CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009276
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Destrin 
Protein Synonyms/Alias
 Actin-depolymerizing factor; ADF 
Gene Name
 DSTN 
Gene Synonyms/Alias
 ACTDP; DSN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19CRIFYDMKVRKCSTPacetylation[1]
19CRIFYDMKVRKCSTPubiquitination[2, 3, 4, 5]
30CSTPEEIKKRKKAVIubiquitination[5]
44IFCLSADKKCIIVEEubiquitination[4]
69VTITDPFKHFVGMLPacetylation[6]
78FVGMLPEKDCRYALYubiquitination[4, 7, 8]
92YDASFETKESRKEELubiquitination[2, 3, 4, 5, 7, 8]
112APELAPLKSKMIYASubiquitination[3, 4, 5]
114ELAPLKSKMIYASSKubiquitination[4]
121KMIYASSKDAIKKKFubiquitination[4]
127SKDAIKKKFQGIKHEubiquitination[4]
132KKKFQGIKHECQANGacetylation[9, 10, 11]
132KKKFQGIKHECQANGubiquitination[4, 7, 12]
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] 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]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] 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]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [11] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [12] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH- independent manner. 
Sequence Annotation
 DOMAIN 4 153 ADF-H.
 MOTIF 30 34 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 19 19 N6-acetyllysine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 165 AA 
Protein Sequence
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV 60
GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS 120
KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPV 165 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
 GO:0030864; C:cortical actin cytoskeleton; IEA:Compara.
 GO:0030042; P:actin filament depolymerization; IEA:InterPro.
 GO:0051014; P:actin filament severing; TAS:ProtInc.
 GO:0008154; P:actin polymerization or depolymerization; TAS:ProtInc.
 GO:0006928; P:cellular component movement; IEA:Compara.
 GO:0000910; P:cytokinesis; IEA:Compara.
 GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Compara. 
Interpro
 IPR002108; Actin-bd_cofilin/tropomyosin.
 IPR017904; ADF/Cofilin/Destrin. 
Pfam
 PF00241; Cofilin_ADF 
SMART
 SM00102; ADF 
PROSITE
 PS51263; ADF_H 
PRINTS
 PR00006; COFILIN.