GSN report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_1903903Biological processregulation of establishment of T cell polarity
GO_0060271Biological processcilium assembly
GO_0035994Biological processresponse to muscle stretch
GO_1903923Biological processpositive regulation of protein processing in phagocytic vesicle
GO_0071801Biological processregulation of podosome assembly
GO_0051016Biological processbarbed-end actin filament capping
GO_0014891Biological processstriated muscle atrophy
GO_0030042Biological processactin filament depolymerization
GO_0010628Biological processpositive regulation of gene expression
GO_0030041Biological processactin filament polymerization
GO_1902174Biological processpositive regulation of keratinocyte apoptotic process
GO_0030031Biological processcell projection assembly
GO_0022617Biological processextracellular matrix disassembly
GO_0051693Biological processactin filament capping
GO_0046597Biological processnegative regulation of viral entry into host cell
GO_0031648Biological processprotein destabilization
GO_0055119Biological processrelaxation of cardiac muscle
GO_0086003Biological processcardiac muscle cell contraction
GO_0008154Biological processactin polymerization or depolymerization
GO_0006911Biological processphagocytosis, engulfment
GO_0042989Biological processsequestering of actin monomers
GO_0051014Biological processactin filament severing
GO_1990000Biological processamyloid fibril formation
GO_0051127Biological processpositive regulation of actin nucleation
GO_0097284Biological processhepatocyte apoptotic process
GO_2001269Biological processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway
GO_0007015Biological processactin filament organization
GO_1903909Biological processregulation of receptor clustering
GO_0007417Biological processcentral nervous system development
GO_0097017Biological processrenal protein absorption
GO_0071346Biological processcellular response to type II interferon
GO_1903906Biological processregulation of plasma membrane raft polarization
GO_0005615Cellular componentextracellular space
GO_0016528Cellular componentsarcoplasm
GO_0005576Cellular componentextracellular region
GO_0005886Cellular componentplasma membrane
GO_0030478Cellular componentactin cap
GO_0002102Cellular componentpodosome
GO_0070062Cellular componentextracellular exosome
GO_0030864Cellular componentcortical actin cytoskeleton
GO_0034774Cellular componentsecretory granule lumen
GO_0005925Cellular componentfocal adhesion
GO_0072562Cellular componentblood microparticle
GO_0015629Cellular componentactin cytoskeleton
GO_1904813Cellular componentficolin-1-rich granule lumen
GO_0005829Cellular componentcytosol
GO_0045335Cellular componentphagocytic vesicle
GO_0005737Cellular componentcytoplasm
GO_0030027Cellular componentlamellipodium
GO_0005634Cellular componentnucleus
GO_0045159Molecular functionmyosin II binding
GO_0005546Molecular functionphosphatidylinositol-4,5-bisphosphate binding
GO_0051015Molecular functionactin filament binding
GO_0036313Molecular functionphosphatidylinositol 3-kinase catalytic subunit binding
GO_0005509Molecular functioncalcium ion binding
GO_0005515Molecular functionprotein binding
GO_0003779Molecular functionactin binding

IV. Literature review

[source]
Gene nameGSN
Protein nameGelsolin (ADF) (Actin-depolymerizing factor)
Gelsolin
Gelsolin (AGEL) (Actin-depolymerizing factor) (ADF) (Brevin)
Synonyms
DescriptionFUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed . Plays a role in ciliogenesis . .

FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. .

FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. .

FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. .

FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. .

FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. .

AccessionsP06396
ENST00000432226.7 [P06396-2]
ENST00000545652.6 [P06396-4]
A0A8V8TND7
A0A0U1RQL8
Q5T0H8
ENST00000477104.2
A0A0A0MT01
ENST00000373808.8 [P06396-3]
ENST00000373818.8 [P06396-1]
ENST00000432226
A0A0A0MS51
ENST00000394353.7
ENST00000449733.7
Q5T0I0
ENST00000699558.1
ENST00000373823.7 [P06396-2]
ENST00000373806.1