FZD7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FZD7_HUMAN
• UniProt AC: O75084
• Protein Name: Frizzled-7
• Gene Name: FZD7
• Organism: Homo sapiens (Human).
• Sequence Length: 574
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Endosome membrane ; Multi-pass membrane protein . Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other cond
• 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..
• Protein Sequence: MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV

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
11	Phosphorylation	PGAAAPLSSLGLCAL CCCCCCHHHHHHHHH	23.58	-
27	Phosphorylation	LALLGALSAGAGAQP HHHHHHHHCCCCCCC	24.91	-
35	Phosphorylation	AGAGAQPYHGEKGIS CCCCCCCCCCCCCCC	15.46	-
42	O-linked_Glycosylation	YHGEKGISVPDHGFC CCCCCCCCCCCCCCC	35.94	55824293
42	Phosphorylation	YHGEKGISVPDHGFC CCCCCCCCCCCCCCC	35.94	-
63	N-linked_Glycosylation	LCTDIAYNQTILPNL CCCCCCCCCCCCHHH	24.40	UniProtKB CARBOHYD
137	Ubiquitination	GCEALMNKFGFQWPE HHHHHHHHHCCCCCC	32.66	-
164	N-linked_Glycosylation	GEICVGQNTSDGSGG CEEEEECCCCCCCCC	35.30	UniProtKB CARBOHYD
191	O-linked_Glycosylation	YLPDLPFTALPPGAS CCCCCCCCCCCCCCC	25.91	OGP
331	Phosphorylation	YRTVAQGTKKEGCTI CCCCCCCCCCCCCCH	27.19	29759185
455	Methylation	FRIRTIMKHDGTKTE HHHHHHHCCCCCCHH	34.39	23644510
455	Ubiquitination	FRIRTIMKHDGTKTE HHHHHHHCCCCCCHH	34.39	33845483
567	Phosphorylation	FYHRLSHSSKGETAV HHHHHHCCCCCCCCC	30.30	28348404
568	Phosphorylation	YHRLSHSSKGETAV- HHHHHCCCCCCCCC-	38.98	22617229
569	Ubiquitination	HRLSHSSKGETAV-- HHHHCCCCCCCCC--	64.87	33845483
572	Phosphorylation	SHSSKGETAV----- HCCCCCCCCC-----	41.19	28348404

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of FZD7_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FZD7_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of FZD7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBQL1_HUMAN	UBQLN1	physical	16189514
DLG4_HUMAN	DLG4	physical	12067714
ZNRF3_HUMAN	ZNRF3	physical	28600110
RSPO2_HUMAN	RSPO2	physical	28600110

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• D10410: Vantictumab (USAN)
• DrugBank
• There are no disease associations of PTM sites.