| UniProt ID | FZD4_HUMAN | |
|---|---|---|
| UniProt AC | Q9ULV1 | |
| Protein Name | Frizzled-4 | |
| Gene Name | FZD4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 537 | |
| 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 (CTNNB1) canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin (CTNNB1) and activation of Wnt target genes. Plays a critical role in retinal vascularization by acting as a receptor for Wnt proteins and norrin (NDP). In retina, it can be both activated by Wnt protein-binding, but also by a Wnt-independent signaling via binding of norrin (NDP), promoting in both cases beta-catenin (CTNNB1) accumulation and stimulation of LEF/TCF-mediated transcriptional programs. 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 | MAWRGAGPSVPGAPGGVGLSLGLLLQLLLLLGPARGFGDEEERRCDPIRISMCQNLGYNVTKMPNLVGHELQTDAELQLTTFTPLIQYGCSSQLQFFLCSVYVPMCTEKINIPIGPCGGMCLSVKRRCEPVLKEFGFAWPESLNCSKFPPQNDHNHMCMEGPGDEEVPLPHKTPIQPGEECHSVGTNSDQYIWVKRSLNCVLKCGYDAGLYSRSAKEFTDIWMAVWASLCFISTAFTVLTFLIDSSRFSYPERPIIFLSMCYNIYSIAYIVRLTVGRERISCDFEEAAEPVLIQEGLKNTGCAIIFLLMYFFGMASSIWWVILTLTWFLAAGLKWGHEAIEMHSSYFHIAAWAIPAVKTIVILIMRLVDADELTGLCYVGNQNLDALTGFVVAPLFTYLVIGTLFIAAGLVALFKIRSNLQKDGTKTDKLERLMVKIGVFSVLYTVPATCVIACYFYEISNWALFRYSADDSNMAVEMLKIFMSLLVGITSGMWIWSAKTLHTWQKCSNRLVNSGKVKREKRGNGWVKPGKGSETVV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 59 | N-linked_Glycosylation | MCQNLGYNVTKMPNL HCCCCCCCCCCCCCC | 32.93 | UniProtKB CARBOHYD | |
| 144 | N-linked_Glycosylation | FAWPESLNCSKFPPQ CCCCCCCCCCCCCCC | 36.98 | UniProtKB CARBOHYD | |
| 212 | Phosphorylation | GYDAGLYSRSAKEFT CCCCCCCCCCHHHHH | 25.46 | 24719451 | |
| 422 | Ubiquitination | KIRSNLQKDGTKTDK HHHHHHCCCCCCCHH | 62.38 | 24816145 | |
| 516 | Acetylation | NRLVNSGKVKREKRG HHHHHCCCCCEEECC | 44.39 | 7668849 | |
| 518 | Acetylation | LVNSGKVKREKRGNG HHHCCCCCEEECCCC | 59.32 | 7668859 | |
| 521 | Acetylation | SGKVKREKRGNGWVK CCCCCEEECCCCCCC | 70.42 | 7668869 |
| 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 FZD4_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FZD4_HUMAN !! | ||||||
* 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 FZD4_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| BAG6_HUMAN | BAG6 | physical | 21900206 | |
| ZNRF3_HUMAN | ZNRF3 | physical | 22575959 | |
| NDP_HUMAN | NDP | physical | 15035989 | |
| NDP_HUMAN | NDP | physical | 17955262 | |
| DVL3_MOUSE | Dvl3 | physical | 25198863 | |
| PZRN3_HUMAN | PDZRN3 | physical | 25198863 | |
| RAB5A_HUMAN | RAB5A | physical | 25198863 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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