CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014756
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Gelsolin 
Protein Synonyms/Alias
 Actin-depolymerizing factor; ADF; Brevin 
Gene Name
 Gsn 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
175GGVASGFKHVVPNEVacetylation[1]
175GGVASGFKHVVPNEVubiquitination[2]
243LKATQVSKGIRDNERubiquitination[2]
297AANRRLAKLYKVSNSacetylation[1]
339LDHGRDGKIFVWKGKacetylation[1]
358DERKAALKTASDFISacetylation[1]
366TASDFISKMQYPRQTacetylation[1]
366TASDFISKMQYPRQTubiquitination[2]
388GGETPLFKQFFKNWRacetylation[1]
392PLFKQFFKNWRDPDQacetylation[1]
546GKPMIIYKGGTSRDGacetylation[1]
582RAVEVMPKAGALNSNacetylation[1]
621TGALELLKVLRAQHVacetylation[1]
726TEALTSAKRYIETDPubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
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 (By similarity). 
Sequence Annotation
 REPEAT 74 124 Gelsolin-like 1.
 REPEAT 196 236 Gelsolin-like 2.
 REPEAT 312 354 Gelsolin-like 3.
 REPEAT 451 502 Gelsolin-like 4.
 REPEAT 574 614 Gelsolin-like 5.
 REPEAT 677 719 Gelsolin-like 6.
 REGION 51 174 Actin-severing (Potential).
 REGION 121 124 Actin-actin interfilament contact point
 REGION 160 167 Polyphosphoinositide binding (By
 REGION 186 194 Polyphosphoinositide binding (By
 REGION 432 780 Actin-binding, Ca-sensitive (Potential).
 METAL 469 469 Calcium 1; via carbonyl oxygen (By
 METAL 470 470 Calcium 1 (By similarity).
 METAL 500 500 Calcium 1 (By similarity).
 METAL 549 549 Calcium 1; via carbonyl oxygen (By
 METAL 589 589 Calcium 2 (By similarity).
 METAL 589 589 Calcium 2; via carbonyl oxygen (By
 METAL 590 590 Calcium 2 (By similarity).
 METAL 612 612 Calcium 2 (By similarity).
 METAL 694 694 Calcium 3; via carbonyl oxygen (By
 METAL 695 695 Calcium 3 (By similarity).
 METAL 717 717 Calcium 3 (By similarity).
 MOD_RES 84 84 Phosphotyrosine (By similarity).
 MOD_RES 407 407 Phosphotyrosine (By similarity).
 MOD_RES 463 463 Phosphotyrosine (By similarity).
 MOD_RES 601 601 Phosphotyrosine (By similarity).
 MOD_RES 649 649 Phosphotyrosine (By similarity).
 DISULFID 213 226 By similarity.  
Keyword
 Actin capping; Actin-binding; Alternative initiation; Calcium; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 780 AA 
Protein Sequence
MAPYCSSLRS ALLVLALCAL SPSHAATASR GRAQERAPQS RVSETRPSTM VVEHPEFLKA 60
GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ LRNGNLQYDL HYWLGNECSQ 120
DESGAAAIFT VQLDDYLNGR AVQHREVQGF ESSTFQGYFK SGLKYKKGGV ASGFKHVVPN 180
EVVVQRLFQV KGRRVVRATE VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ 240
VSKGIRDNER SGRAQVHVSE EGSEPEAMLQ VLGPKPDLPQ GTEDTAKEDA ANRRLAKLYK 300
VSNSGGSMSV SLVADENPFA QSALRSEDCF ILDHGRDGKI FVWKGKQANM DERKAALKTA 360
SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT DGPGLSYLSS HIANVERVPF 420
DAATLHTSTA MAAQHGMDDD GTGQKQIWRI EGSNKVLVDP ATYGQFYGGD SYIILYNYRH 480
GGRQGQIIYN WQGAQSTQDE VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK 540
PMIIYKGGTS RDGGQTTPAS TRLFQVRASS SGATRAVEVM PKAGALNSND AFVLKTPSAA 600
YLWVGTGASD AEKTGALELL KVLRAQHVQV EEGSEPDGFW EALGGKTAYR TSPRLKDKKM 660
DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD TWDQVFVWVG KDSQEEEKTE 720
ALTSAKRYIE TDPANRDRRT PITVVRQGFE PPSFVGWFLG WDDDYWSVDP LDRALAELAA 780 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:RGD.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0001726; C:ruffle; IDA:RGD.
 GO:0003779; F:actin binding; IDA:RGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
 GO:0051014; P:actin filament severing; ISS:UniProtKB.
 GO:0007568; P:aging; IEP:RGD.
 GO:0006915; P:apoptotic process; IDA:RGD.
 GO:0071276; P:cellular response to cadmium ion; IDA:RGD.
 GO:0060271; P:cilium morphogenesis; ISS:UniProtKB.
 GO:0014003; P:oligodendrocyte development; IEP:RGD.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:RGD.
 GO:0030155; P:regulation of cell adhesion; IMP:RGD.
 GO:0045471; P:response to ethanol; IEP:RGD.
 GO:0051593; P:response to folic acid; IEP:RGD.
 GO:0042246; P:tissue regeneration; IEP:RGD.
 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.