Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Gelsolin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Gelsolin a 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. Its expression is significantly decreased in many tumors and transformed cell lines. Gelsolin and other proteins including E-cadherin, BRCA, p21WAF, HoxA5, and retinoic acid receptor II are regulated by epigenetic changes in breast cancers. Gelsolin helps mediate the ability of HDAC inhibitors to protect neurons from oxygen/glucose deprivation. Two human isoforms are produced by alternative initiation. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Secreted, signal peptide; Actin binding protein; Nuclear receptor co-regulator; Secreted
Cellular Component: ruffle; protein complex; perinuclear region of cytoplasm; lamellipodium; extracellular region; cytosol; actin cytoskeleton
Molecular Function: protein binding; calcium ion binding; actin binding
Biological Process: regulation of cell adhesion; actin filament severing; phosphoinositide-mediated signaling; apoptosis; vesicle-mediated transport; response to ethanol; actin filament polymerization; tissue regeneration; response to folic acid; barbed-end actin filament capping; oligodendrocyte development; cell structure disassembly during apoptosis; aging
Reference #:  P06396 (UniProtKB)
Alt. Names/Synonyms: Actin-depolymerizing factor; ADF; AGEL; Brevin; DKFZp313L0718; GELS; Gelsolin; gelsolin (amyloidosis, Finnish type); GSN
Gene Symbols: GSN
Molecular weight: 85,698 Da
Basal Isoelectric point: 5.9  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Gelsolin

Protein Structure Not Found.


STRING  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  NURSA


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S35-ga ATASRGAsQAGAPQG
0 1 S51-p VPEARPNsMVVEHPE
1 0 Y86-p VPVPTNLyGDFFTGD
0 1 K177 GGVASGFKHVVPNEV
0 1 K193 VQRLFQVKGRRVVRA
0 1 K245-ac LKATQVSkGIRDNER
0 4 K245 LKATQVSKGIRDNER
0 1 S261-p GRARVHVsEEGtEPE
0 1 T265-p VHVsEEGtEPEAMLQ
0 1 T309 KVSNGAGTMSVSLVA
0 2 K360-ub EERKAALkTASDFIT
0 7 K368-ub TASDFITkMDYPkQT
0 2 K373-ub ITkMDYPkQTQVSVL
0 1 T386 VLPEGGETPLFkQFF
0 6 K390-ac GGETPLFkQFFKNWR
1 0 Y409-p TDGLGLSyLSSHIAN
0 1 T431-ga AATLHTStAMAAQHG
2 1 Y465-p VPVDPATyGQFYGGD
0 1 S473-p GQFYGGDsYIILyNy
0 1 Y478-p GDsYIILyNyRHGGR
0 1 Y480-p sYIILyNyRHGGRQG
0 2 K584-ub RAVEVLPkAGALNSN
0 2 K597 SNDAFVLKTPSAAyL
1 31 Y603-p LKTPSAAyLWVGTGA
0 1 K648-ac FWEALGGkAAyRTSP
1 0 Y651-p ALGGkAAyRTSPRLK
0 1 K728-ac TEALTSAkRYIETDP
0 1 K728-ub TEALTSAkRYIETDP
0 1 T742-p PANRDRRtPITVVKQ
  mouse

 
A33 ATTSRGRAQERAPQS
T49 VSEARPSTMVVEHPE
Y84 VPVPPNLYGDFFTGD
K175-ub GGVASGFkHVVPNEV
K191-ub VQRLFQVkGRRVVRA
K243 LKATQVSKGIRDNER
K243-ub LKATQVSkGIRDNER
S259 GRAQVHVSEEGGEPE
G263 VHVSEEGGEPEAMLQ
S307-p KVSNGAGsMSVSLVA
K358-ub EERKAALkTASDFIS
K366-ub TASDFISkMQYPRQT
R371 ISkMQYPRQTQVSVL
T384-p VLPEGGEtPLFKQFF
K388 GGEtPLFKQFFKNWR
Y407 TDGPGLGYLSSHIAN
T429 AATLHTSTAMAAQHG
Y463 VPVDPATYGQFYGGD
S471 GQFYGGDSYIILYNY
Y476 GDSYIILYNYRHGGR
Y478 SYIILYNYRHGGRQG
K582-ub RAVEVMPkSGALNSN
K595-ub SNDAFVLkTPSAAYL
Y601 LkTPSAAYLWVGAGA
K646 FWEALGGKTAYRTSP
Y649 ALGGKTAYRTSPRLK
K726 TEALTSAKRYIETDP
K726 TEALTSAKRYIETDP
T740 PANRDRRTPITVVRQ
  rat

 
A33 ATASRGRAQERAPQS
T49 VSETRPSTMVVEHPE
Y84 VPVPPNLYGDFFTGD
K175 GGVASGFKHVVPNEV
K191 VQRLFQVKGRRVVRA
K243 LKATQVSKGIRDNER
K243 LKATQVSKGIRDNER
S259 GRAQVHVSEEGSEPE
S263 VHVSEEGSEPEAMLQ
S307 KVSNSGGSMSVSLVA
K358 DERKAALKTASDFIS
K366-ub TASDFISkMQYPRQT
R371 ISkMQYPRQTQVSVL
T384 VLPEGGETPLFkQFF
K388-ac GGETPLFkQFFKNWR
Y407 TDGPGLSYLSSHIAN
T429 AATLHTSTAMAAQHG
Y463 VLVDPATYGQFYGGD
S471 GQFYGGDSYIILYNY
Y476 GDSYIILYNYRHGGR
Y478 SYIILYNYRHGGRQG
K582 RAVEVMPKAGALNSN
K595 SNDAFVLKTPSAAYL
Y601 LKTPSAAYLWVGTGA
K646 FWEALGGKTAYRTSP
Y649 ALGGKTAYRTSPRLK
K726 TEALTSAKRYIETDP
K726 TEALTSAKRYIETDP
T740 PANRDRRTPITVVRQ
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.