Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
TXNDC2 TXNDC2 TXN2 TXN2 TXNDC8 TXNDC8 TMX3 TMX3 PGAM1 PGAM1 NME8 NME8 DNAJC10 DNAJC10 ERP44 ERP44 PDILT PDILT ERP27 ERP27 PDIA2 PDIA2 PGAM2 PGAM2 PRDX4 PRDX4 TXNDC16 TXNDC16 PDIA4 PDIA4 TXN TXN TXNDC9 TXNDC9 PDIA3 PDIA3 TXNDC11 TXNDC11 P4HB P4HB SRXN1 SRXN1 PDIA6 PDIA6 TXNDC5 TXNDC5 PDIA5 PDIA5 ZNF593 ZNF593 GDPD5 GDPD5
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:
NME8NME/NM23 family member 8; Probably required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of fibrous sheath (FS) proteins occurs. May be involved in the reduction of disulfide bonds within the sperm FS components. In vitro, it has neither NDP kinase nor reducing activity on disulfide bonds (588 aa)
TXN2thioredoxin 2; Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Could be involved in the resistance to anti-tumor agents. Possesses a dithiol-reducing activity (166 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)
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)
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)
TXNDC16thioredoxin domain containing 16 (825 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)
PGAM2phosphoglycerate mutase 2 (muscle); Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity (253 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)
TXNDC2thioredoxin 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)
PDILTprotein disulfide isomerase-like, testis expressed; Probable redox-inactive chaperone involved in spermatogenesis (584 aa)
PDIA5protein disulfide isomerase family A, member 5 (519 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)
GDPD5glycerophosphodiester phosphodiesterase domain containing 5; Promotes neurite formation. Cooperates with PRDX1 to drive postmitotic motor neuron differentiation. The glycerophosphodiester phosphodiesterase activity may be required for its role in neuronal differentiation. May contribute to the osmotic regulation of cellular glycerophosphocholine (605 aa)
PGAM1phosphoglycerate mutase 1 (brain); Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity (254 aa)
ZNF593zinc finger protein 593; Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity. Could act either by binding to DNA octamer or by interacting with Oct-2. May also be a modulator of other octamer-binding proteins (134 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)
TXNthioredoxin; 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)
PRDX4peroxiredoxin 4; Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (271 aa)
TXNDC5thioredoxin domain containing 5 (endoplasmic reticulum); Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide- isomerase deficiency in yeast (By similarity) (432 aa)
SRXN1sulfiredoxin 1; Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase (137 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (37%)