WNT3A_HUMAN - dbPTM
WNT3A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WNT3A_HUMAN
UniProt AC P56704
Protein Name Protein Wnt-3a
Gene Name WNT3A
Organism Homo sapiens (Human).
Sequence Length 352
Subcellular Localization Secreted, extracellular space, extracellular matrix . Secreted .
Protein Description Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. [PubMed: 20093360]
Protein Sequence MAPLGYFLLLCSLKQALGSYPIWWSLAVGPQYSSLGSQPILCASIPGLVPKQLRFCRNYVEIMPSVAEGIKIGIQECQHQFRGRRWNCTTVHDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTAAICGCSSRHQGSPGKGWKWGGCSEDIEFGGMVSREFADARENRPDARSAMNRHNNEAGRQAIASHMHLKCKCHGLSGSCEVKTCWWSQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRPRYTYFKVPTERDLVYYEASPNFCEPNPETGSFGTRDRTCNVSSHGIDGCDLLCCGRGHNARAERRREKCRCVFHWCCYVSCQECTRVYDVHTCK
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
65PhosphorylationNYVEIMPSVAEGIKI
HHHHHCHHHHHHHHC
19.31-
87N-linked_GlycosylationQFRGRRWNCTTVHDS
HHCCCCCCCEEHHHH
16.0821244856
209O-palmitoyl serineKCKCHGLSGSCEVKT
EEEECCCCCCCEEEE
33.00-
209O-palmitoleoylationKCKCHGLSGSCEVKT
EEEECCCCCCCEEEE
33.0024292069
235PhosphorylationGDFLKDKYDSASEMV
HHHHHHHCCCHHHHH
25.8421955146
237PhosphorylationFLKDKYDSASEMVVE
HHHHHCCCHHHHHHH
30.5121955146
239PhosphorylationKDKYDSASEMVVEKH
HHHCCCHHHHHHHHH
30.1221955146
298N-linked_GlycosylationGTRDRTCNVSSHGID
CCCCCCCCCCCCCCC
35.7721244856

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 WNT3A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WNT3A_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 WNT3A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FZD1_HUMANFZD1physical
10557084
KCTD1_HUMANKCTD1genetic
24736394
CALX_HUMANCANXphysical
26186194
GRP78_HUMANHSPA5physical
26186194
WNT3_HUMANWNT3physical
26186194
2AAB_HUMANPPP2R1Bphysical
26186194
2A5D_HUMANPPP2R5Dphysical
26186194
2A5A_HUMANPPP2R5Aphysical
26186194
2A5B_HUMANPPP2R5Bphysical
26186194
2A5E_HUMANPPP2R5Ephysical
26186194
FEM1B_HUMANFEM1Bphysical
26186194
2ABD_HUMANPPP2R2Dphysical
26186194
TRAF2_HUMANTRAF2physical
26186194
WNT3_HUMANWNT3physical
28514442
2A5A_HUMANPPP2R5Aphysical
28514442
2A5B_HUMANPPP2R5Bphysical
28514442
2A5E_HUMANPPP2R5Ephysical
28514442
2A5D_HUMANPPP2R5Dphysical
28514442
2AAB_HUMANPPP2R1Bphysical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
CALX_HUMANCANXphysical
28514442
SDF2L_HUMANSDF2L1physical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
TRAF2_HUMANTRAF2physical
28514442

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 WNT3A_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"WLS-dependent secretion of WNT3A requires Ser209 acylation andvacuolar acidification.";
Coombs G.S., Yu J., Canning C.A., Veltri C.A., Covey T.M.,Cheong J.K., Utomo V., Banerjee N., Zhang Z.H., Jadulco R.C.,Concepcion G.P., Bugni T.S., Harper M.K., Mihalek I., Jones C.M.,Ireland C.M., Virshup D.M.;
J. Cell Sci. 123:3357-3367(2010).
Cited for: PALMITOYLATION AT SER-209 BY PORCN, AND MUTAGENESIS OF SER-209.

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