dbPTM

DVL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DVL2_HUMAN
UniProt AC	O14641
Protein Name	Segment polarity protein dishevelled homolog DVL-2
Gene Name	DVL2
Organism	Homo sapiens (Human).
Sequence Length	736
Subcellular Localization	Cell membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm, cytosol . Cytoplasmic vesicle . Nucleus . Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytopl
Protein Description	Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling..
Protein Sequence	MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQAYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVHTDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLPGATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRAHPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQSFHMAMGNPSEFFVDVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGSSTGGG ------CCCCCCCCC	26.95	-
4	Phosphorylation	----MAGSSTGGGGV ----CCCCCCCCCCC	18.39	25849741
5	Phosphorylation	---MAGSSTGGGGVG ---CCCCCCCCCCCC	30.10	23401153
6	Phosphorylation	--MAGSSTGGGGVGE --CCCCCCCCCCCCC	41.36	23401153
14	Phosphorylation	GGGGVGETKVIYHLD CCCCCCCEEEEEECC	25.36	23401153
18	Phosphorylation	VGETKVIYHLDEEET CCCEEEEEECCCCCC	10.18	19920076
27	Phosphorylation	LDEEETPYLVKIPVP CCCCCCCEEEEECCC	31.39	19920076
30	Ubiquitination	EETPYLVKIPVPAER CCCCEEEEECCCHHH	38.40	29967540
37	Methylation	KIPVPAERITLGDFK EECCCHHHEECCCHH	29.33	-
39	Phosphorylation	PVPAERITLGDFKSV CCCHHHEECCCHHHH	30.80	-
41	Ubiquitination	PAERITLGDFKSVLQ CHHHEECCCHHHHHC	29.65	21963094
44	Ubiquitination	RITLGDFKSVLQRPA HEECCCHHHHHCCCC	44.38	29967540
54	Ubiquitination	LQRPAGAKYFFKSMD HCCCCCCHHHHEECC	41.49	-
58	Ubiquitination	AGAKYFFKSMDQDFG CCCHHHHEECCCCCC	34.66	32015554
59	Phosphorylation	GAKYFFKSMDQDFGV CCHHHHEECCCCCCE	23.57	22199227
83	Ubiquitination	ARLPCFNGRVVSWLV CCCCCCCCEEEEEEE	11.96	22505724
93	Ubiquitination	VSWLVSSDNPQPEMA EEEEECCCCCCCCCC	64.42	21963094
125	Phosphorylation	PPLPPERTSGIGDSR CCCCCCCCCCCCCCC	29.64	23312004
126	Phosphorylation	PLPPERTSGIGDSRP CCCCCCCCCCCCCCC	34.33	23312004
131	Phosphorylation	RTSGIGDSRPPSFHP CCCCCCCCCCCCCCC	41.28	23312004
135	Phosphorylation	IGDSRPPSFHPNVSS CCCCCCCCCCCCCCC	38.58	23312004
141	Phosphorylation	PSFHPNVSSSHENLE CCCCCCCCCCCCCCC	32.53	23312004
142	Phosphorylation	SFHPNVSSSHENLEP CCCCCCCCCCCCCCC	31.28	26471730
143	Phosphorylation	FHPNVSSSHENLEPE CCCCCCCCCCCCCCC	27.58	22817900
151	Phosphorylation	HENLEPETETESVVS CCCCCCCCCCCHHHH	59.95	30576142
153	Phosphorylation	NLEPETETESVVSLR CCCCCCCCCHHHHHC	40.77	30576142
155	Phosphorylation	EPETETESVVSLRRE CCCCCCCHHHHHCCC	34.93	23312004
158	Phosphorylation	TETESVVSLRRERPR CCCCHHHHHCCCCCC	17.63	30576142
169	Phosphorylation	ERPRRRDSSEHGAGG CCCCCCCCCCCCCCC	35.50	30576142
170	Phosphorylation	RPRRRDSSEHGAGGH CCCCCCCCCCCCCCC	37.59	30576142
192	Phosphorylation	LERHLAGYESSSTLM HHHHHCCCCCCCCEE	13.66	30576142
194	Phosphorylation	RHLAGYESSSTLMTS HHHCCCCCCCCEECC	22.54	27251275
195	Phosphorylation	HLAGYESSSTLMTSE HHCCCCCCCCEECCC	18.53	22817900
196	Phosphorylation	LAGYESSSTLMTSEL HCCCCCCCCEECCCC	34.54	22817900
197	Phosphorylation	AGYESSSTLMTSELE CCCCCCCCEECCCCC	23.61	30576142
200	Phosphorylation	ESSSTLMTSELESTS CCCCCEECCCCCCCC	23.35	25907765
201	Phosphorylation	SSSTLMTSELESTSL CCCCEECCCCCCCCC	26.64	25907765
205	Phosphorylation	LMTSELESTSLGDSD EECCCCCCCCCCCCC	35.60	30576142
206	Phosphorylation	MTSELESTSLGDSDE ECCCCCCCCCCCCCC	20.70	20068231
207	Phosphorylation	TSELESTSLGDSDEE CCCCCCCCCCCCCCH	39.37	30576142
211	Phosphorylation	ESTSLGDSDEEDTMS CCCCCCCCCCHHHHH	45.16	21248752
216	Phosphorylation	GDSDEEDTMSRFSSS CCCCCHHHHHHHCCH	21.96	30576142
217	Ubiquitination	DSDEEDTMSRFSSST CCCCHHHHHHHCCHH	4.13	22505724
218	Phosphorylation	SDEEDTMSRFSSSTE CCCHHHHHHHCCHHC	32.06	30576142
221	Phosphorylation	EDTMSRFSSSTEQSS HHHHHHHCCHHCHHH	23.44	29255136
222	Phosphorylation	DTMSRFSSSTEQSSA HHHHHHCCHHCHHHH	38.27	29255136
223	Phosphorylation	TMSRFSSSTEQSSAS HHHHHCCHHCHHHHH	34.46	29255136
224	Phosphorylation	MSRFSSSTEQSSASR HHHHCCHHCHHHHHH	39.74	29255136
224	Ubiquitination	MSRFSSSTEQSSASR HHHHCCHHCHHHHHH	39.74	21890473
227	Phosphorylation	FSSSTEQSSASRLLK HCCHHCHHHHHHHHH	22.95	29255136
228	Phosphorylation	SSSTEQSSASRLLKR CCHHCHHHHHHHHHH	29.92	29255136
230	Phosphorylation	STEQSSASRLLKRHR HHCHHHHHHHHHHHH	25.96	29255136
231	Methylation	TEQSSASRLLKRHRR HCHHHHHHHHHHHHH	43.70	-
250	Phosphorylation	RPPRLERTSSFSSVT CCCCCCCCCCCCCCC	21.24	27251275
251	Phosphorylation	PPRLERTSSFSSVTD CCCCCCCCCCCCCCC	35.29	24719451
252	Phosphorylation	PRLERTSSFSSVTDS CCCCCCCCCCCCCCC	28.65	27251275
254	Phosphorylation	LERTSSFSSVTDSTM CCCCCCCCCCCCCCC	26.33	27251275
255	Phosphorylation	ERTSSFSSVTDSTMS CCCCCCCCCCCCCCE	27.33	27251275
257	Phosphorylation	TSSFSSVTDSTMSLN CCCCCCCCCCCCEEE	26.61	-
275	Phosphorylation	VTLNMEKYNFLGISI EEECCHHCCEEEEEE	9.61	19920076
281	Phosphorylation	KYNFLGISIVGQSNE HCCEEEEEEEECCCC	14.93	19690332
286	Phosphorylation	GISIVGQSNERGDGG EEEEEECCCCCCCCC	34.43	-
289	Asymmetric dimethylarginine	IVGQSNERGDGGIYI EEECCCCCCCCCEEE	53.40	-
295	Phosphorylation	ERGDGGIYIGSIMKG CCCCCCEEEECEEEC	11.51	19920076
297	Ubiquitination	GDGGIYIGSIMKGGA CCCCEEEECEEECCE	8.31	21963094
298	Phosphorylation	DGGIYIGSIMKGGAV CCCEEEECEEECCEE	15.22	-
301	Ubiquitination	IYIGSIMKGGAVAAD EEEECEEECCEEEEC	53.15	21906983
339	Ubiquitination	DAVRVLRDIVHKPGP HHHHHHHHHHCCCCC	43.00	22505724
343	Ubiquitination	VLRDIVHKPGPIVLT HHHHHHCCCCCEEEE	40.55	33845483
349	Ubiquitination	HKPGPIVLTVAKCWD CCCCCEEEEEEECCC	3.10	21963094
353	Ubiquitination	PIVLTVAKCWDPSPQ CEEEEEEECCCCCCC	31.36	21963094
358	Phosphorylation	VAKCWDPSPQAYFTL EEECCCCCCCCEEEC	27.46	21945579
362	Phosphorylation	WDPSPQAYFTLPRNE CCCCCCCEEECCCCC	7.58	21945579
364	Phosphorylation	PSPQAYFTLPRNEPI CCCCCEEECCCCCCC	24.15	21945579
396	Phosphorylation	TFPAYPGSSSMSTIT CCCCCCCCCCCCEEC	18.09	28348404
397	Phosphorylation	FPAYPGSSSMSTITS CCCCCCCCCCCEECC	35.66	28348404
398	Phosphorylation	PAYPGSSSMSTITSG CCCCCCCCCCEECCC	20.60	28348404
400	Phosphorylation	YPGSSSMSTITSGSS CCCCCCCCEECCCCC	20.71	28348404
401	Phosphorylation	PGSSSMSTITSGSSL CCCCCCCEECCCCCC	21.45	28348404
403	Phosphorylation	SSSMSTITSGSSLPD CCCCCEECCCCCCCC	27.42	28348404
404	Phosphorylation	SSMSTITSGSSLPDG CCCCEECCCCCCCCC	32.59	28348404
406	Phosphorylation	MSTITSGSSLPDGCE CCEECCCCCCCCCCC	28.59	28348404
407	Phosphorylation	STITSGSSLPDGCEG CEECCCCCCCCCCCC	47.66	28348404
418	Phosphorylation	GCEGRGLSVHTDMAS CCCCCCCEEECCHHH	18.06	20873877
421	Phosphorylation	GRGLSVHTDMASVTK CCCCEEECCHHHHHH	25.89	28348404
423	Sulfoxidation	GLSVHTDMASVTKAM CCEEECCHHHHHHHH	2.92	30846556
425	Phosphorylation	SVHTDMASVTKAMAA EEECCHHHHHHHHHC	24.55	24247654
427	Phosphorylation	HTDMASVTKAMAAPE ECCHHHHHHHHHCCC	15.58	27251275
428	Ubiquitination	TDMASVTKAMAAPES CCHHHHHHHHHCCCC	33.73	32015554
430	Sulfoxidation	MASVTKAMAAPESGL HHHHHHHHHCCCCCC	3.30	21406390
463	Phosphorylation	SDVVDWLYHHVEGFP HHHHHHHHHHHCCCH	5.89	19920076
473	Ubiquitination	VEGFPERREARKYAS HCCCHHHHHHHHHHH	40.02	22505724
477	Ubiquitination	PERREARKYASGLLK HHHHHHHHHHHHHHH	52.82	22505724
478	Phosphorylation	ERREARKYASGLLKA HHHHHHHHHHHHHHH	10.63	21712546
480	Phosphorylation	REARKYASGLLKAGL HHHHHHHHHHHHHHH	27.21	22468782
480	Ubiquitination	REARKYASGLLKAGL HHHHHHHHHHHHHHH	27.21	21890473
484	Ubiquitination	KYASGLLKAGLIRHT HHHHHHHHHHHHHHH	45.51	27667366
491	Phosphorylation	KAGLIRHTVNKITFS HHHHHHHHCCCCCCC	18.87	22468782
496	Phosphorylation	RHTVNKITFSEQCYY HHHCCCCCCCHHEEE	23.79	22468782
580	Phosphorylation	SYTYGGGSASSQHSE CCCCCCCCCCCCCCC	28.40	-
582	Phosphorylation	TYGGGSASSQHSEGS CCCCCCCCCCCCCCC	32.03	-
583	Phosphorylation	YGGGSASSQHSEGSR CCCCCCCCCCCCCCC	31.46	-
586	Phosphorylation	GSASSQHSEGSRSSG CCCCCCCCCCCCCCC	35.70	-
589	Phosphorylation	SSQHSEGSRSSGSTR CCCCCCCCCCCCCCC	25.57	-
591	Phosphorylation	QHSEGSRSSGSTRSD CCCCCCCCCCCCCCC	40.52	-
592	Phosphorylation	HSEGSRSSGSTRSDG CCCCCCCCCCCCCCC	35.34	-
594	Phosphorylation	EGSRSSGSTRSDGGA CCCCCCCCCCCCCCC	23.69	-
595	Phosphorylation	GSRSSGSTRSDGGAG CCCCCCCCCCCCCCC	37.40	-
597	Phosphorylation	RSSGSTRSDGGAGRT CCCCCCCCCCCCCCC	40.47	-
604	Phosphorylation	SDGGAGRTGRPEERA CCCCCCCCCCCHHCC	36.30	25278378
614	Phosphorylation	PEERAPESKSGSGSE CHHCCCCCCCCCCCC	30.94	20363803
615	Ubiquitination	EERAPESKSGSGSES HHCCCCCCCCCCCCC	58.11	32142685
616	Phosphorylation	ERAPESKSGSGSESE HCCCCCCCCCCCCCC	47.69	20363803
618	Phosphorylation	APESKSGSGSESEPS CCCCCCCCCCCCCCC	46.35	30576142
620	Phosphorylation	ESKSGSGSESEPSSR CCCCCCCCCCCCCCC	39.38	20363803
622	Phosphorylation	KSGSGSESEPSSRGG CCCCCCCCCCCCCCC	57.41	23090842
625	Phosphorylation	SGSESEPSSRGGSLR CCCCCCCCCCCCCCC	28.72	23090842
626	Phosphorylation	GSESEPSSRGGSLRR CCCCCCCCCCCCCCC	45.73	23090842
627	Methylation	SESEPSSRGGSLRRG CCCCCCCCCCCCCCC	58.80	-
630	Phosphorylation	EPSSRGGSLRRGGEA CCCCCCCCCCCCCCC	22.87	23090842
632	Symmetric dimethylarginine	SSRGGSLRRGGEASG CCCCCCCCCCCCCCC	36.57	-
633	Methylation	SRGGSLRRGGEASGT CCCCCCCCCCCCCCC	63.86	-
638	Phosphorylation	LRRGGEASGTSDGGP CCCCCCCCCCCCCCC	38.00	26471730
640	Phosphorylation	RGGEASGTSDGGPPP CCCCCCCCCCCCCCC	22.58	20068231
641	Phosphorylation	GGEASGTSDGGPPPS CCCCCCCCCCCCCCC	37.47	20068231
648	Phosphorylation	SDGGPPPSRGSTGGA CCCCCCCCCCCCCCC	55.86	28555341
649	Methylation	DGGPPPSRGSTGGAP CCCCCCCCCCCCCCC	49.18	-
651	Phosphorylation	GPPPSRGSTGGAPNL CCCCCCCCCCCCCCC	23.83	23312004
652	Phosphorylation	PPPSRGSTGGAPNLR CCCCCCCCCCCCCCC	42.32	23312004
659	Methylation	TGGAPNLRAHPGLHP CCCCCCCCCCCCCCC	37.17	-
709	Phosphorylation	PPVRDLGSVPPELTA CCCCCCCCCCHHHHC	38.45	20873877
715	Phosphorylation	GSVPPELTASRQSFH CCCCHHHHCCHHHHH	22.41	21406692
717	Phosphorylation	VPPELTASRQSFHMA CCHHHHCCHHHHHHH	26.14	21406692
718	Methylation	PPELTASRQSFHMAM CHHHHCCHHHHHHHC	33.43	-
720	Phosphorylation	ELTASRQSFHMAMGN HHHCCHHHHHHHCCC	18.93	21406692
729	Phosphorylation	HMAMGNPSEFFVDVM HHHCCCHHHCCEECC	51.54	21406692

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
18	Y	Phosphorylation	Kinase	SRC	P12931	PSP
27	Y	Phosphorylation	Kinase	SRC	P12931	PSP
143	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS
143	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
206	T	Phosphorylation	Kinase	PLK1	P53350	PSP
224	T	Phosphorylation	Kinase	CSNK1D	P48730	GPS
224	T	Phosphorylation	Kinase	CSNK1E	P49674	GPS
275	Y	Phosphorylation	Kinase	SRC	P12931	PSP
295	Y	Phosphorylation	Kinase	SRC	P12931	PSP
463	Y	Phosphorylation	Kinase	SRC	P12931	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	VHL	P40337	PMID:20639871
-	K	Ubiquitination	E3 ubiquitin ligase	NHLRC1	Q6VVB1	PMID:22223637
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:22826439
-	K	Ubiquitination	E3 ubiquitin ligase	RNF185	Q96GF1	PMID:24727453
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:31867777
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:31867777

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DVL2_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 DVL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PHS_HUMAN	PCBD1	physical	16189514
UBP5_HUMAN	USP5	physical	16189514
POLI_HUMAN	POLI	physical	16189514
CCD33_HUMAN	CCDC33	physical	16189514
DPPA2_HUMAN	DPPA2	physical	16189514
MCRS1_HUMAN	MCRS1	physical	16189514
ARG39_HUMAN	ARHGEF39	physical	16189514
U2AF2_HUMAN	U2AF2	physical	16189514
TIFA_HUMAN	TIFA	physical	16189514
ELOA2_HUMAN	TCEB3B	physical	16189514
DDI1_HUMAN	DDI1	physical	16189514
RNPS1_HUMAN	RNPS1	physical	16189514
CPSF7_HUMAN	CPSF7	physical	16189514
SNF8_HUMAN	SNF8	physical	16189514
SNIP1_HUMAN	SNIP1	physical	16189514
PRPF3_HUMAN	PRPF3	physical	16189514
BAHD1_HUMAN	BAHD1	physical	16189514
P53_HUMAN	TP53	physical	16189514
BAG3_HUMAN	BAG3	physical	16189514
TRAF2_HUMAN	TRAF2	physical	16189514
ZN263_HUMAN	ZNF263	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
ENKD1_HUMAN	ENKD1	physical	16189514
OTUL_HUMAN	OTULIN	physical	16189514
AP1M1_HUMAN	AP1M1	physical	16189514
VINEX_HUMAN	SORBS3	physical	16189514
RHXF2_HUMAN	RHOXF2	physical	16189514
ZN250_HUMAN	ZNF250	physical	16189514
ZN165_HUMAN	ZNF165	physical	16189514
DVL2_HUMAN	DVL2	physical	16189514
THAP1_HUMAN	THAP1	physical	16189514
ZBT8A_HUMAN	ZBTB8A	physical	16189514
DAB2_HUMAN	DAB2	physical	12805222
CSK21_HUMAN	CSNK2A1	physical	10806215
CTNB1_HUMAN	CTNNB1	physical	10806215
SIR1_HUMAN	SIRT1	physical	20439735
NHLC1_HUMAN	NHLRC1	physical	22223637
ITCH_HUMAN	ITCH	physical	22826439
LRRK2_HUMAN	LRRK2	physical	19625296
OTUL_HUMAN	OTULIN	physical	23708998
PG12A_HUMAN	PLA2G12A	physical	21988832
SQSTM_HUMAN	SQSTM1	physical	21691068
SYTC_HUMAN	TARS	physical	22863883
IRS1_HUMAN	IRS1	physical	24616100
IRS2_HUMAN	IRS2	physical	24616100
SQSTM_HUMAN	SQSTM1	physical	24616100
RN185_HUMAN	RNF185	physical	24727453
DVL3_HUMAN	DVL3	physical	24643799
WWTR1_HUMAN	WWTR1	physical	20412773
RUSC1_HUMAN	RUSC1	physical	21516116
TZAP_HUMAN	ZBTB48	physical	21516116
ARRC_HUMAN	ARR3	physical	21516116
UIMC1_HUMAN	UIMC1	physical	21516116
MGN2_HUMAN	MAGOHB	physical	21516116
AAPK1_HUMAN	PRKAA1	physical	21516116
TPM3_HUMAN	TPM3	physical	21516116
WASP_HUMAN	WAS	physical	21516116
YES_HUMAN	YES1	physical	21516116
NOL12_HUMAN	NOL12	physical	21516116
ZGPAT_HUMAN	ZGPAT	physical	21516116
BAG3_HUMAN	BAG3	physical	21516116
C1QBP_HUMAN	C1QBP	physical	26496610
GRP78_HUMAN	HSPA5	physical	26496610
BACD2_HUMAN	TNFAIP1	physical	26496610
COBL1_HUMAN	COBLL1	physical	26496610
RB6I2_HUMAN	ERC1	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610
AR6P4_HUMAN	ARL6IP4	physical	26496610
DDX41_HUMAN	DDX41	physical	26496610
NBAS_HUMAN	NBAS	physical	26496610
CWC25_HUMAN	CWC25	physical	26496610
IMUP_HUMAN	C19orf33	physical	26496610
PHLB2_HUMAN	PHLDB2	physical	26496610
C19L2_HUMAN	CWF19L2	physical	26496610
ZBT17_HUMAN	ZBTB17	physical	25558878
DACT1_HUMAN	DACT1	physical	25558878
FZD5_HUMAN	FZD5	physical	25825523
RNF43_HUMAN	RNF43	physical	25825523
VHL_HUMAN	VHL	physical	25825496
BAKOR_HUMAN	ATG14	physical	25825496
PI3R4_HUMAN	PIK3R4	physical	25825496
A16L1_HUMAN	ATG16L1	physical	25825496
WWP1_HUMAN	WWP1	physical	26701932
WWP2_HUMAN	WWP2	physical	26701932
ITCH_HUMAN	ITCH	physical	26701932
EPN1_HUMAN	EPN1	physical	25871009
CUL3_HUMAN	CUL3	physical	27477274

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 DVL2_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, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND TYR-275, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASSSPECTROMETRY.	18669648 [Abstract]