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  • 11.0 [archived version]
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DCT DCT FMO1 FMO1 FBLN7 FBLN7 TXNDC11 TXNDC11 UHMK1 UHMK1 FMO3 FMO3 RNASEL RNASEL FMO5 FMO5 FMO6P FMO6P COQ4 COQ4 EDEM2 EDEM2 FMO2 FMO2 USP7 USP7 CANX CANX P4HB P4HB BRINP2 BRINP2 EDEM3 EDEM3 SHH SHH PDIA3 PDIA3 OS9 OS9 PDIA4 PDIA4 FMO4 FMO4 SEL1L SEL1L ERN1 ERN1 FOXRED2 FOXRED2 ERN2 ERN2
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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:
some 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 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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FMO2Dimethylaniline monooxygenase [N-oxide-forming] 2; Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive (472 aa)
FMO6PPutative dimethylaniline monooxygenase [N-oxide-forming] 6; It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full-length transcripts (418 aa)
CANXCalnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] (592 aa)
FMO5Dimethylaniline monooxygenase [N-oxide-forming] 5; In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme (533 aa)
ERN2Serine/threonine-protein kinase/endoribonuclease IRE2; Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins; Belongs to the protein kinase superfamily. Ser/Thr protein kinase family (974 aa)
TXNDC11Thioredoxin domain-containing protein 11; May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation (958 aa)
PDIA4Protein disulfide-isomerase A4; Protein disulfide isomerase family A member 4; Belongs to the protein disulfide isomerase family (645 aa)
SHHSonic hedgehog protein; Sonic hedgehog protein- The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Once cleaved, ShhC is degraded in the endoplasmic reticulum (By similarity); Hedgehog signaling molecule family (462 aa)
PDIA3Protein disulfide-isomerase A3; Protein disulfide isomerase family A member 3; Belongs to the protein disulfide isomerase family (505 aa)
COQ4Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial; Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides (265 aa)
EDEM3ER degradation-enhancing alpha-mannosidase-like protein 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) (932 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; MRH domain containing (667 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 [...] (508 aa)
FBLN7Fibulin-7; An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation; Fibulins (439 aa)
SEL1LProtein sel-1 homolog 1; Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling (794 aa)
USP7Ubiquitin carboxyl-terminal hydrolase 7; Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53- dependent transcription regulation, cell growth repression and apoptosis. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of [...] (1102 aa)
BRINP2BMP/retinoic acid-inducible neural-specific protein 2; Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition (783 aa)
RNASEL2-5A-dependent ribonuclease; Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress- response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL [...] (741 aa)
FMO4Dimethylaniline monooxygenase [N-oxide-forming] 4; This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides (558 aa)
FMO3Dimethylaniline monooxygenase [N-oxide-forming] 3; Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds (532 aa)
EDEM2ER degradation-enhancing alpha-mannosidase-like protein 2; Initiates the endoplasmic reticulum-associated degradation (ERAD) that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner. Catalyzes the first mannose trimming step, from Man9GlcNAc2 to Man8GlcNAc2. Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle; Belongs to the glycosyl hydrolase 47 family (578 aa)
FOXRED2FAD-dependent oxidoreductase domain-containing protein 2; Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation (684 aa)
DCTL-dopachrome tautomerase; Catalyzes the conversion of L-dopachrome into 5,6- dihydroxyindole-2-carboxylic acid (DHICA). Involved in regulating eumelanin and phaeomelanin levels; Belongs to the tyrosinase family (552 aa)
ERN1Serine/threonine-protein kinase/endoribonuclease IRE1; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis (977 aa)
UHMK1Serine/threonine-protein kinase Kist; Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus controlling CDKN1B subcellular location and cell cycle progression in G1 phase. May be involved in trafficking and/or processing of RNA (By similarity); Belongs to the protein kinase superfamily. Ser/Thr protein kinase family (419 aa)
FMO1Dimethylaniline monooxygenase [N-oxide-forming] 1; This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines (532 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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