Home

gelsolin (human)

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: Secreted; Motility/polarity/chemotaxis; Actin binding protein; Secreted, signal peptide; Nuclear receptor co-regulator Cellular Component: ruffle; extracellular space; 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; oligodendrocyte development; barbed-end actin filament capping; 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:  Regulation of Actin Dynamics Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below gelsolin 1C0F - S=53-176 (human) 1C0G - S=53-176 (human) 1D4X - G=52-177 (human) 1DEJ - S=53-176 (human) 1EQY - S=52-176 (human) 1ESV - S=52-176 (human) 1H1V - G=439-769 (human) 1KCQ - A=185-288 (human) 1MDU - A/D=52-176 (human) 1NLV - G=52-176 (human) 1NM1 - G=52-176 (human) 1NMD - G=52-176 (human) 1P8X - A/B/C=439-782 (human) 1P8Z - G=52-187 (human) 1SOL - A=177-196 (human) 1T44 - G=55-183 (human) 1YAG - G=52-176 (human) 1YVN - G=52-176 (human) 2FF3 - A=51-179 (human) 2FF6 - G=51-179 (human) 2FH1 - A/B/C=439-782 (human) 2FH2 - A/B/C=439-782 (human) 2FH3 - A/B/C=439-782 (human) 2FH4 - A/B/C=439-782 (human) 3A5L - S=53-176 (human) 3A5M - S=53-176 (human) 3A5N - S=53-176 (human) 3A5O - S=53-176 (human) 3CI5 - G=52-176 (human) 3CIP - G=52-176 (human) 3FFK - A/D=52-426 (human) 3FFN - A/B=1-782 (human) 3TU5 - B=21-44 (human) 1NPH - A=439-767 (mouse)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1C0F 1C0G 1D4X 1DEJ 1EQY 1ESV 1H1V 1KCQ 1MDU 1NLV 1NM1 1NMD 1P8X 1P8Z 1SOL 1T44 1YAG 1YVN 2FF3 2FF6 2FH1 2FH2 2FH3 2FH4 3A5L 3A5M 3A5N 3A5O 3CI5 3CIP 3FFK 3FFN 3TU5  |  Phospho3D  |  DISEASE 105120 137350  |  Source  |  NURSA  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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		S51-p	VPEARPNsMVVEHPE
1	0		Y86-p	VPVPTNLyGDFFTGD
0	1		K177	GGVASGFKHVVPNEV
0	1		K193	VQRLFQVKGRRVVRA
0	1		K245-a	LKATQVSkGIRDNER
0	4		K245	LKATQVSKGIRDNER
0	1		S261-p	GRARVHVsEEGtEPE
0	1		T265-p	VHVsEEGtEPEAMLQ
0	1		T309	KVSNGAGTMSVSLVA
0	2		K360-u	EERKAALkTASDFIT
0	7		K368-u	TASDFITkMDYPkQT
0	2		K373-u	ITkMDYPkQTQVSVL
0	6		K390-a	GGETPLFkQFFKNWR
1	0		Y409-p	TDGLGLSyLSSHIAN
1	1		Y465-p	VPVDPATyGQFYGGD
0	1		S473-p	GQFYGGDsYIILyNy
0	1		Y478-p	GDsYIILyNyRHGGR
0	1		Y480-p	sYIILyNyRHGGRQG
0	2		K584-u	RAVEVLPkAGALNSN
0	2		K597	SNDAFVLKTPSAAyL
1	27		Y603-p	LKTPSAAyLWVGTGA
0	1		K648-a	FWEALGGkAAyRTSP
1	0		Y651-p	ALGGkAAyRTSPRLK
0	1		K728-a	TEALTSAkRYIETDP
0	1		K728-u	TEALTSAkRYIETDP

	mouse
T49	VSEARPSTMVVEHPE
Y84	VPVPPNLYGDFFTGD
K175-u	GGVASGFkHVVPNEV
K191-u	VQRLFQVkGRRVVRA
K243	LKATQVSKGIRDNER
K243-u	LKATQVSkGIRDNER
S259	GRAQVHVSEEGGEPE
G263	VHVSEEGGEPEAMLQ
S307-p	KVSNGAGsMSVSLVA
K358-u	EERKAALkTASDFIS
K366-u	TASDFISkMQYPRQT
R371	ISkMQYPRQTQVSVL
K388	GGETPLFKQFFKNWR
Y407	TDGPGLGYLSSHIAN
Y463	VPVDPATYGQFYGGD
S471	GQFYGGDSYIILYNY
Y476	GDSYIILYNYRHGGR
Y478	SYIILYNYRHGGRQG
K582-u	RAVEVMPkSGALNSN
K595-u	SNDAFVLkTPSAAYL
Y601	LkTPSAAYLWVGAGA
K646	FWEALGGKTAYRTSP
Y649	ALGGKTAYRTSPRLK
K726	TEALTSAKRYIETDP
K726	TEALTSAKRYIETDP

	rat
T49	VSETRPSTMVVEHPE
Y84	VPVPPNLYGDFFTGD
K175	GGVASGFKHVVPNEV
K191	VQRLFQVKGRRVVRA
K243	LKATQVSKGIRDNER
K243	LKATQVSKGIRDNER
S259	GRAQVHVSEEGSEPE
S263	VHVSEEGSEPEAMLQ
S307	KVSNSGGSMSVSLVA
K358	DERKAALKTASDFIS
K366-u	TASDFISkMQYPRQT
R371	ISkMQYPRQTQVSVL
K388-a	GGETPLFkQFFKNWR
Y407	TDGPGLSYLSSHIAN
Y463	VLVDPATYGQFYGGD
S471	GQFYGGDSYIILYNY
Y476	GDSYIILYNYRHGGR
Y478	SYIILYNYRHGGRQG
K582	RAVEVMPKAGALNSN
K595	SNDAFVLKTPSAAYL
Y601	LKTPSAAYLWVGTGA
K646	FWEALGGKTAYRTSP
Y649	ALGGKTAYRTSPRLK
K726	TEALTSAKRYIETDP
K726	TEALTSAKRYIETDP

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.