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C5 C5 CHRM2 CHRM2 CXCL16 CXCL16 CCL5 CCL5 POMC POMC CXCL10 CXCL10 PNOC PNOC CXCL13 CXCL13 PDYN PDYN APLN APLN P2RY14 P2RY14 HEBP1 HEBP1 C3AR1 C3AR1 BDKRB2 BDKRB2 FPR1 FPR1 MTNR1B MTNR1B CXCL11 CXCL11 C3 C3 MTNR1A MTNR1A P2RY12 P2RY12 IL8 IL8 S1PR1 S1PR1 ADCY4 ADCY4 CXCR2 CXCR2 CXCL6 CXCL6 ADCY6 ADCY6
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:
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 (189 aa)
PDYNprodynorphin; Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity) (254 aa)
C5complement component 5; 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 (1676 aa)
CXCL6chemokine (C-X-C motif) ligand 6; Chemotactic for neutrophil granulocytes (114 aa)
C3complement component 3; C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates (1663 aa)
MTNR1Bmelatonin receptor 1B; High affinity receptor for melatonin. Likely to mediates the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity (362 aa)
POMCproopiomelanocortin; ACTH stimulates the adrenal glands to release cortisol (267 aa)
CXCL13chemokine (C-X-C motif) ligand 13; Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils. Does not induce calcium release in B- lymphocytes. Binds to BLR1/CXCR5 (109 aa)
CCL5chemokine (C-C motif) ligand 5; Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. Binds to 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 second processed form RANTES(4-68) exh [...] (91 aa)
CXCL16chemokine (C-X-C motif) ligand 16; Acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis (By similarity). Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo (273 aa)
PNOCprepronociceptin; Nociceptin is the ligand of the opioid receptor-like receptor (OPRL1). It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development (By similarity) (176 aa)
C3AR1complement component 3a receptor 1; Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production (482 aa)
FPR1formyl peptide receptor 1; High affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (350 aa)
MTNR1Amelatonin receptor 1A; High affinity receptor for melatonin. Likely to mediates the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity (350 aa)
S1PR1sphingosine-1-phosphate receptor 1; Receptor for the lysosphingolipid sphingosine 1- phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. This inducible epithelial cell G-protein-coupled receptor may be involved in the processes that regulate the differentiation of endothelial cells. Seems to be coupled to the G(i) subclass of heteromeric G proteins (382 aa)
APLNapelin; Endogenous ligand for APJ, an alternative coreceptor with CD4 for HIV-1 infection. Inhibits HIV-1 entry in cells coexpressing CD4 and APJ. Apelin-36 has a greater inhibitory activity on HIV infection than other synthetic apelin derivatives. The oral intake in the colostrum and the milk could have a role in the modulation of the immune responses in neonates. May also have a role in the central control of body fluid homeostasis by influencing AVP release and drinking behavior (77 aa)
CXCL10chemokine (C-X-C motif) ligand 10; Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3 (98 aa)
IL8interleukin 8 (99 aa)
CXCL11chemokine (C-X-C motif) ligand 11; Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses (94 aa)
P2RY12purinergic receptor P2Y, G-protein coupled, 12; Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Involved in platelet aggregation (342 aa)
BDKRB2bradykinin receptor B2; Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system (391 aa)
P2RY14purinergic receptor P2Y, G-protein coupled, 14; Receptor for UDP-glucose and other UDP-sugar coupled to G-proteins. Not activated by ATP, ADP, UTP or ATP (338 aa)
ADCY6adenylate cyclase 6; Membrane-bound, calcium-inhibitable adenylyl cyclase (By similarity) (1168 aa)
ADCY4adenylate cyclase 4; This is a membrane-bound, calmodulin-insensitive adenylyl cyclase (By similarity) (1077 aa)
CXCR2chemokine (C-X-C motif) receptor 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)
CHRM2cholinergic receptor, muscarinic 2; The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition (466 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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