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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 | OTUB2 | OTU domain, ubiquitin aldehyde binding 2; Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both ’Lys-48’- and ’Lys-63’-linked polyubiquitin chains, with a preference for ’Lys-63’-linked polyubiquitin chains (234 aa) | ||
 | F9 | coagulation factor IX; Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa (461 aa) | ||
 | VWF | von Willebrand factor; Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma (2813 aa) | ||
 | USP13 | ubiquitin specific peptidase 13 (isopeptidase T-3); Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum- associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels- mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34- containing complexes regula [...] (863 aa) | ||
 | GPC1 | glypican 1; Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-med [...] (558 aa) | ||
 | F13A1 | coagulation factor XIII, A1 polypeptide; Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin (732 aa) | ||
 | GP9 | glycoprotein IX (platelet); The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib (177 aa) | ||
 | FGB | fibrinogen beta chain; Fibrinogen has a double function- yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation (491 aa) | ||
 | FGA | fibrinogen alpha chain; Fibrinogen has a double function- yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation (866 aa) | ||
 | SDC2 | syndecan 2; Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity) (201 aa) | ||
 | F2 | coagulation factor II (thrombin); 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 (622 aa) | ||
 | PLG | plasminogen; 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 invasion may be modulated b [...] (810 aa) | ||
 | KLK6 | kallikrein-related peptidase 6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells [...] (244 aa) | ||
 | PFAS | phosphoribosylformylglycinamidine synthase (1338 aa) | ||
 | KLK2 | kallikrein-related peptidase 2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin (261 aa) | ||
 | GP5 | glycoprotein V (platelet); The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis (560 aa) | ||
 | GP1BA | glycoprotein Ib (platelet), alpha polypeptide; GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium (652 aa) | ||
 | FGG | fibrinogen gamma chain (453 aa) | ||
 | F8 | coagulation factor VIII, procoagulant component; Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa (2351 aa) | ||
 | F13B | coagulation factor XIII, B polypeptide; The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin (661 aa) | ||
 | SERPINC1 | serpin peptidase inhibitor, clade C (antithrombin), member 1 (464 aa) | ||
 | F5 | coagulation factor V (proaccelerin, labile factor); Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin (2224 aa) | ||
 | F10 | coagulation factor X; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting (488 aa) | ||
 | SUCLG1 | succinate-CoA ligase, alpha subunit; Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity) (346 aa) | ||
 | GP1BB | glycoprotein Ib (platelet), beta polypeptide; Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium (206 aa) | ||
 | ISCA2 | iron-sulfur cluster assembly 2 homolog (S. cerevisiae); Involved in the assembly of mitochondrial iron-sulfur proteins. Probably involved in the binding of an intermediate of Fe/S cluster assembly (By similarity) (154 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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