FZD3_HUMAN - dbPTM
FZD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FZD3_HUMAN
UniProt AC Q9NPG1
Protein Name Frizzled-3
Gene Name FZD3
Organism Homo sapiens (Human).
Sequence Length 666
Subcellular Localization Membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein. Cell surface . Apical cell membrane
Multi-pass membrane protein. Colocalizes with FZD6 at the apical face of the cell (By similarity).
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. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, 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. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner (By similarity)..
Protein Sequence MAMTWIVFSLWPLTVFMGHIGGHSLFSCEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLDCSRDFRPFLCALYAPICMEYGRVTLPCRRLCQRAYSECSKLMEMFGVPWPEDMECSRFPDCDEPYPRLVDLNLAGEPTEGAPVAVQRDYGFWCPRELKIDPDLGYSFLHVRDCSPPCPNMYFRREELSFARYFIGLISIICLSATLFTFLTFLIDVTRFRYPERPIIFYAVCYMMVSLIFFIGFLLEDRVACNASIPAQYKASTVTQGSHNKACTMLFMILYFFTMAGSVWWVILTITWFLAAVPKWGSEAIEKKALLFHASAWGIPGTLTIILLAMNKIEGDNISGVCFVGLYDVDALRYFVLAPLCLYVVVGVSLLLAGIISLNRVRIEIPLEKENQDKLVKFMIRIGVFSILYLVPLLVVIGCYFYEQAYRGIWETTWIQERCREYHIPCPYQVTQMSRPDLILFLMKYLMALIVGIPSVFWVGSKKTCFEWASFFHGRRKKEIVNESRQVLQEPDFAQSLLRDPNTPIIRKSRGTSTQGTSTHASSTQLAMVDDQRSKAGSIHSKVSSYHGSLHRSRDGRYTPCSYRGMEERLPHGSMSRLTDHSRHSSSHRLNEQSRHSSIRDLSNNPMTHITHGTSMNRVIEEDGTSA
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
42N-linked_GlycosylationMCQDLPYNTTFMPNL
HCCCCCCCCCCCHHH
30.61UniProtKB CARBOHYD
150O-linked_GlycosylationLNLAGEPTEGAPVAV
ECCCCCCCCCCCEEE
42.63OGP
170UbiquitinationFWCPRELKIDPDLGY
EECCCCEECCCCCCC
40.07-
178PhosphorylationIDPDLGYSFLHVRDC
CCCCCCCCEEEEECC
21.38-
265N-linked_GlycosylationLEDRVACNASIPAQY
HCCHHHCCCCCCCCH
27.30UniProtKB CARBOHYD
275PhosphorylationIPAQYKASTVTQGSH
CCCCHHCCCCCCCCH
21.1822210691
356N-linked_GlycosylationMNKIEGDNISGVCFV
CHHCCCCCCCCEEEE
40.98UniProtKB CARBOHYD
408UbiquitinationRIEIPLEKENQDKLV
EEEEECCCCCHHHHH
70.4233845483
535PhosphorylationQEPDFAQSLLRDPNT
HCCHHHHHHHCCCCC
26.4124719451
542PhosphorylationSLLRDPNTPIIRKSR
HHHCCCCCCEEECCC
22.6621815630
549MethylationTPIIRKSRGTSTQGT
CCEEECCCCCCCCCC
56.28-
551PhosphorylationIIRKSRGTSTQGTST
EEECCCCCCCCCCCC
27.7323312004
552PhosphorylationIRKSRGTSTQGTSTH
EECCCCCCCCCCCCC
22.8923312004
553PhosphorylationRKSRGTSTQGTSTHA
ECCCCCCCCCCCCCC
30.7523312004
556PhosphorylationRGTSTQGTSTHASST
CCCCCCCCCCCCCCC
22.1923312004
557PhosphorylationGTSTQGTSTHASSTQ
CCCCCCCCCCCCCCE
25.6423312004
558PhosphorylationTSTQGTSTHASSTQL
CCCCCCCCCCCCCEE
22.6923312004
561PhosphorylationQGTSTHASSTQLAMV
CCCCCCCCCCEEEEE
26.7223312004
562PhosphorylationGTSTHASSTQLAMVD
CCCCCCCCCEEEEEC
22.4323312004
563PhosphorylationTSTHASSTQLAMVDD
CCCCCCCCEEEEECC
25.7123312004
577PhosphorylationDQRSKAGSIHSKVSS
CCHHHCCCHHHHHHH
23.2224719451
583PhosphorylationGSIHSKVSSYHGSLH
CCHHHHHHHHCCCCC
28.9925159151
584PhosphorylationSIHSKVSSYHGSLHR
CHHHHHHHHCCCCCC
24.9225159151
585PhosphorylationIHSKVSSYHGSLHRS
HHHHHHHHCCCCCCC
11.6025849741
588PhosphorylationKVSSYHGSLHRSRDG
HHHHHCCCCCCCCCC
14.0027251275
597PhosphorylationHRSRDGRYTPCSYRG
CCCCCCCCCCCCCCC
22.1424732914
598PhosphorylationRSRDGRYTPCSYRGM
CCCCCCCCCCCCCCH
19.2324732914
601PhosphorylationDGRYTPCSYRGMEER
CCCCCCCCCCCHHHH
21.0424732914
613PhosphorylationEERLPHGSMSRLTDH
HHHCCCCCHHHHCCC
15.5628857561
647PhosphorylationDLSNNPMTHITHGTS
HHCCCCCCCCCCCCC
16.0422912867
650PhosphorylationNNPMTHITHGTSMNR
CCCCCCCCCCCCCCC
13.4728348404
653PhosphorylationMTHITHGTSMNRVIE
CCCCCCCCCCCCEEC
19.7328348404
654PhosphorylationTHITHGTSMNRVIEE
CCCCCCCCCCCEECC
20.7432142685
664PhosphorylationRVIEEDGTSA-----
CEECCCCCCC-----
33.5328348404
665PhosphorylationVIEEDGTSA------
EECCCCCCC------
37.1933259812

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 FZD3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FZD3_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 FZD3_HUMAN !!

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

Oops, there are no PPI records of FZD3_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FZD3_HUMAN

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Related Literatures of Post-Translational Modification

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