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HEBP1 HEBP1 CCL13 CCL13 DRD4 DRD4 OPRD1 OPRD1 GRM6 GRM6 CX3CL1 CX3CL1 CXCL6 CXCL6 TAS2R8 TAS2R8 CXCL3 CXCL3 TAS2R9 TAS2R9 C5 C5 CCL1 CCL1 TAS2R10 TAS2R10 CXCR2 CXCR2 CCL11 CCL11 CCL25 CCL25 GNB3 GNB3 CCL21 CCL21 TAS2R7 TAS2R7 CXCR1 CXCR1 CXCL5 CXCL5 CCL5 CCL5 BDKRB1 BDKRB1 GNB4 GNB4 HNRNPA0 HNRNPA0 XCL2 XCL2
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.
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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:
some 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 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:
CX3CL1Fractalkine; Acts as a ligand for both CX3CR1 and integrins. Binds to CX3CR1. Binds to integrins ITGAV-ITGB3 and ITGA4-ITGB1. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner. In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins. In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1. The soluble form is chemotactic for T-cells and monocytes and not for neutrophils. The membrane-bound fo [...] (397 aa)
HEBP1Heme-binding protein 1; May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N- methylprotoporphyrin with similar affinities; Belongs to the HEBP family (189 aa)
DRD4Dopamine receptor D4; Belongs to the G-protein coupled receptor 1 family (419 aa)
BDKRB1B1 bradykinin receptor; This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation (353 aa)
C5Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing (1676 aa)
CCL1C-C motif chemokine 1; Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8; Belongs to the intercrine beta (chemokine CC) family (96 aa)
CCL13C-C motif chemokine 13; Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. Signals through CCR2B and CCR3 receptors. Plays a role in the accumulation of leukocytes at both sides of allergic and non-allergic inflammation. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. May play a role in the monocyte attraction in tissues chronically exposed to exogenous pathogens; Chemokine ligands (98 aa)
CXCL6C-X-C motif chemokine 6; Chemotactic for neutrophil granulocytes. Signals through binding and activation of its receptors (CXCR1 and CXCR2). In addition to its chemotactic and angiogenic properties, it has strong antibacterial activity against Gram-positive and Gram- negative bacteria (90-fold-higher when compared to CXCL5 and CXCL7); Chemokine ligands (114 aa)
GNB3Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction (340 aa)
GRM6Metabotropic glutamate receptor 6; G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Signaling stimulates TRPM1 channel activity and Ca(2+) uptake. Required for normal vision; Glutamate metabotropic receptors (877 aa)
GNB4Guanine nucleotide-binding protein subunit beta-4; Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction (340 aa)
OPRD1Delta-type opioid receptor; G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. [...] (372 aa)
TAS2R8Taste receptor type 2 member 8; Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5; Belongs to the G-protein coupled receptor T2R family (309 aa)
TAS2R10Taste receptor type 2 member 10; Gustducin-coupled strychnine receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium- regulated cation channel TRPM5 (307 aa)
TAS2R7Taste receptor type 2 member 7; Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (318 aa)
TAS2R9Taste receptor type 2 member 9; Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5 (By similarity) (312 aa)
CCL21C-C motif chemokine 21; Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4; Belongs to the intercrine beta (chemokine CC) family (134 aa)
CXCR1C-X-C chemokine receptor type 1; Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system. This receptor binds to IL-8 with a high affinity and to MGSA (GRO) with a low affinity; C-X-C motif chemokine receptors (350 aa)
CXCL3C-X-C motif chemokine 3; Ligand for CXCR2 (By similarity). Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. In vitro, the processed form GRO-gamma(5-73) shows a fivefold higher chemotactic activity for neutrophilic granulocytes; Chemokine ligands (107 aa)
CXCL5C-X-C motif chemokine 5; Involved in neutrophil activation. In vitro, ENA-78(8- 78) and ENA-78(9-78) show a threefold higher chemotactic activity for neutrophil granulocytes; Chemokine ligands (114 aa)
CCL11Eotaxin; In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions. Binds to CCR3; Chemokine ligands (97 aa)
HNRNPA0Heterogeneous nuclear ribonucleoprotein A0; mRNA-binding component of ribonucleosomes. Specifically binds AU-rich element (ARE)-containing mRNAs. Involved in post- transcriptional regulation of cytokines mRNAs (305 aa)
CXCR2C-X-C chemokine receptor type 2; Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2 (360 aa)
XCL2Cytokine SCM-1 beta; Chemotactic activity for lymphocytes but not for monocytes or neutrophils; Chemokine ligands (114 aa)
CCL25C-C motif chemokine 25; Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Isoform 2 is an antagonist of isoform 1. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4; Belongs to the intercrine beta (chemokine CC) family (150 aa)
CCL5C-C motif chemokine 5; Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1- infection. The secon [...] (91 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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