Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Gelsolin  

UniProtKB / Swiss-Prot ID :  GELS_HUMAN

Gene Name (Synonyms) : 
GSN  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted. 

Protein Function :  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. 

Protein Sequence MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQI...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHCCCCCCCEE...
Protein Variant
LocationDescription
22S -> L (in a breast cancer sample;somatic mutation).
129A -> T (in dbSNP:rs2230287). VAR_024690
201T -> I (in a breast cancer sample;somatic mutation).
214D -> N (in AMYL5). VAR_007718
214D -> Y (in AMYL5). VAR_007719
231N -> D (in dbSNP:rs11550199). VAR_061982
611S -> N (in a breast cancer sample;somatic mutation).
668R -> L (in dbSNP:rs9696578). VAR_033958
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
61N6-acetyllysinePEFLKAGKE
HHHHHCCCC
61.49HPRD
Link
86PhosphotyrosinePTNLYGDFF
CHHHCCCEE
19.40Phosphositeplus
Link
86Phosphotyrosine; by SRC; in vitro.PTNLYGDFF
CHHHCCCEE
19.40UniProtKB
Link
215S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)NNGDCFILD
CCCCEEEEE
2.12HPRD
Link-
228S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)IHQWCGSNS
EEEEECCCC
3.26HPRD
Link-
261PhosphoserineRVHVSEEGT
EEEEEECCC
18.30HPRD
Link-
261PhosphoserineRVHVSEEGT
EEEEEECCC
18.30Phosphositeplus
Link-
361PhosphothreonineAALKTASDF
HHHHHHHHH
32.04HPRD
Link-
368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DFITKMDYP
HHHHHCCCC
25.59Phosphositeplus
Link-
373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MDYPKQTQV
CCCCCCCEE
60.80Phosphositeplus
Link-
403nonePDQTDGLGL
CCCCCCCCC
44.69HPRD
Link-
404N-myristoyl glycineDQTDGLGLS
CCCCCCCCC
25.65HPRD
Link-
409PhosphotyrosineLGLSYLSSH
CCCCCHHHH
18.69Phosphositeplus
Link-
409Phosphotyrosine; by SRC; in vitro.LGLSYLSSH
CCCCCHHHH
18.69UniProtKB
Link-
465PhosphotyrosineDPATYGQFY
CHHHCCEEE
15.84Phosphositeplus
Link-
465Phosphotyrosine (SRC)DPATYGQFY
CHHHCCEEE
15.84PhosphoELM
Link-
465Phosphotyrosine; by SRC.DPATYGQFY
CHHHCCEEE
15.84UniProtKB
Link-
584Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EVLPKAGAL
EECCCCCCC
56.12Phosphositeplus
Link-
603PhosphotyrosinePSAAYLWVG
CCEEEEEEC
10.79Phosphositeplus
Link-
603Phosphotyrosine; by SRC; in vitro.PSAAYLWVG
CCEEEEEEC
10.79UniProtKB
Link-
651PhosphotyrosineGKAAYRTSP
CCCCCCCCC
21.20Phosphositeplus
Link-
651Phosphotyrosine; by SRC; in vitro.GKAAYRTSP
CCCCCCCCC
21.20UniProtKB
Link-
728Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LTSAKRYIE
HHHHHHHHH
45.56Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TM1L1_HUMANphysical interactionEBI-732070
intact16169070
ACTS_HUMANin vitroHPRD:00674HPRD10583954
ACTG_HUMANin vitroHPRD:00674HPRD7849017
11733011
A4_HUMANin vitro
in vivo
HPRD:00674HPRD10329371
ACTB_HUMANin vivoHPRD:00674HPRD10945978
FINC_HUMANin vivoHPRD:00674HPRD6092370
FHIT_HUMANin vitroHPRD:00674HPRD12833632
TM1L1_HUMANyeast 2-hybridHPRD:00674HPRD16169070
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Disease Reference
Kegg disease
OMIM disease
105120Amyloidosis 5 (AMYL5)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Identification of Tyr438 as the major in vitro c-Src phosphorylationsite in human gelsolin: a mass spectrometric approach.";
De Corte V., Demol H., Goethals M., Van Damme J., Gettemans J.,Vandekerckhove J.;
Protein Sci. 8:234-241(1999).
Cited for: PHOSPHORYLATION AT TYR-86; TYR-409; TYR-465; TYR-603 AND TYR-651.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures