FZD6_HUMAN - dbPTM
FZD6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FZD6_HUMAN
UniProt AC O60353
Protein Name Frizzled-6
Gene Name FZD6
Organism Homo sapiens (Human).
Sequence Length 706
Subcellular Localization Membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein . Cell surface . Apical cell membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane
Multi-pass membrane protein . Colocalizes with FZD3 at the apical
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. Together with FZD3, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear (By similarity)..
Protein Sequence MEMFTFLLTCIFLPLLRGHSLFTCEPITVPRCMKMAYNMTFFPNLMGHYDQSIAAVEMEHFLPLANLECSPNIETFLCKAFVPTCIEQIHVVPPCRKLCEKVYSDCKKLIDTFGIRWPEELECDRLQYCDETVPVTFDPHTEFLGPQKKTEQVQRDIGFWCPRHLKTSGGQGYKFLGIDQCAPPCPNMYFKSDELEFAKSFIGTVSIFCLCATLFTFLTFLIDVRRFRYPERPIIYYSVCYSIVSLMYFIGFLLGDSTACNKADEKLELGDTVVLGSQNKACTVLFMLLYFFTMAGTVWWVILTITWFLAAGRKWSCEAIEQKAVWFHAVAWGTPGFLTVMLLAMNKVEGDNISGVCFVGLYDLDASRYFVLLPLCLCVFVGLSLLLAGIISLNHVRQVIQHDGRNQEKLKKFMIRIGVFSGLYLVPLVTLLGCYVYEQVNRITWEITWVSDHCRQYHIPCPYQAKAKARPELALFMIKYLMTLIVGISAVFWVGSKKTCTEWAGFFKRNRKRDPISESRRVLQESCEFFLKHNSKVKHKKKHYKPSSHKLKVISKSMGTSTGATANHGTSAVAITSHDYLGQETLTEIQTSPETSMREVKADGASTPRLREQDCGEPASPAASISRLSGEQVDGKGQAGSVSESARSEGRISPKSDITDTGLAQSNNLQVPSSSEPSSLKGSTSLLVHPVSGVRKEQGGGCHSDT
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---MEMFTFLLTCIF
---CCHHHHHHHHHH		16.44-
28PhosphorylationLFTCEPITVPRCMKM
CCCCCCCCHHHHHHH		34.8624719451
38N-linked_GlycosylationRCMKMAYNMTFFPNL
HHHHHHHHCCCCHHH		17.30UniProtKB CARBOHYD
108UbiquitinationKVYSDCKKLIDTFGI
HHHHHHHHHHHHHCC		57.94-
136O-linked_GlycosylationCDETVPVTFDPHTEF
CCCCCCCEECCCCCC		19.09OGP
141O-linked_GlycosylationPVTFDPHTEFLGPQK
CCEECCCCCCCCCHH		33.54OGP
148UbiquitinationTEFLGPQKKTEQVQR
CCCCCCHHCCHHHHH		65.87-
150O-linked_GlycosylationFLGPQKKTEQVQRDI
CCCCHHCCHHHHHHH		38.3955831897
166UbiquitinationFWCPRHLKTSGGQGY
CCCCCCCCCCCCCCC		34.22-
191UbiquitinationPCPNMYFKSDELEFA
CCCCCEECHHHHHHH		39.2421906983
352N-linked_GlycosylationMNKVEGDNISGVCFV
HHCCCCCCCCCEEEE		40.98UniProtKB CARBOHYD
496PhosphorylationSAVFWVGSKKTCTEW
HHHEECCCCCCHHHH		22.74-
517PhosphorylationNRKRDPISESRRVLQ
CCCCCCCCHHHHHHH		34.6028348404
519PhosphorylationKRDPISESRRVLQES
CCCCCCHHHHHHHHH		20.7023312004
526PhosphorylationSRRVLQESCEFFLKH
HHHHHHHHHHHHHHC		13.1421712546
532UbiquitinationESCEFFLKHNSKVKH
HHHHHHHHCCHHCCC		35.27-
532MethylationESCEFFLKHNSKVKH
HHHHHHHHCCHHCCC		35.27-
545UbiquitinationKHKKKHYKPSSHKLK
CCCCCCCCCCHHHCE		37.84-
547PhosphorylationKKKHYKPSSHKLKVI
CCCCCCCCHHHCEEE		40.7128152594
548PhosphorylationKKHYKPSSHKLKVIS
CCCCCCCHHHCEEEE		32.9228152594
580PhosphorylationVAITSHDYLGQETLT
EEEECCCCCCCCHHH		13.8127642862
592PhosphorylationTLTEIQTSPETSMRE
HHHHCCCCCCCCCCH		12.3630624053
606PhosphorylationEVKADGASTPRLREQ
HHCCCCCCCCCCCCC		44.4625159151
607PhosphorylationVKADGASTPRLREQD
HCCCCCCCCCCCCCC		16.3425159151
620PhosphorylationQDCGEPASPAASISR
CCCCCCCCCCHHHHH		26.2830266825
624PhosphorylationEPASPAASISRLSGE
CCCCCCHHHHHHCCC		24.1730266825
626PhosphorylationASPAASISRLSGEQV
CCCCHHHHHHCCCCC		25.3630266825
629PhosphorylationAASISRLSGEQVDGK
CHHHHHHCCCCCCCC		38.8929255136
636UbiquitinationSGEQVDGKGQAGSVS
CCCCCCCCCCCCCCC		43.3021906983
641PhosphorylationDGKGQAGSVSESARS
CCCCCCCCCCHHHHH		26.0329255136
643PhosphorylationKGQAGSVSESARSEG
CCCCCCCCHHHHHCC		27.7729255136
645PhosphorylationQAGSVSESARSEGRI
CCCCCCHHHHHCCCC		22.8327794612
648PhosphorylationSVSESARSEGRISPK
CCCHHHHHCCCCCCC		44.0823663014
653PhosphorylationARSEGRISPKSDITD
HHHCCCCCCCCCCCC		25.5528355574
656PhosphorylationEGRISPKSDITDTGL
CCCCCCCCCCCCCCC		37.3130266825
659PhosphorylationISPKSDITDTGLAQS
CCCCCCCCCCCCHHC		32.2823663014
661PhosphorylationPKSDITDTGLAQSNN
CCCCCCCCCCHHCCC		25.9923663014
666PhosphorylationTDTGLAQSNNLQVPS
CCCCCHHCCCCCCCC		23.2923663014
673PhosphorylationSNNLQVPSSSEPSSL
CCCCCCCCCCCCCCC		47.8723090842
674PhosphorylationNNLQVPSSSEPSSLK
CCCCCCCCCCCCCCC		32.4323090842
675PhosphorylationNLQVPSSSEPSSLKG
CCCCCCCCCCCCCCC		58.8423090842
678PhosphorylationVPSSSEPSSLKGSTS
CCCCCCCCCCCCCCE		44.2223090842
679PhosphorylationPSSSEPSSLKGSTSL
CCCCCCCCCCCCCEE		44.8323090842
681UbiquitinationSSEPSSLKGSTSLLV
CCCCCCCCCCCEEEE		53.41-
683PhosphorylationEPSSLKGSTSLLVHP
CCCCCCCCCEEEEEE		17.1529514088
684PhosphorylationPSSLKGSTSLLVHPV
CCCCCCCCEEEEEEC		31.8729514088
685PhosphorylationSSLKGSTSLLVHPVS
CCCCCCCEEEEEECC		22.7729514088
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
648SPhosphorylationKinaseGRK2P25098
PSP
648SPhosphorylationKinaseGRK5P34947
PSP
648SPhosphorylationKinaseCK1EP49674
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FZD6_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 FZD6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SFRP1_HUMANSFRP1physical
10347172
Drug and Disease Associations
Kegg Disease
H01307 Nonsyndromic congenital nail disorder (NDNC)
OMIM Disease
614157Nail disorder, non-syndromic congenital, 10 (NDNC10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FZD6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-606 AND THR-607, ANDMASS SPECTROMETRY.

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