UniProt Accession

 GELS_HUMAN; P06396; A2A418; A8MUD1; A8MYN7; B7Z373; Q5T0I2; Q8WVV7 

Genbank Protein ID

 X04412; AK096280; AK125819; AK295572; AK315494; AL137068; AL513122; AL513122; CH471090; CH471090; CH471090; BC017491; BC026033 

Genbank Nucleotide ID

 CAA28000.1; BAG53247.1; BAG54252.1; BAH12109.1; BAG37878.1; CAI14413.1; CAM20459.1; EAW87489.1; EAW87490.1; EAW87491.1; AAH17491.1; AAH26033.1 

Protein Name

 Gelsolin 

Protein Synonyms/Alias

 AGEL; Actin-depolymerizing factor; ADF; Brevin 

Gene Name

 GSN 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
61	VEHPEFLKAGKEPGL	acetylation	[1]
368	TASDFITKMDYPKQT	ubiquitination	[2, 3]
373	ITKMDYPKQTQVSVL	ubiquitination	[4]
584	RAVEVLPKAGALNSN	ubiquitination	[2, 3]
728	TEALTSAKRYIETDP	ubiquitination	[4]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional Description

 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. 

Sequence Annotation

 REPEAT 76 126 Gelsolin-like 1.
 REPEAT 198 238 Gelsolin-like 2.
 REPEAT 314 356 Gelsolin-like 3.
 REPEAT 453 504 Gelsolin-like 4.
 REPEAT 576 616 Gelsolin-like 5.
 REPEAT 679 721 Gelsolin-like 6.
 REGION 53 176 Actin-severing (Potential).
 REGION 123 126 Actin-actin interfilament contact point.
 REGION 162 169 Polyphosphoinositide binding (By
 REGION 188 196 Polyphosphoinositide binding (By
 REGION 434 782 Actin-binding, Ca-sensitive (Potential).
 METAL 471 471 Calcium 1; via carbonyl oxygen.
 METAL 472 472 Calcium 1.
 METAL 502 502 Calcium 1.
 METAL 551 551 Calcium 1; via carbonyl oxygen.
 METAL 591 591 Calcium 2.
 METAL 591 591 Calcium 2; via carbonyl oxygen.
 METAL 592 592 Calcium 2.
 METAL 614 614 Calcium 2.
 METAL 696 696 Calcium 3; via carbonyl oxygen.
 METAL 697 697 Calcium 3.
 METAL 719 719 Calcium 3.
 MOD_RES 86 86 Phosphotyrosine; by SRC; in vitro.
 MOD_RES 409 409 Phosphotyrosine; by SRC; in vitro.
 MOD_RES 465 465 Phosphotyrosine; by SRC.
 MOD_RES 603 603 Phosphotyrosine; by SRC; in vitro.
 MOD_RES 651 651 Phosphotyrosine; by SRC; in vitro.
 DISULFID 215 228 In isoform 1.  

Keyword

 3D-structure; Actin capping; Actin-binding; Alternative initiation; Alternative splicing; Amyloid; Amyloidosis; Calcium; Cilium biogenesis/degradation; Complete proteome; Corneal dystrophy; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Disulfide bond; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 782 AA 

Protein Sequence

Gene Ontology

 GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0001726; C:ruffle; IEA:Compara.
 GO:0005509; F:calcium ion binding; TAS:ProtInc.
 GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
 GO:0051014; P:actin filament severing; IDA:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0051016; P:barbed-end actin filament capping; TAS:ProtInc.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0071276; P:cellular response to cadmium ion; IEA:Compara.
 GO:0060271; P:cilium morphogenesis; IMP:UniProtKB.
 GO:0014003; P:oligodendrocyte development; IEA:Compara.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:Compara.
 GO:0030155; P:regulation of cell adhesion; IEA:Compara.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0051593; P:response to folic acid; IEA:Compara.
 GO:0042246; P:tissue regeneration; IEA:Compara.
 GO:0016192; P:vesicle-mediated transport; IEA:Compara. 

Interpro

 IPR007123; Gelsolin_dom.
 IPR007122; Villin/Gelsolin. 

Pfam

 PF00626; Gelsolin 

SMART

 SM00262; GEL 

PROSITE

  

PRINTS

 PR00597; GELSOLIN.