DVL1_RAT - dbPTM
DVL1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DVL1_RAT
UniProt AC Q9WVB9
Protein Name Segment polarity protein dishevelled homolog DVL-1
Gene Name Dvl1
Organism Rattus norvegicus (Rat).
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) (By similarity)..
Protein Sequence MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNRDEAARTNGHPRGDRRRELGLPPDSASTVLSSELESSSFIDSDEEDNTSRLSSSTEQSTSSRLIRKHKCRRRKQRLRQTDRASSFSSITDSTMSLNIITVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTIPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAITRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAIVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSMLKHGFLRHTVNKITFSEQCYYVFGDLCSNLASLNLNSGSSGASDQDTLAPLPHPSVPWPLGQGYPYQYPGPPPCFPPAYQDPGFSYGSGSAGSQQSEGSKSSGSTRSSHRTPGREERRATGAGGSGSESDHTVPSGSGSTGWWERPVSQLSRGSSPRSQASAVAPGLPPLHPLTKAYAVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM
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 Orthologous
Protein Cluster
51PhosphorylationAYKFFFKSMDQDFGV
HHHHHHCCCCCCCCE
23.5727097102
177PhosphorylationELGLPPDSASTVLSS
HCCCCCCCHHHHHCH
29.8728551015
179PhosphorylationGLPPDSASTVLSSEL
CCCCCCHHHHHCHHH
24.0128551015
180PhosphorylationLPPDSASTVLSSELE
CCCCCHHHHHCHHHH
25.7828551015
183PhosphorylationDSASTVLSSELESSS
CCHHHHHCHHHHHCC
19.8928551015
184PhosphorylationSASTVLSSELESSSF
CHHHHHCHHHHHCCC
41.8828551015
188PhosphorylationVLSSELESSSFIDSD
HHCHHHHHCCCCCCC
43.8628551015
189PhosphorylationLSSELESSSFIDSDE
HCHHHHHCCCCCCCC
21.6428551015
190PhosphorylationSSELESSSFIDSDEE
CHHHHHCCCCCCCCC
35.1828551015
194PhosphorylationESSSFIDSDEEDNTS
HHCCCCCCCCCCCCC
41.9528551015
200PhosphorylationDSDEEDNTSRLSSST
CCCCCCCCCCCCCCC
27.7828551015
201PhosphorylationSDEEDNTSRLSSSTE
CCCCCCCCCCCCCCC
37.1628551015
377PhosphorylationLTGALPRYGTSPCSS
HHCCCCCCCCCCCCC
23.8625575281
379PhosphorylationGALPRYGTSPCSSAI
CCCCCCCCCCCCCCC
22.1425575281
380PhosphorylationALPRYGTSPCSSAIT
CCCCCCCCCCCCCCE
21.3928689409
383PhosphorylationRYGTSPCSSAITRTS
CCCCCCCCCCCEECC
26.6225575281
384PhosphorylationYGTSPCSSAITRTSS
CCCCCCCCCCEECCC
30.3325575281
387PhosphorylationSPCSSAITRTSSSSL
CCCCCCCEECCCCCC
27.8425575281
389PhosphorylationCSSAITRTSSSSLTS
CCCCCEECCCCCCCC
25.0625575281
390PhosphorylationSSAITRTSSSSLTSS
CCCCEECCCCCCCCC
25.5725575281
391PhosphorylationSAITRTSSSSLTSSV
CCCEECCCCCCCCCC
24.2728689409
392PhosphorylationAITRTSSSSLTSSVP
CCEECCCCCCCCCCC
29.1825575281
393PhosphorylationITRTSSSSLTSSVPG
CEECCCCCCCCCCCC
37.3025575281
395PhosphorylationRTSSSSLTSSVPGAP
ECCCCCCCCCCCCCC
22.3928689409
396PhosphorylationTSSSSLTSSVPGAPQ
CCCCCCCCCCCCCCC
34.3325575281
397PhosphorylationSSSSLTSSVPGAPQL
CCCCCCCCCCCCCCC
27.3925575281
410PhosphorylationQLEEAPLTVKSDMSA
CCCCCCCEECCCHHH
25.4825575281
632PhosphorylationSRGSSPRSQASAVAP
CCCCCCHHHHHHHCC
33.2227097102
635PhosphorylationSSPRSQASAVAPGLP
CCCHHHHHHHCCCCC
18.6827097102
674PhosphorylationAAVPPELTGSRQSFQ
HCCCHHHCCCHHHHH
31.3027097102
676PhosphorylationVPPELTGSRQSFQKA
CCHHHCCCHHHHHHH
23.1627097102
679PhosphorylationELTGSRQSFQKAMGN
HHCCCHHHHHHHHCC
28.6527097102

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 DVL1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DVL1_RAT !!

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 DVL1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AXIN1_RATAxin1physical
11113207

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DVL1_RAT

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Related Literatures of Post-Translational Modification

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