FRIZ4_DROME - dbPTM
FRIZ4_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRIZ4_DROME
UniProt AC Q9NBW1
Protein Name Frizzled-4
Gene Name fz4
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 705
Subcellular Localization 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. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles..
Protein Sequence MKPTCILCLLVVILLHPRISKSSTSGNPSASSSSSSPPEIPAFRQCETIRIEMCRKIGYNETSMPNLVGNEMQTDVEYTLQTFAPLIEYDCSSQLKLFLCAAYVPMCTPKAPVHAIGPCRSLCESVRIRCHPVLQGFGFPWPPALDCDKFPRENNHETMCMEGPGELHQPQQEQDLYGLPGQGIPGGLGGKLPMDCSGLAKSHLYVRLPRSGRCAPLCEADILFTPAEKHLAEIWVSTWAYAALGLALVATVCLLASDGSRLASAKWSRLLSPLIWCHNMVTLGWAVRFMVGRTGTACGTDPQAPNESLLTVDGLSNASCASVFLMRYYFGMAACAWWAVLCLGWHRDIRRHSPDSKGHVVIPSNFGGSPAKRNSAKTAQQDLTQNNFVCFVAWGLPAFQTSAVIVARFVDADELLGACFVGNQSDKALQILVATPVFCYWIFGSMNLISGYLVHCRTKEILRNSNALSVQQQLQQLSAHSSSGIGIFLFIYGLACAMLLLAVIYEFANIDVWLGSGDTNTPLWPFLLRAFMELMLGICCFAWVLGPSISTLYKRQVSNGKMVKHTSAGAATGHLDGHSSSRGSHAACNSTVVSYHSVRTSMASVPLPPSPYKLKTSPGTGSISLNQMSNYSLGRSVHHQQRHSPHHHHHQQQQHHQFHPHHNHQHHSTSSHRLYYPPGSYASQKYSQHGSYYPHLQQYGNETLL
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
60N-linked_GlycosylationMCRKIGYNETSMPNL
HHHHHCCCCCCCCCC
40.64-
306N-linked_GlycosylationGTDPQAPNESLLTVD
CCCCCCCCCCCEEEC
55.28-
317N-linked_GlycosylationLTVDGLSNASCASVF
EEECCCCCHHHHHHH
40.70-
423N-linked_GlycosylationLGACFVGNQSDKALQ
HCCCEECCCCHHHHH
32.64-

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 FRIZ4_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRIZ4_DROME !!

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 FRIZ4_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DSH_DROMEdshphysical
12958364
ARRB_DROMEArr2physical
12958364
WNT8_DROMEwntDphysical
22069480

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FRIZ4_DROME

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Related Literatures of Post-Translational Modification

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