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SLC6A3 SLC6A3 CHRNA6 CHRNA6 ADRA2A ADRA2A CHRNB3 CHRNB3 CHRNA5 CHRNA5 NLGN2 NLGN2 DRD2 DRD2 RAB3B RAB3B FLOT1 FLOT1 ADRA1A ADRA1A SLC18A2 SLC18A2
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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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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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SLC6A3Sodium-dependent dopamine transporter; Amine transporter. Terminates the action of dopamine by its high affinity sodium-dependent reuptake into presynaptic terminals. (620 aa)
CHRNA6Neuronal acetylcholine receptor subunit alpha-6; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane; Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-6/CHRNA6 sub- subfamily. (494 aa)
ADRA2AAlpha-2A adrenergic receptor; Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p- octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol. (465 aa)
CHRNB3Neuronal acetylcholine receptor subunit beta-3; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. (458 aa)
CHRNA5Neuronal acetylcholine receptor subunit alpha-5; After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. (468 aa)
NLGN2Neuroligin-2; Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Promotes clustering of postsynaptic LHFPL4 (By similarity). Modulates signaling by inhibitory synapses [...] (835 aa)
DRD2D(2) dopamine receptor; Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase; Belongs to the G-protein coupled receptor 1 family. (443 aa)
RAB3BRas-related protein Rab-3B; Protein transport. Probably involved in vesicular traffic (By similarity); Belongs to the small GTPase superfamily. Rab family. (219 aa)
FLOT1Flotillin-1; May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. (427 aa)
ADRA1AAlpha-1A adrenergic receptor; This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes. Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1A sub-subfamily. (475 aa)
SLC18A2Synaptic vesicular amine transporter; Involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters. Pumps cytosolic monoamines including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. Requisite for vesicular amine storage prior to secretion via exocytosis. (514 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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