STRINGSTRING
A2M A2M SERPINA1 SERPINA1 F5 F5 AFP AFP FGB FGB FGA FGA F10 F10 SERPIND1 SERPIND1 ITIH2 ITIH2 HRG HRG F2 F2 KLKB1 KLKB1 FGG FGG APOH APOH AMBP AMBP RBP4 RBP4 SERPINA5 SERPINA5 GC GC ITIH1 ITIH1 SERPINF2 SERPINF2 AHSG AHSG SERPINA3-2 SERPINA3-2 F12 F12 F13B F13B TF TF SERPINC1 SERPINC1 KNG1 KNG1 PLG PLG ORM1 ORM1 F13A1 F13A1 TTR TTR TF-2 TF-2
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
A2MAlpha-2-macroglobulin. (1504 aa)
SERPINA1Alpha-1-antitrypsin; Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin (By similarity). (420 aa)
F5Coagulation factor V heavy chain; Coagulation factor V is a cofactor that participates with factor Xa to activate prothrombin to thrombin; Belongs to the multicopper oxidase family. (2258 aa)
AFPAlpha-fetoprotein; Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin; Belongs to the ALB/AFP/VDB family. (610 aa)
FGBFibrinogen beta chain; Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it i [...] (534 aa)
FGAFibrinogen alpha chain; Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it [...] (924 aa)
F10Uncharacterized protein. (536 aa)
SERPIND1Serpin family D member 1; Belongs to the serpin family. (517 aa)
ITIH2Inter-alpha-trypsin inhibitor heavy chain H2; May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. (923 aa)
HRGUncharacterized protein. (561 aa)
F2Activation peptide fragment 1; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). (623 aa)
KLKB1Uncharacterized protein; Belongs to the peptidase S1 family. (643 aa)
FGGFibrinogen gamma chain. (454 aa)
APOHBeta-2-glycoprotein 1. (345 aa)
AMBPInter-alpha-trypsin inhibitor light chain; Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization; In the N-terminal section; belongs to the calycin superfamily. Lipocalin family. (364 aa)
RBP4Retinol-binding protein 4; Retinol-binding protein that mediates retinol transport in blood plasma. Delivers retinol from the liver stores to the peripheral tissues. Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane. Belongs to the calycin superfamily. Lipocalin family. (238 aa)
SERPINA5Plasma serine protease inhibitor preproprotein; Belongs to the serpin family. (408 aa)
GCGC vitamin D binding protein. (476 aa)
ITIH1Inter-alpha-trypsin inhibitor heavy chain H1; May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. (927 aa)
SERPINF2Alpha-2-antiplasmin isoform X2; Belongs to the serpin family. (563 aa)
AHSGAlpha-2-HS-glycoprotein. (394 aa)
SERPINA3-2SERPIN domain-containing protein; Belongs to the serpin family. (473 aa)
F12Coagulation factor XIIa heavy chain; Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (By similarity). (646 aa)
F13BCoagulation factor XIII B chain. (663 aa)
TFInhibitor of carbonic anhydrase; Inhibitor for carbonic anhydrase 2 (CA2). Does not bind iron ions. (707 aa)
SERPINC1SERPIN domain-containing protein; Belongs to the serpin family. (431 aa)
KNG1Kininogen 1. (630 aa)
PLGPlasmin heavy chain A, short form; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invas [...] (816 aa)
ORM1Lipocln_cytosolic_FA-bd_dom domain-containing protein. (212 aa)
F13A1Coagulation factor XIII A chain. (774 aa)
TTRTransthyretin; Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Belongs to the transthyretin family. (234 aa)
TF-2Serotransferrin; 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. (702 aa)
Your Current Organism:
Sus scrofa
NCBI taxonomy Id: 9823
Other names: S. scrofa, pig, pigs, swine, wild boar
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