dbPTM

DEST_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DEST_HUMAN
UniProt AC	P60981
Protein Name	Destrin
Gene Name	DSTN
Organism	Homo sapiens (Human).
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	MASGVQVADEVCRIFYDMKVRKCSTPEEIKKRKKAVIFCLSADKKCIIVEEGKEILVGDVGVTITDPFKHFVGMLPEKDCRYALYDASFETKESRKEELMFFLWAPELAPLKSKMIYASSKDAIKKKFQGIKHECQANGPEDLNRACIAEKLGGSLIVAFEGCPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGVQVAD ------CCCCCCHHH	18.26	20068231
3	Phosphorylation	-----MASGVQVADE -----CCCCCCHHHH	37.89	29255136
7 (in isoform 2)	Phosphorylation	-	7.24	20068231
16	Phosphorylation	DEVCRIFYDMKVRKC HHHHHHHHCCCCCCC	16.86	26356563
19	Ubiquitination	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	21890473
19	Acetylation	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	19608861
19	Malonylation	CRIFYDMKVRKCSTP HHHHHCCCCCCCCCH	35.67	26320211
22	Ubiquitination	FYDMKVRKCSTPEEI HHCCCCCCCCCHHHH	35.21	-
24	Phosphorylation	DMKVRKCSTPEEIKK CCCCCCCCCHHHHHH	50.46	23911959
25	Phosphorylation	MKVRKCSTPEEIKKR CCCCCCCCHHHHHHH	44.16	26657352
30	Acetylation	CSTPEEIKKRKKAVI CCCHHHHHHHCCEEE	50.21	25953088
30	Ubiquitination	CSTPEEIKKRKKAVI CCCHHHHHHHCCEEE	50.21	-
34	Acetylation	EEIKKRKKAVIFCLS HHHHHHCCEEEEEEC	52.50	26051181
41	Phosphorylation	KAVIFCLSADKKCII CEEEEEECCCCEEEE	35.29	28348404
44	Malonylation	IFCLSADKKCIIVEE EEEECCCCEEEEEEC	49.62	26320211
44	Ubiquitination	IFCLSADKKCIIVEE EEEECCCCEEEEEEC	49.62	-
44	Acetylation	IFCLSADKKCIIVEE EEEECCCCEEEEEEC	49.62	25953088
45	Ubiquitination	FCLSADKKCIIVEEG EEECCCCEEEEEECC	31.08	-
45	Acetylation	FCLSADKKCIIVEEG EEECCCCEEEEEECC	31.08	27452117
63	Phosphorylation	LVGDVGVTITDPFKH EECCCCEEECCHHHH	16.54	27251275
65	Phosphorylation	GDVGVTITDPFKHFV CCCCEEECCHHHHHH	28.40	27251275
69	Acetylation	VTITDPFKHFVGMLP EEECCHHHHHHCCCC	41.33	20167786
74	Sulfoxidation	PFKHFVGMLPEKDCR HHHHHHCCCCHHCHH	4.79	30846556
75	Ubiquitination	FKHFVGMLPEKDCRY HHHHHCCCCHHCHHH	4.00	21890473
78	Ubiquitination	FVGMLPEKDCRYALY HHCCCCHHCHHHHEE	61.25	-
78	Malonylation	FVGMLPEKDCRYALY HHCCCCHHCHHHHEE	61.25	26320211
78	Acetylation	FVGMLPEKDCRYALY HHCCCCHHCHHHHEE	61.25	23749302
82	Phosphorylation	LPEKDCRYALYDASF CCHHCHHHHEEECCC	13.80	28152594
85	Phosphorylation	KDCRYALYDASFETK HCHHHHEEECCCCCC	10.99	28796482
88	Phosphorylation	RYALYDASFETKESR HHHEEECCCCCCHHH	22.25	25159151
91	Phosphorylation	LYDASFETKESRKEE EEECCCCCCHHHHHH	37.79	26356563
92	Ubiquitination	YDASFETKESRKEEL EECCCCCCHHHHHHH	46.63	21890473
92	Acetylation	YDASFETKESRKEEL EECCCCCCHHHHHHH	46.63	23236377
100	Sulfoxidation	ESRKEELMFFLWAPE HHHHHHHHHHHHCHH	2.24	28183972
112	Ubiquitination	APELAPLKSKMIYAS CHHHHCCCCCHHHHC	47.15	21906983
112	Acetylation	APELAPLKSKMIYAS CHHHHCCCCCHHHHC	47.15	71271
112	Sumoylation	APELAPLKSKMIYAS CHHHHCCCCCHHHHC	47.15	-
113	Phosphorylation	PELAPLKSKMIYASS HHHHCCCCCHHHHCC	34.83	28270605
114	Sumoylation	ELAPLKSKMIYASSK HHHCCCCCHHHHCCH	27.94	-
114	Acetylation	ELAPLKSKMIYASSK HHHCCCCCHHHHCCH	27.94	184757
114	Sumoylation	ELAPLKSKMIYASSK HHHCCCCCHHHHCCH	27.94	-
114	Ubiquitination	ELAPLKSKMIYASSK HHHCCCCCHHHHCCH	27.94	21890473
115	Sulfoxidation	LAPLKSKMIYASSKD HHCCCCCHHHHCCHH	3.50	30846556
117	Phosphorylation	PLKSKMIYASSKDAI CCCCCHHHHCCHHHH	9.27	27273156
119	Phosphorylation	KSKMIYASSKDAIKK CCCHHHHCCHHHHHH	22.43	26356563
120	Phosphorylation	SKMIYASSKDAIKKK CCHHHHCCHHHHHHH	26.78	26356563
121	Sumoylation	KMIYASSKDAIKKKF CHHHHCCHHHHHHHH	49.00	-
121	Sumoylation	KMIYASSKDAIKKKF CHHHHCCHHHHHHHH	49.00	-
121	Acetylation	KMIYASSKDAIKKKF CHHHHCCHHHHHHHH	49.00	8273249
121	Ubiquitination	KMIYASSKDAIKKKF CHHHHCCHHHHHHHH	49.00	-
125	Acetylation	ASSKDAIKKKFQGIK HCCHHHHHHHHHHHC	52.19	8273263
127	Malonylation	SKDAIKKKFQGIKHE CHHHHHHHHHHHCHH	37.61	26320211
127	Acetylation	SKDAIKKKFQGIKHE CHHHHHHHHHHHCHH	37.61	25953088
127	Ubiquitination	SKDAIKKKFQGIKHE CHHHHHHHHHHHCHH	37.61	-
132	Malonylation	KKKFQGIKHECQANG HHHHHHHCHHHHHCC	39.93	26320211
132	Acetylation	KKKFQGIKHECQANG HHHHHHHCHHHHHCC	39.93	21466224
132	Ubiquitination	KKKFQGIKHECQANG HHHHHHHCHHHHHCC	39.93	-
132	Sumoylation	KKKFQGIKHECQANG HHHHHHHCHHHHHCC	39.93	-
132	Sumoylation	KKKFQGIKHECQANG HHHHHHHCHHHHHCC	39.93	-
135	S-nitrosylation	FQGIKHECQANGPED HHHHCHHHHHCCHHH	4.65	22126794
147	S-nitrosylation	PEDLNRACIAEKLGG HHHHHHHHHHHHHCC	2.46	19483679
147	S-nitrosocysteine	PEDLNRACIAEKLGG HHHHHHHHHHHHHCC	2.46	-
155	Phosphorylation	IAEKLGGSLIVAFEG HHHHHCCCEEEEEEC	17.08	23663014

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
3	S	Phosphorylation	Kinase	LIMK1	P53667	PSP
3	S	Phosphorylation	Kinase	LIMK2	P53671	PSP
3	S	Phosphorylation	Kinase	TESK1	Q63572	PSP

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PIEZ1_HUMAN	PIEZO1	physical	22939629
RINI_HUMAN	RNH1	physical	22939629
TERA_HUMAN	VCP	physical	22939629
URM1_HUMAN	URM1	physical	22939629
PTMA_HUMAN	PTMA	physical	22939629
DPP3_HUMAN	DPP3	physical	22939629
IBP7_HUMAN	IGFBP7	physical	22939629
MGDP1_HUMAN	MDP1	physical	22939629
OTUB1_HUMAN	OTUB1	physical	22939629
OCTC_HUMAN	CROT	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
TPM2_HUMAN	TPM2	physical	22939629
PP4R2_HUMAN	PPP4R2	physical	22939629
DNPH1_HUMAN	DNPH1	physical	22939629
SC24A_HUMAN	SEC24A	physical	22939629
MYH11_HUMAN	MYH11	physical	22939629
FCL_HUMAN	TSTA3	physical	22939629
RN114_HUMAN	RNF114	physical	22939629
ITSN1_HUMAN	ITSN1	physical	22939629
STMN2_HUMAN	STMN2	physical	22939629
SRSF2_HUMAN	SRSF2	physical	22939629
MCFD2_HUMAN	MCFD2	physical	22939629
PEX19_HUMAN	PEX19	physical	22939629
HSPB8_HUMAN	HSPB8	physical	22939629
PALLD_HUMAN	PALLD	physical	22939629
LIMD1_HUMAN	LIMD1	physical	22939629
PAXI_HUMAN	PXN	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
STAT6_HUMAN	STAT6	physical	22939629
NMI_HUMAN	NMI	physical	22939629
POMP_HUMAN	POMP	physical	22939629
TM1L2_HUMAN	TOM1L2	physical	22939629
UNK_HUMAN	UNK	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
OTUL_HUMAN	OTULIN	physical	22939629
TTC1_HUMAN	TTC1	physical	22939629
UBA3_HUMAN	UBA3	physical	22939629
DJB12_HUMAN	DNAJB12	physical	22939629
S23IP_HUMAN	SEC23IP	physical	22939629
PSMD9_HUMAN	PSMD9	physical	22939629
SGTA_HUMAN	SGTA	physical	22939629
SP100_HUMAN	SP100	physical	22939629
PDLI5_HUMAN	PDLIM5	physical	22939629
LTOR5_HUMAN	LAMTOR5	physical	22939629
PUM1_HUMAN	PUM1	physical	22939629
MCM7_HUMAN	MCM7	physical	22939629
PTMS_HUMAN	PTMS	physical	22939629
ITB1_HUMAN	ITGB1	physical	22939629
TBA1C_HUMAN	TUBA1C	physical	22939629
ACTS_HUMAN	ACTA1	physical	8399167
GABT_HUMAN	ABAT	physical	26344197
AL4A1_HUMAN	ALDH4A1	physical	26344197
HIBCH_HUMAN	HIBCH	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
LDHA_HUMAN	LDHA	physical	26344197
LDH6A_HUMAN	LDHAL6A	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
MEMO1_HUMAN	MEMO1	physical	26344197
MIF_HUMAN	MIF	physical	26344197
NDKB_HUMAN	NME2	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
SPRE_HUMAN	SPR	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197

Drug and Disease Associations

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

Regulatory Network of DEST_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19413330 [Abstract]
"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.	12665801 [Abstract]
"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.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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.	19369195 [Abstract]
"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.	19413330 [Abstract]
"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.	17081983 [Abstract]