CHRNA7 report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of CHRNA7 at tissue level.

III. Associated gene sets

GO_0042391Biological processregulation of membrane potential
GO_0051247Biological processpositive regulation of protein metabolic process
GO_0007611Biological processlearning or memory
GO_0045766Biological processpositive regulation of angiogenesis
GO_0060079Biological processexcitatory postsynaptic potential
GO_0007165Biological processsignal transduction
GO_0034220Biological processmonoatomic ion transmembrane transport
GO_0006811Biological processmonoatomic ion transport
GO_0095500Biological processacetylcholine receptor signaling pathway
GO_1902430Biological processnegative regulation of amyloid-beta formation
GO_1905906Biological processregulation of amyloid fibril formation
GO_1904645Biological processresponse to amyloid-beta
GO_0006874Biological processintracellular calcium ion homeostasis
GO_0001934Biological processpositive regulation of protein phosphorylation
GO_0043410Biological processpositive regulation of MAPK cascade
GO_1905920Biological processpositive regulation of CoA-transferase activity
GO_2000463Biological processpositive regulation of excitatory postsynaptic potential
GO_0098815Biological processmodulation of excitatory postsynaptic potential
GO_0050893Biological processsensory processing
GO_1905144Biological processresponse to acetylcholine
GO_0097061Biological processdendritic spine organization
GO_1902004Biological processpositive regulation of amyloid-beta formation
GO_0007268Biological processchemical synaptic transmission
GO_0001666Biological processresponse to hypoxia
GO_0035094Biological processresponse to nicotine
GO_0140059Biological processdendrite arborization
GO_1900273Biological processpositive regulation of long-term synaptic potentiation
GO_0007613Biological processmemory
GO_0008284Biological processpositive regulation of cell population proliferation
GO_0050890Biological processcognition
GO_0032720Biological processnegative regulation of tumor necrosis factor production
GO_0050808Biological processsynapse organization
GO_0070374Biological processpositive regulation of ERK1 and ERK2 cascade
GO_0007271Biological processsynaptic transmission, cholinergic
GO_0006816Biological processcalcium ion transport
GO_0007614Biological processshort-term memory
GO_0070588Biological processcalcium ion transmembrane transport
GO_1902991Biological processregulation of amyloid precursor protein catabolic process
GO_0005886Cellular componentplasma membrane
GO_0016020Cellular componentmembrane
GO_0098794Cellular componentpostsynapse
GO_0043005Cellular componentneuron projection
GO_0044853Cellular componentplasma membrane raft
GO_0045202Cellular componentsynapse
GO_0045211Cellular componentpostsynaptic membrane
GO_0005892Cellular componentacetylcholine-gated channel complex
GO_0042803Molecular functionprotein homodimerization activity
GO_0005216Molecular functionmonoatomic ion channel activity
GO_0001540Molecular functionamyloid-beta binding
GO_0015464Molecular functionacetylcholine receptor activity
GO_0017081Molecular functionchloride channel regulator activity
GO_0042166Molecular functionacetylcholine binding
GO_0015643Molecular functiontoxic substance binding
GO_0022848Molecular functionacetylcholine-gated monoatomic cation-selective channel activity
GO_0005515Molecular functionprotein binding
GO_0005262Molecular functioncalcium channel activity

IV. Literature review

[source]
Gene nameCHRNA7
Protein nameAlpha-7 nicotinic cholinergic receptor subunit
Cholinergic receptor nicotinic alpha 7 subunit
Neuronal acetylcholine receptor subunit alpha-7
SynonymsNACHRA7
DescriptionFUNCTION: 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. The channel is blocked by alpha-bungarotoxin.

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

FUNCTION: 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. The channel is blocked by alpha-bungarotoxin. .

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A0A1B0GU04
ENST00000638106.1
ENST00000635722.1
A0A1B0GU11
Q693P7
ENST00000638081.1
A0A1B0GV44
A0A1B0GUR5
ENST00000635759.1
ENST00000306901.9 [P36544-1]
ENST00000675428.1 [P36544-2]
A0A1B0GV43
ENST00000637350.1
ENST00000645153.1
ENST00000454250.7 [P36544-2]
ENST00000637971.1
ENST00000637552.1
ENST00000632335.2
A0A1B0GVN6
ENST00000437966.3 [P36544-3]
A0A1B0GVP9
ENST00000636440.1
ENST00000635883.1
ENST00000637786.2
A0A1B0GVI5
ENST00000637183.1
A0A1B0GVH2
ENST00000636850.1
A0A1B0GWH1
ENST00000637519.1
ENST00000455693.3 [P36544-1]
ENST00000636271.1
A0A1B0GV25
A0A1B0GV86
A0A1B0GTE0
ENST00000636603.1
ENST00000635884.1
ENST00000635978.1
ENST00000638031.1
A0A1B0GU93
ENST00000636044.1
A0A1B0GW47
ENST00000637348.1
A0A1B0GTT0
ENST00000637033.1
A0A1B0GTT9
A0A1B0GU56
Q5W554
A0A1W2PN81
P36544