dbPTM

DEST_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DEST_MOUSE
UniProt AC	Q9R0P5
Protein Name	Destrin
Gene Name	Dstn
Organism	Mus musculus (Mouse).
Sequence Length	165
Subcellular Localization
Protein Description	Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner..
Protein Sequence	MASGVQVADEVCRIFYDMKVRKCSTPEEIKKRKKAVIFCLSADKKCIVVEEGKEILVGDVGATITDPFKHFVGMLPEKDCRYALYDASFETKESRKEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAEKLGGSLIVAFEGSPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGVQVAD ------CCCCCCHHH	18.26	19131326
3	Phosphorylation	-----MASGVQVADE -----CCCCCCHHHH	37.89	26824392
16	Phosphorylation	DEVCRIFYDMKVRKC HHHHHHHHCCCCCCC	16.86	-
19	Acetylation	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	23954790
19	Malonylation	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	26320211
19	Ubiquitination	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	-
19	Succinylation	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	23954790
22	Malonylation	FYDMKVRKCSTPEEI HHCCCCCCCCCHHHH	35.21	26320211
23	S-nitrosocysteine	YDMKVRKCSTPEEIK HCCCCCCCCCHHHHH	3.72	-
23	Glutathionylation	YDMKVRKCSTPEEIK HCCCCCCCCCHHHHH	3.72	24333276
23	S-nitrosylation	YDMKVRKCSTPEEIK HCCCCCCCCCHHHHH	3.72	19101475
24	Phosphorylation	DMKVRKCSTPEEIKK CCCCCCCCCHHHHHH	50.46	26824392
25	Phosphorylation	MKVRKCSTPEEIKKR CCCCCCCCHHHHHHH	44.16	22817900
30	Acetylation	CSTPEEIKKRKKAVI CCCHHHHHHHCCEEE	50.21	22826441
39	S-nitrosylation	RKKAVIFCLSADKKC HCCEEEEEECCCCEE	1.70	20925432
39	S-nitrosocysteine	RKKAVIFCLSADKKC HCCEEEEEECCCCEE	1.70	-
41	Phosphorylation	KAVIFCLSADKKCIV CEEEEEECCCCEEEE	35.29	26824392
44	Acetylation	IFCLSADKKCIVVEE EEEECCCCEEEEEEC	49.62	22826441
44	Ubiquitination	IFCLSADKKCIVVEE EEEECCCCEEEEEEC	49.62	-
45	Malonylation	FCLSADKKCIVVEEG EEECCCCEEEEEECC	29.73	26320211
69	Acetylation	ATITDPFKHFVGMLP CEECCHHHHHHCCCC	41.33	23954790
78	Ubiquitination	FVGMLPEKDCRYALY HHCCCCHHHHHHHEE	61.25	-
78	Acetylation	FVGMLPEKDCRYALY HHCCCCHHHHHHHEE	61.25	22733758
78	Malonylation	FVGMLPEKDCRYALY HHCCCCHHHHHHHEE	61.25	26320211
80	S-nitrosocysteine	GMLPEKDCRYALYDA CCCCHHHHHHHEEEC	5.47	-
80	S-nitrosylation	GMLPEKDCRYALYDA CCCCHHHHHHHEEEC	5.47	21278135
88	Phosphorylation	RYALYDASFETKESR HHHEEECCCCCCHHH	22.25	28066266
91	Phosphorylation	LYDASFETKESRKEE EEECCCCCCHHHHHH	37.79	28066266
92	Acetylation	YDASFETKESRKEEL EECCCCCCHHHHHHH	46.63	23236377
92	Ubiquitination	YDASFETKESRKEEL EECCCCCCHHHHHHH	46.63	-
112	Ubiquitination	APEQAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
114	Ubiquitination	EQAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
117	Phosphorylation	PLKSKMIYASSKDAI CCCCCEEEECCHHHH	9.27	20116462
119	Phosphorylation	KSKMIYASSKDAIKK CCCEEEECCHHHHHH	22.43	22499769
120	Phosphorylation	SKMIYASSKDAIKKK CCEEEECCHHHHHHH	26.78	22499769
121	Acetylation	KMIYASSKDAIKKKF CEEEECCHHHHHHHC	49.00	8273255
121	Ubiquitination	KMIYASSKDAIKKKF CEEEECCHHHHHHHC	49.00	-
127	Acetylation	SKDAIKKKFPGIKHE CHHHHHHHCCCCCCE	52.36	22733758
132	Ubiquitination	KKKFPGIKHEYQANG HHHCCCCCCEECCCC	35.98	-
132	Malonylation	KKKFPGIKHEYQANG HHHCCCCCCEECCCC	35.98	26320211
132	Acetylation	KKKFPGIKHEYQANG HHHCCCCCCEECCCC	35.98	22826441
147	S-nitrosylation	PEDLNRTCIAEKLGG HHHHHHHHHHHHHCC	2.21	21278135
147	S-nitrosocysteine	PEDLNRTCIAEKLGG HHHHHHHHHHHHHCC	2.21	-
163	Phosphorylation	LIVAFEGSPV----- EEEEEECCCC-----	18.45	22324799

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of DEST_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DEST_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DEST_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DEST_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DEST_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.	19367708 [Abstract]