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.
Node Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
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
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 | ERLEC1 | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins (483 aa) | ||
 | FMO2 | flavin containing monooxygenase 2 (non-functional); 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 (471 aa) | ||
 | FOXRED2 | FAD-dependent oxidoreductase domain containing 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) | ||
 | PDIA2 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (525 aa) | ||
 | FMO6P | flavin containing monooxygenase 6 pseudogene; 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 (539 aa) | ||
 | FMO5 | flavin containing monooxygenase 5; In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme (533 aa) | ||
 | CPOX | coproporphyrinogen oxidase; Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III (454 aa) | ||
 | ERP27 | endoplasmic reticulum protein 27 (273 aa) | ||
 | PDIA6 | protein disulfide isomerase family A, member 6; May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (440 aa) | ||
 | TXNDC16 | thioredoxin domain containing 16 (825 aa) | ||
 | TXNDC11 | thioredoxin domain containing 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) | ||
 | PDIA4 | protein disulfide isomerase family A, member 4 (645 aa) | ||
 | TMX3 | thioredoxin-related transmembrane protein 3; Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase (454 aa) | ||
 | PDIA3 | protein disulfide isomerase family A, member 3 (505 aa) | ||
 | TXNDC2 | thioredoxin domain containing 2 (spermatozoa); Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase (553 aa) | ||
 | OS9 | osteosarcoma amplified 9, endoplasmic reticulum lectin (667 aa) | ||
 | P4HB | prolyl 4-hydroxylase, beta polypeptide; 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 [...] (508 aa) | ||
 | USP7 | ubiquitin specific peptidase 7 (herpes virus-associated); 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 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53- dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen pero [...] (1102 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | FMO1 | flavin containing monooxygenase 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) | ||
 | FMO4 | flavin containing monooxygenase 4; This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides (558 aa) | ||
 | FMO3 | flavin containing monooxygenase 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) | ||
 | MAN1B1 | mannosidase, alpha, class 1B, member 1; Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (699 aa) | ||
 | EDEM2 | ER degradation enhancer, mannosidase alpha-like 2 (578 aa) | ||
 | TXNDC8 | thioredoxin domain containing 8 (spermatozoa); May be required for post-translational modifications of proteins required for acrosomal biogenesis. May act by reducing disulfide bonds within the sperm (115 aa) | ||
 | TXN | thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates A [...] (105 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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