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SERPINC1 SERPINC1 PIGR PIGR ANPEP ANPEP AZGP1 AZGP1 HPX HPX CP CP LGALS3BP LGALS3BP ORM1 ORM1 GGT1 GGT1 APOH APOH VNN1 VNN1 ADGRG6 ADGRG6 FCGBP FCGBP JCHAIN JCHAIN SERPINA1 SERPINA1 ORM2 ORM2 ACE2 ACE2 TF TF GGT1-2 GGT1-2 LCN2 LCN2
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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:
a 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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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SERPINC1Antithrombin-III; Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin. (464 aa)
PIGRPolymeric immunoglobulin receptor; This receptor binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment. (764 aa)
ANPEPAminopeptidase N; Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding [...] (967 aa)
AZGP1Zinc-alpha-2-glycoprotein; Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids; Belongs to the MHC class I family. (298 aa)
HPXHemopexin; Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. (462 aa)
CPCeruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity). (1065 aa)
LGALS3BPGalectin-3-binding protein; Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells. (585 aa)
ORM1Alpha-1-acid glycoprotein 1; Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction; Belongs to the calycin superfamily. Lipocalin family. (201 aa)
GGT1Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] (569 aa)
APOHBeta-2-glycoprotein 1; Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells. (345 aa)
VNN1Pantetheinase; Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine; Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family. (513 aa)
ADGRG6Adhesion G-protein coupled receptor G6; G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane (By similarity). Couples to G(i)-proteins as well as G(s)-proteins. Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons. Regulates neural, cardiac and ear development via G-protein- and/or N-terminus- dependent signaling (By similarity). May act as a receptor for PRNP which may promote myelin homeostasis (By similarity). (1250 aa)
FCGBPIgGFc-binding protein; May be involved in the maintenance of the mucosal structure as a gel-like component of the mucosa. (4204 aa)
JCHAINImmunoglobulin J chain; Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. It also help to bind these immunoglobulins to secretory component. (159 aa)
SERPINA1Short peptide from AAT; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin; Belongs to the serpin family. (418 aa)
ORM2Alpha-1-acid glycoprotein 2; Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction. (201 aa)
ACE2Processed angiotensin-converting enzyme 2; Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. By cleavage of angiotensin II, may be an important regulator of heart function. By cleavage of angiotensin II, may also have a protective role in acute lung injury (By similarity). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SL6A19 in intestine, regulating traffickin [...] (805 aa)
TFSerotransferrin; Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. (698 aa)
GGT1-2Gamma-glutamyltransferase 1. (569 aa)
LCN2Neutrophil gelatinase-associated lipocalin; Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of [...] (198 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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