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

UniProtKB / Swiss-Prot ID :  DEST_HUMAN

Gene Name (Synonyms) : 
DSTN, ACTDP, DSN  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH- independent manner. 

Protein Sequence MASGVQVADEVCRIFYDMKVRKCSTPEEIKKRKKAVIFCLSADKKCIIVEEGKEILVGDVGVTITDPFKH...
Predicted Secondary Structure CCCCCEECHHHHHHHHHHHHHHCCCHHHHCCCCCEEEEEECCCCEEEEEEECCEEEECCCCCCCCCCHHH...
Protein Variant
LocationDescription
139G -> E (in a colorectal cancer sample;somatic mutation).
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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
2N-acetylalanine.---MASGVQ
---CCCCCE
18.26UniProtKB
Link-
3Phosphoserine--MASGVQV
--CCCCCEE
37.89HPRD
Link-
3Phosphoserine--MASGVQV
--CCCCCEE
37.89Phosphositeplus
Link-
3Phosphoserine (TESK2)--MASGVQV
--CCCCCEE
37.89HPRD
Link-
3Phosphoserine.--MASGVQV
--CCCCCEE
37.89UniProtKB
Link-
16PhosphotyrosineCRIFYDMKV
HHHHHHHHH
16.86Phosphositeplus
Link-
19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FYDMKVRKC
HHHHHHHHC
35.67Phosphositeplus
Link-
19N6-acetyllysineFYDMKVRKC
HHHHHHHHC
35.67HPRD
Link-
19N6-acetyllysineFYDMKVRKC
HHHHHHHHC
35.67Phosphositeplus
Link-
19N6-acetyllysine.FYDMKVRKC
HHHHHHHHC
35.67UniProtKB
Link-
24PhosphoserineVRKCSTPEE
HHHCCCHHH
50.46HPRD
Link-
69N6-acetyllysineTDPFKHFVG
CCCHHHHHH
41.33Phosphositeplus
Link-
85PhosphotyrosineRYALYDASF
EEEEEEEEE
10.99Phosphositeplus
Link-
92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SFETKESRK
EEECCCCCC
46.63Phosphositeplus
Link-
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LAPLKSKMI
CCCHHHHHH
47.15Phosphositeplus
Link-
114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PLKSKMIYA
CHHHHHHHH
27.94Phosphositeplus
Link-
114N6-acetyllysine.PLKSKMIYA
CHHHHHHHH
27.94UniProtKB
Link-
117PhosphotyrosineSKMIYASSK
HHHHHHHHH
9.27Phosphositeplus
Link-
147S-nitrosocysteineLNRACIAEK
CCHHHHHHH
2.46dbSNO
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SMAD9_HUMANphysical interactionMINT-61935MINT15231748
ACTG_HUMANphysical interactionMINT-67797MINT16189514
ACTB_HUMANphysical interactionEBI-754393
intact16189514
ACTG_HUMANin vitroHPRD:16446HPRD8399167
SHBG_HUMANyeast 2-hybridHPRD:16446HPRD15862967
SMAD9_HUMANyeast 2-hybridHPRD:16446HPRD15231748
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-114, AND MASSSPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures