CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002337
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
194LKATQVSKGIRDNERubiquitination[1]
251RKLAKLYKVSNGAGTubiquitination[1]
309EERKAALKTASDFITubiquitination[1]
317TASDFITKMDYPKQTubiquitination[1]
322ITKMDYPKQTQVSVLubiquitination[1]
597FWEALGGKAAYRTSPubiquitination[1]
677TEALTSAKRYIETDPubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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
MVVEHPEFLK AGKEPGLQIW RVEKFDLVPV PTNLYGDFFT GDAYVILKTV QLRNGNLQYD 60
LHYWLGNECS QDESGAAAIF TVQLDDYLNG RAVQHREVQG FESATFLGYF KSGLKYKKGG 120
VASGFKHVVP NEVVVQRLFQ VKGRRVVRAT EVPVSWESFN NGDCFILDLG NNIHQWCGSN 180
SNRYERLKAT QVSKGIRDNE RSGRARVHVS EEGTEPEAML QVLGPKPALP AGTEDTAKED 240
AANRKLAKLY KVSNGAGTMS VSLVADENPF AQGALKSEDC FILDHGKDGK IFVWKGKQAN 300
TEERKAALKT ASDFITKMDY PKQTQVSVLP EGGETPLFKQ FFKNWRDPDQ TDGLGLSYLS 360
SHIANVERVP FDAATLHTST AMAAQHGMDD DGTGQKQIWR IEGSNKVPVD PATYGQFYGG 420
DSYIILYNYR HGGRQGQIIY NWQGAQSTQD EVAASAILTA QLDEELGGTP VQSRVVQGKE 480
PAHLMSLFGG KPMIIYKGGT SREGGQTAPA STRLFQVRAN SAGATRAVEV LPKAGALNSN 540
DAFVLKTPSA AYLWVGTGAS EAEKTGAQEL LRVLRAQPVQ VAEGSEPDGF WEALGGKAAY 600
RTSPRLKDKK MDAHPPRLFA CSNKIGRFVI EEVPGELMQE DLATDDVMLL DTWDQVFVWV 660
GKDSQEEEKT EALTSAKRYI ETDPANRDRR TPITVVKQGF EPPSFVGWFL GWDDDYWSVD 720
PLDRAMAELA A 731 
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.