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TXNDC11 TXNDC11 TMX3 TMX3 PDIA6 PDIA6 FMO6P FMO6P ERP27 ERP27 CPOX CPOX PDIA4 PDIA4 PDIA3 PDIA3 FOXRED2 FOXRED2 FMO4 FMO4 PDIA2 PDIA2 DNAJC10 DNAJC10 P4HB P4HB UBC UBC TXNDC9 TXNDC9 OS9 OS9 EDEM3 EDEM3 ERP44 ERP44 FMO3 FMO3 USP7 USP7 TXNDC8 TXNDC8 FMO2 FMO2 ERLEC1 ERLEC1 MAN1B1 MAN1B1 FMO5 FMO5 FMO1 FMO1
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 protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
ERLEC1endoplasmic 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)
FMO2flavin 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)
FOXRED2FAD-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)
PDIA2protein 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)
FMO6Pflavin 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)
FMO5flavin containing monooxygenase 5; In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme (533 aa)
ERP44endoplasmic reticulum protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum (406 aa)
DNAJC10DnaJ (Hsp40) homolog, subfamily C, member 10 (793 aa)
CPOXcoproporphyrinogen 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)
TXNDC9thioredoxin domain containing 9; Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin (226 aa)
ERP27endoplasmic reticulum protein 27 (273 aa)
PDIA6protein 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)
TXNDC11thioredoxin 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)
PDIA4protein disulfide isomerase family A, member 4 (645 aa)
TMX3thioredoxin-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)
PDIA3protein disulfide isomerase family A, member 3 (505 aa)
EDEM3ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) (932 aa)
OS9osteosarcoma amplified 9, endoplasmic reticulum lectin (667 aa)
P4HBprolyl 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)
USP7ubiquitin 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)
UBCubiquitin C (685 aa)
FMO1flavin 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)
FMO4flavin containing monooxygenase 4; This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides (558 aa)
FMO3flavin 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)
MAN1B1mannosidase, 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)
TXNDC8thioredoxin 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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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