FZD2_HUMAN - dbPTM
FZD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FZD2_HUMAN
UniProt AC Q14332
Protein Name Frizzled-2
Gene Name FZD2
Organism Homo sapiens (Human).
Sequence Length 565
Subcellular Localization Membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein.
Protein Description Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues..
Protein Sequence MRPRSALPRLLLPLLLLPAAGPAQFHGEKGISIPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSICERARQGCEALMNKFGFQWPERLRCEHFPRHGAEQICVGQNHSEDGAPALLTTAPPPGLQPGAGGTPGGPGGGGAPPRYATLEHPFHCPRVLKVPSYLSYKFLGERDCAAPCEPARPDGSMFFSQEETRFARLWILTWSVLCCASTFFTVTTYLVDMQRFRYPERPIIFLSGCYTMVSVAYIAGFVLQERVVCNERFSEDGYRTVVQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQIDGDLLSGVCFVGLNSLDPLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLERLMVRIGVFSVLYTVPATIVIACYFYEQAFREHWERSWVSQHCKSLAIPCPAHYTPRMSPDFTVYMIKYLMTLIVGITSGFWIWSGKTLHSWRKFYTRLTNSRHGETTV
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
5Phosphorylation---MRPRSALPRLLL
---CCCHHHHHHHHH
36.5224719451
32O-linked_GlycosylationFHGEKGISIPDHGFC
HCCCCCCCCCCCCCC
36.4255825697
53N-linked_GlycosylationLCTDIAYNQTIMPNL
EECHHCCCCCCCHHH
24.4029748286
112PhosphorylationQAIPPCRSICERARQ
HHCHHHHHHHHHHHH
38.0028634120
127UbiquitinationGCEALMNKFGFQWPE
HHHHHHHHHCCCCCH
32.66-
154N-linked_GlycosylationEQICVGQNHSEDGAP
CEEECCCCCCCCCCC
34.42UniProtKB CARBOHYD
165O-linked_GlycosylationDGAPALLTTAPPPGL
CCCCCEEECCCCCCC
23.0555827455
166O-linked_GlycosylationGAPALLTTAPPPGLQ
CCCCEEECCCCCCCC
36.8255827461
179O-linked_GlycosylationLQPGAGGTPGGPGGG
CCCCCCCCCCCCCCC
20.1755827467
194O-linked_GlycosylationGAPPRYATLEHPFHC
CCCCCCCCCCCCCCC
24.6055830743
206UbiquitinationFHCPRVLKVPSYLSY
CCCCCCCCCCCCCCC
49.60-
210PhosphorylationRVLKVPSYLSYKFLG
CCCCCCCCCCCEECC
8.1324719451
212PhosphorylationLKVPSYLSYKFLGER
CCCCCCCCCEECCCC
20.3124719451
213PhosphorylationKVPSYLSYKFLGERD
CCCCCCCCEECCCCC
11.8123879269
214UbiquitinationVPSYLSYKFLGERDC
CCCCCCCEECCCCCC
30.6421890473
284PhosphorylationERPIIFLSGCYTMVS
CCCEEEEECCCHHHH
18.9722210691
287PhosphorylationIIFLSGCYTMVSVAY
EEEEECCCHHHHHHH
11.0322210691
288PhosphorylationIFLSGCYTMVSVAYI
EEEECCCHHHHHHHH
18.3822210691
291PhosphorylationSGCYTMVSVAYIAGF
ECCCHHHHHHHHHHH
7.1022210691
446MethylationFRIRTIMKHDGTKTE
HHHHHHHCCCCCCHH
34.39-
446"N6,N6-dimethyllysine"FRIRTIMKHDGTKTE
HHHHHHHCCCCCCHH
34.39-
500UbiquitinationSWVSQHCKSLAIPCP
HHHHHHHHHCCCCCC
46.51-
510PhosphorylationAIPCPAHYTPRMSPD
CCCCCCCCCCCCCCC
22.1227174698
511PhosphorylationIPCPAHYTPRMSPDF
CCCCCCCCCCCCCCH
8.4427174698
515PhosphorylationAHYTPRMSPDFTVYM
CCCCCCCCCCHHHHH
23.6927174698
519PhosphorylationPRMSPDFTVYMIKYL
CCCCCCHHHHHHHHH
20.3627174698
521PhosphorylationMSPDFTVYMIKYLMT
CCCCHHHHHHHHHHH
7.0627174698
534PhosphorylationMTLIVGITSGFWIWS
HHHHHHHHCCCEECC
19.50-
541PhosphorylationTSGFWIWSGKTLHSW
HCCCEECCCCCHHHH
22.68-
547PhosphorylationWSGKTLHSWRKFYTR
CCCCCHHHHHHHHHH
31.5224719451
552PhosphorylationLHSWRKFYTRLTNSR
HHHHHHHHHHHHCCC
8.25-

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 FZD2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FZD2_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 FZD2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WNT3A_HUMANWNT3Aphysical
19910923
WNT5A_HUMANWNT5Aphysical
19910923

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 FZD2_HUMAN

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Related Literatures of Post-Translational Modification

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