819 aa)
CaluCalumenin; Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma- carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). (315 aa)
Lyz2Lysozyme C-1; Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. In the intestine they may also have a digestive function. (148 aa)
Erp44Endoplasmic reticulum protein 44. (406 aa)
Foxred2FAD-dependent oxidoreductase domain-containing 2. (665 aa)
Ptprn2Receptor-type tyrosine-protein phosphatase N2; Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones [...] (1004 aa)
Tor3aTorsin-3A. (395 aa)
Dnajb9DnaJ homolog subfamily B member 9; Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (By similarity). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similar [...] (222 aa)
CalrCalreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. (416 aa)
Txndc11Thioredoxin domain-containing 11. (947 aa)
Erp29Endoplasmic reticulum resident protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. (260 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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