FRIZ2_DROME - dbPTM
FRIZ2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRIZ2_DROME
UniProt AC Q9VVX3
Protein Name Frizzled-2
Gene Name fz2
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 694
Subcellular Localization 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. Required to coordinate the cytoskeletons of epidermal cells to produce a parallel array of cuticular hairs and bristles..
Protein Sequence MRHNRLKVLILGLVLLLTSCRADGPLHSADHGMGGMGMGGHGLDASPAPGYGVPVIPKDPNLRCEEITIPMCRGIGYNMTSFPNEMNHETQDEAGLEVHQFWPLVEIKCSPDLKFFLCSMYTPICLEDYHKPLPVCRSVCERARSGCAPIMQQYSFEWPERMACEHLPLHGDPDNLCMEQPSYTEAGSGGSSGGSGGSGSGSGSGGKRKQGGSGSGGSGAGGSSGSTSTKPCRGRNSKNCQNPQGEKASGKECSCSCRSPLIFLGKEQLLQQQSQMPMMHHPHHWYMNLTVQRIAGVPNCGIPCKGPFFSNDEKDFAGLWIALWSGLCFCSTLMTLTTFIIDTERFKYPERPIVFLSACYFMVAVGYLSRNFLQNEEIACDGLLLRESSTGPHSCTLVFLLTYFFGMASSIWWVILSFTWFLAAGLKWGNEAITKHSQYFHLAAWLIPTVQSVAVLLLSAVDGDPILGICYVGNLNPDHLKTFVLAPLFVYLVIGTTFLMAGFVSLFRIRSVIKQQGGVGAGVKADKLEKLMIRIGIFSVLYTVPATIVIGCYLYEAAYFEDWIKALACPCAQVKGPGKKPLYSVLMLKYFMALAVGITSGVWIWSGKTLESWRRFWRRLLGAPDRTGANQALIKQRPPIPHPYAGSGMGMPVGSAAGSLLATPYTQAGGASVASTSHHHLHHHVLKQPAASHV
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
78N-linked_GlycosylationMCRGIGYNMTSFPNE
ECCCCCCCCCCCCCC
23.26-
288N-linked_GlycosylationHPHHWYMNLTVQRIA
CCCCCEECCCHHHHH
19.50-

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 FRIZ2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRIZ2_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 FRIZ2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WIF1_DROMEshfgenetic
22383891
WNTG_DROMEwggenetic
9671581
WNTG_DROMEwggenetic
9875856
WNTG_DROMEwggenetic
10996794
ITBN_DROMEItgbetanugenetic
23054837
GNAO_DROMEGalphaogenetic
16617104
LAMA_DROMELanAgenetic
23054837
DALY_DROMEdallygenetic
10421372
HID_DROMEWgenetic
16369482
DCO_DROMEdcogenetic
16824922
FRIZ_DROMEfzgenetic
10556068
FRIZ_DROMEfzgenetic
9671581
MARF_DROMEMarfphysical
27451905
DSH_DROMEdshphysical
14636582
WNTG_DROMEwgphysical
22203956
WNTG_DROMEwgphysical
22285813
WNTG_DROMEwgphysical
8717036
IMA_DROMEPenphysical
20601947
FRIZ2_DROMEfz2physical
17960137

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FRIZ2_DROME

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Related Literatures of Post-Translational Modification

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