dbPTM

DEMA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DEMA_MOUSE
UniProt AC	Q9WV69
Protein Name	Dematin
Gene Name	Dmtn
Organism	Mus musculus (Mouse).
Sequence Length	405
Subcellular Localization	Cytoplasm. Cytoplasm, cytosol . Cytoplasm, perinuclear region . Cytoplasm, cytoskeleton. Cell membrane. Membrane . Endomembrane system. Cell projection . Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellu
Protein Description	Membrane-cytoskeleton-associated protein with F-actin-binding activity that induces F-actin bundles formation and stabilization. Its F-actin-bundling activity is reversibly regulated upon its phosphorylation by the cAMP-dependent protein kinase A (PKA). Binds to the erythrocyte membrane glucose transporter-1 SLC2A1/GLUT1, and hence stabilizes and attaches the spectrin-actin network to the erythrocytic plasma membrane. Plays a role in maintaining the functional integrity of PKA-activated erythrocyte shape and the membrane mechanical properties. Plays also a role as a modulator of actin dynamics in fibroblasts; acts as negative regulator of the RhoA activation pathway. In platelets, functions as a regulator of internal calcium mobilization across the dense tubular system that affects platelet granule secretion pathways and aggregation. Also required for the formation of a diverse set of cell protrusions, such as filopodia and lamellipodia, necessary for platelet cell spreading, motility and migration. Acts as a tumor suppressor and inhibits malignant cell transformation..
Protein Sequence	MERLQKQPLTSPGSVSSSRDSSVPGSPSSIVAKMDNQVLGYKDLAAIPKDKAILDIERPDLMIYEPHFTYSLLEHVELPRSRECSLSPKSTSPPPSPEVWAESRTLGIISQASTPRTTGTPRTSLPHFHHPETTRPDSNIYKKPPIYKQRESVGGSPQSKHLIEDLIIESSKFPAAQPPDPNQPAKIETDYWPCPPSLAVVETEWRKRKASRKGAEEEEEEEDDDSEEEIKAIRERQKEELSKVTSNLGKMILKEEMEKSLPIRRKTRSLPDRTPFHTSLHSGTSKSSSLPSYGRTTLSRLQSTEFSPSGSEAGSPGLQNGEGQRGRMDRGNSLPCVLEQKIYPYEMLVVTNKGRTKLPPGVDRMRLERHLSAEDFSRVFAMSPEEFGKLALWKRNELKKKASLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	RLQKQPLTSPGSVSS HHHCCCCCCCCCCCC	39.29	25521595
11	Phosphorylation	LQKQPLTSPGSVSSS HHCCCCCCCCCCCCC	34.64	25521595
14	Phosphorylation	QPLTSPGSVSSSRDS CCCCCCCCCCCCCCC	23.39	20415495
16	Phosphorylation	LTSPGSVSSSRDSSV CCCCCCCCCCCCCCC	25.05	20415495
17	Phosphorylation	TSPGSVSSSRDSSVP CCCCCCCCCCCCCCC	27.51	20415495
18	O-linked_Glycosylation	SPGSVSSSRDSSVPG CCCCCCCCCCCCCCC	32.38	62205353
18	Phosphorylation	SPGSVSSSRDSSVPG CCCCCCCCCCCCCCC	32.38	20415495
21	Phosphorylation	SVSSSRDSSVPGSPS CCCCCCCCCCCCCHH	31.93	25521595
22	Phosphorylation	VSSSRDSSVPGSPSS CCCCCCCCCCCCHHH	36.30	25521595
26	Phosphorylation	RDSSVPGSPSSIVAK CCCCCCCCHHHHEEE	18.62	25521595
28	Phosphorylation	SSVPGSPSSIVAKMD CCCCCCHHHHEEEEC	34.10	25521595
29	Phosphorylation	SVPGSPSSIVAKMDN CCCCCHHHHEEEECC	25.19	25521595
71	Phosphorylation	YEPHFTYSLLEHVEL ECCCCCCHHHHHCCC	24.34	21183079
81	Phosphorylation	EHVELPRSRECSLSP HHCCCCCCCCCCCCC	30.41	22817900
85	Phosphorylation	LPRSRECSLSPKSTS CCCCCCCCCCCCCCC	27.42	22324799
87	Phosphorylation	RSRECSLSPKSTSPP CCCCCCCCCCCCCCC	17.62	25521595
90	Phosphorylation	ECSLSPKSTSPPPSP CCCCCCCCCCCCCCH	37.19	25521595
91	Phosphorylation	CSLSPKSTSPPPSPE CCCCCCCCCCCCCHH	51.91	25521595
92	Phosphorylation	SLSPKSTSPPPSPEV CCCCCCCCCCCCHHH	42.36	25521595
96	Phosphorylation	KSTSPPPSPEVWAES CCCCCCCCHHHHHHC	39.19	25521595
103	Phosphorylation	SPEVWAESRTLGIIS CHHHHHHCCEEEEEE	23.87	24925903
110	Phosphorylation	SRTLGIISQASTPRT CCEEEEEECCCCCCC	20.13	22817900
110	O-linked_Glycosylation	SRTLGIISQASTPRT CCEEEEEECCCCCCC	20.13	30059200
113	Phosphorylation	LGIISQASTPRTTGT EEEEECCCCCCCCCC	31.16	21082442
114	Phosphorylation	GIISQASTPRTTGTP EEEECCCCCCCCCCC	21.58	21082442
118	Phosphorylation	QASTPRTTGTPRTSL CCCCCCCCCCCCCCC	40.10	21082442
120	Phosphorylation	STPRTTGTPRTSLPH CCCCCCCCCCCCCCC	13.91	21082442
124	Phosphorylation	TTGTPRTSLPHFHHP CCCCCCCCCCCCCCC	40.98	29899451
133	O-linked_Glycosylation	PHFHHPETTRPDSNI CCCCCCCCCCCCCCC	32.34	30059200
134	O-linked_Glycosylation	HFHHPETTRPDSNIY CCCCCCCCCCCCCCC	38.24	30059200
138	Phosphorylation	PETTRPDSNIYKKPP CCCCCCCCCCCCCCC	28.01	21082442
141	Phosphorylation	TRPDSNIYKKPPIYK CCCCCCCCCCCCCCC	19.74	-
152	Phosphorylation	PIYKQRESVGGSPQS CCCCCCCCCCCCCCH	28.40	25521595
156	Phosphorylation	QRESVGGSPQSKHLI CCCCCCCCCCHHHHH	17.53	25521595
159	Phosphorylation	SVGGSPQSKHLIEDL CCCCCCCHHHHHHHH	25.98	22817900
211	Phosphorylation	EWRKRKASRKGAEEE HHHHHHHHHCCCHHH	37.24	29899451
226	Phosphorylation	EEEEDDDSEEEIKAI HHHCCCCCHHHHHHH	54.63	25521595
242	Phosphorylation	ERQKEELSKVTSNLG HHHHHHHHHHHHHHH	28.49	-
267	Phosphorylation	SLPIRRKTRSLPDRT CCCCCCCCCCCCCCC	24.55	29472430
269	Phosphorylation	PIRRKTRSLPDRTPF CCCCCCCCCCCCCCC	49.86	27742792
272 (in isoform 4)	Phosphorylation	-	72.83	29899451
278	Phosphorylation	PDRTPFHTSLHSGTS CCCCCCCEECCCCCC	33.10	29899451
278 (in isoform 4)	Phosphorylation	-	33.10	21183079
279 (in isoform 4)	Phosphorylation	-	18.60	22807455
279	Phosphorylation	DRTPFHTSLHSGTSK CCCCCCEECCCCCCC	18.60	29899451
282 (in isoform 4)	Phosphorylation	-	49.40	22807455
284 (in isoform 4)	Phosphorylation	-	35.68	22807455
285	O-linked_Glycosylation	TSLHSGTSKSSSLPS EECCCCCCCCCCCCC	33.78	30059200
285	Phosphorylation	TSLHSGTSKSSSLPS EECCCCCCCCCCCCC	33.78	-
286 (in isoform 4)	Phosphorylation	-	54.95	29899451
287	O-linked_Glycosylation	LHSGTSKSSSLPSYG CCCCCCCCCCCCCCC	25.56	162431
287	Phosphorylation	LHSGTSKSSSLPSYG CCCCCCCCCCCCCCC	25.56	24925903
288	Phosphorylation	HSGTSKSSSLPSYGR CCCCCCCCCCCCCCC	39.36	24925903
289	Phosphorylation	SGTSKSSSLPSYGRT CCCCCCCCCCCCCCC	51.93	18388127
290 (in isoform 4)	Phosphorylation	-	3.36	22807455
292	Phosphorylation	SKSSSLPSYGRTTLS CCCCCCCCCCCCCHH	45.58	24925903
293	Phosphorylation	KSSSLPSYGRTTLSR CCCCCCCCCCCCHHH	14.53	24925903
296	Phosphorylation	SLPSYGRTTLSRLQS CCCCCCCCCHHHHHC	27.94	-
297 (in isoform 2)	Phosphorylation	-	22.75	29899451
299	Phosphorylation	SYGRTTLSRLQSTEF CCCCCCHHHHHCCCC	28.93	29899451
303	Phosphorylation	TTLSRLQSTEFSPSG CCHHHHHCCCCCCCC	34.20	15345747
303 (in isoform 2)	Phosphorylation	-	34.20	21183079
304	Phosphorylation	TLSRLQSTEFSPSGS CHHHHHCCCCCCCCC	28.26	25521595
304 (in isoform 2)	Phosphorylation	-	28.26	22807455
307	Phosphorylation	RLQSTEFSPSGSEAG HHHCCCCCCCCCCCC	16.36	19060867
307 (in isoform 2)	Phosphorylation	-	16.36	22807455
309	Phosphorylation	QSTEFSPSGSEAGSP HCCCCCCCCCCCCCC	54.47	25521595
309 (in isoform 2)	Phosphorylation	-	54.47	22807455
311	Phosphorylation	TEFSPSGSEAGSPGL CCCCCCCCCCCCCCC	28.72	21183079
311 (in isoform 2)	Phosphorylation	-	28.72	29899451
315 (in isoform 2)	Phosphorylation	-	23.89	22807455
315	Phosphorylation	PSGSEAGSPGLQNGE CCCCCCCCCCCCCCC	23.89	22817900
333	Phosphorylation	GRMDRGNSLPCVLEQ CCCCCCCCCCEEEEC	36.19	25521595
372	Phosphorylation	MRLERHLSAEDFSRV HHHHHHCCHHHHHHH	24.40	25521595
377	Phosphorylation	HLSAEDFSRVFAMSP HCCHHHHHHHHCCCH	39.60	24925903
381	Phosphorylation	EDFSRVFAMSPEEFG HHHHHHHCCCHHHHH	8.49	-
383	Phosphorylation	FSRVFAMSPEEFGKL HHHHHCCCHHHHHHH	26.23	22324799
403	Phosphorylation	NELKKKASLF----- HHHHHHHHCC-----	38.91	-

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
403	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
403	S	Phosphorylation		-
Phosphorylation at Ser-403 by PKA causes the C-terminal headpiece domain to associate with the N-terminal core domain, and leads to the inhibition of its actin bundling activity (By similarity).

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 DEMA_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of DEMA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-372, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91; SER-289 AND SER-333,AND MASS SPECTROMETRY.	17114649 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-156; SER-226 ANDSER-372, AND MASS SPECTROMETRY.	16452087 [Abstract]
"Proteomic analysis of in vivo phosphorylated synaptic proteins."; Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.; J. Biol. Chem. 280:5972-5982(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-226, AND MASSSPECTROMETRY.	15572359 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114, AND MASSSPECTROMETRY.	17242355 [Abstract]

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