DVL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DVL1_MOUSE
• UniProt AC: P51141
• Protein Name: Segment polarity protein dishevelled homolog DVL-1
• Gene Name: Dvl1
• Organism: Mus musculus (Mouse).
• Sequence Length: 695
• Subcellular Localization: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm, cytosol . Cytoplasmic vesicle . Localizes at the cell membrane upon interaction with frizzled family members.
• Protein Description: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ)..
• Protein Sequence: MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNRDEAARTNGHPRGDRRRDLGLPPDSASTVLSSELESSSFIDSDEEDNTSRLSSSTEQSTSSRLVRKHKCRRRKQRLRQTDRASSFSSITDSTMSLNIITVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTIPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAITRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAIVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSMLKHGFLRHTVNKITFSEQCYYVFGDLCSNLASLNLNSGSSGASDQDTLAPLPHPSVPWPLGQGYPYQYPGPPPCFPPAYQDPGFSCGSGSAGSQQSEGSKSSGSTRSSHRTPGREERRATGAGGSGSESDHTVPSGSGSTGWWERPVSQLSRGSSPRSQASAVAPGLPPLHPLTKAYAVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	ADFKNVLSNRPVHAY HHHHHHHHCCCCHHH	26.89	28059163
45	Phosphorylation	SNRPVHAYKFFFKSM HCCCCHHHHHHHCCC	8.08	28059163
51	Phosphorylation	AYKFFFKSMDQDFGV HHHHHHCCCCCCCCE	23.57	26643407
89	Phosphorylation	VLAEGAHSDAGSQGT EEECCCCCCCCCCCC	28.73	-
115	Phosphorylation	RTGGIGDSRPPSFHP CCCCCCCCCCCCCCC	41.28	29514104
119	Phosphorylation	IGDSRPPSFHPNVAS CCCCCCCCCCCCCCC	38.58	29514104
139	Phosphorylation	DNETGTESMVSHRRE CCCCCCHHHHHHHHH	25.07	22817900
142	Phosphorylation	TGTESMVSHRRERAR CCCHHHHHHHHHHHH	11.57	22817900
153	Dimethylation	ERARRRNRDEAARTN HHHHHHCHHHHHHHC	41.14	-
158	Dimethylation	RNRDEAARTNGHPRG HCHHHHHHHCCCCCC	35.45	-
184	Phosphorylation	SASTVLSSELESSSF CHHHHHCHHHHHCCC	41.88	25195567
190	Phosphorylation	SSELESSSFIDSDEE CHHHHHCCCCCCCCC	35.18	25293948
194	Phosphorylation	ESSSFIDSDEEDNTS HHCCCCCCCCCCCCC	41.95	21743459
200	Phosphorylation	DSDEEDNTSRLSSST CCCCCCCCCCCCCCC	27.78	25293948
201	Phosphorylation	SDEEDNTSRLSSSTE CCCCCCCCCCCCCCC	37.16	25293948
244	Phosphorylation	FSSITDSTMSLNIIT CCHHCCCCCEEEEEE	17.37	-
346	Phosphorylation	WDPTPRSYFTIPRAD CCCCCCCCEEECCCC	13.16	29514104
377	Phosphorylation	LTGALPRYGTSPCSS HHCCCCCCCCCCCCC	23.86	28066266
379	Phosphorylation	GALPRYGTSPCSSAI CCCCCCCCCCCCCCC	22.14	28066266
380	Phosphorylation	ALPRYGTSPCSSAIT CCCCCCCCCCCCCCE	21.39	23684622
383	Phosphorylation	RYGTSPCSSAITRTS CCCCCCCCCCCEECC	26.62	28066266
383	O-linked_Glycosylation	RYGTSPCSSAITRTS CCCCCCCCCCCEECC	26.62	22517741
384	Phosphorylation	YGTSPCSSAITRTSS CCCCCCCCCCEECCC	30.33	28066266
387	Phosphorylation	SPCSSAITRTSSSSL CCCCCCCEECCCCCC	27.84	28066266
389	Phosphorylation	CSSAITRTSSSSLTS CCCCCEECCCCCCCC	25.06	25338131
396	Phosphorylation	TSSSSLTSSVPGAPQ CCCCCCCCCCCCCCC	34.33	25521595
416	Phosphorylation	LTVKSDMSAIVRVMQ CEECCCHHHHHHHCC	21.60	-
559	Phosphorylation	AYQDPGFSCGSGSAG HHCCCCCCCCCCCCC	24.39	22817900
562	Phosphorylation	DPGFSCGSGSAGSQQ CCCCCCCCCCCCCCC	33.62	22817900
573	Phosphorylation	GSQQSEGSKSSGSTR CCCCCCCCCCCCCCC	25.88	22817900
594	Phosphorylation	GREERRATGAGGSGS CHHHCCCCCCCCCCC	26.25	-
599	Phosphorylation	RATGAGGSGSESDHT CCCCCCCCCCCCCCC	37.92	25338131
601	Phosphorylation	TGAGGSGSESDHTVP CCCCCCCCCCCCCCC	35.31	25338131
632	Phosphorylation	SRGSSPRSQASAVAP CCCCCCHHHHHHHCC	33.22	27180971
635	Phosphorylation	SSPRSQASAVAPGLP CCCHHHHHHHCCCCC	18.68	26370283
651	Phosphorylation	LHPLTKAYAVVGGPP CCCCCCEEEECCCCC	11.07	29514104
674	Phosphorylation	AAVPPELTGSRQSFQ HCCCHHHCCCHHHHH	31.30	30352176
676	Phosphorylation	VPPELTGSRQSFQKA CCHHHCCCHHHHHHH	23.16	25521595
679	Phosphorylation	ELTGSRQSFQKAMGN HHCCCHHHHHHHHCC	28.65	25521595

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
139	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
142	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DVL1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DVL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MUSK_MOUSE	Musk	physical	12165471
RYK_MOUSE	Ryk	genetic	15454084
KC1E_MOUSE	Csnk1e	genetic	14966280
DVL2_MOUSE	Dvl2	genetic	16571627
CSK2A_DROME	CkIIalpha	physical	10409711
DVL2_MOUSE	Dvl2	genetic	16116426
DVL2_MOUSE	Dvl2	genetic	19008950
DVL3_MOUSE	Dvl3	genetic	19008950
PRIC1_MOUSE	Prickle1	physical	19788910
PRIC2_MOUSE	Prickle2	physical	19788910
BRD7_HUMAN	BRD7	physical	12941796
VANG2_HUMAN	VANGL2	physical	28481871

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-559, AND MASSSPECTROMETRY.
PubMed: 19367708