PTK7_MOUSE - dbPTM
PTK7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTK7_MOUSE
UniProt AC Q8BKG3
Protein Name Inactive tyrosine-protein kinase 7
Gene Name Ptk7
Organism Mus musculus (Mouse).
Sequence Length 1062
Subcellular Localization Membrane
Single-pass type I membrane protein. Cell junction. Colocalizes with MMP14 at cell junctions. Also localizes at the leading edge of migrating cells.
Protein Description Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis..
Protein Sequence MGARPLTLLRALLLPLLAGAQAAIVFIKEPSSQDALQGRRALLRCEVEAPDPVHVYWLLNGVPVQDTERRFAQGSSLSFAAVDRLQDSGAFQCVARDNVTGEEVRSTNASFNIKWIEAGPVVLKHPASEAEIQPQTQVTLRCHIDGHPRPTYQWFRDGTPLSDDQSTHTVSSRERNLTLRPASPEHSGLYSCCAHNAFGQACSSQNFTLSVADESFARVVLAPQDVVVARNEEAMFHCQFSAQPPPSLQWVFEDETPITNRSRPPHLRRAVVFANGSLLLTQVRPRNAGVYRCIGQGQRGPPIVLEATLHLAEIEDMLPFEPRVFIAGDEERVTCPAPQGLPTPSVWWEHAGVPLPAHGRVHQKGLELVFVTIAESDTGVYTCHASNLAGQRRQDVNITVATVPTWLRKPQDSQLEEGKPGYLHCLTQATPKPTVIWYRNQMLISEDSRFEVSKNGTLRINSVEVYDGTLYRCVSSTPAGSIEAQARVQVLEKLKFTPPPQPQQCMEFDKEATVPCSATGREKPTVKWVRADGSSLPEWVTDNAGTLHFARVTRDDAGNYTCIASNEPQGQIRAHVQLTVAVFITFKVEPERTTVYQGHTALLRCEAQGDPKPLIQWKGKDRILDPTKLGPRMHIFQNGSLVIHDVAPEDSGSYTCIAGNSCNIRHTEAPLLVVDKPVMEDSEGPGSPPPYKMIQTIGLSVGAAVAYIIAVLGLMFYCKKRCKAKRLQKQPEGEEPEMECLNGGPLQNGQPSAEIQEEVALTSLGSGPPATNKRHSAGDRMHFPRASLQPITTLGKSEFGEVFLAKAQGVEEGATETLVLVKSLQSRDEQQQLDFRREVEMFGKLNHANVVRLLGLCREAEPHYMVLEYVDLGDLKQFLRISKNKDEKLKSQPLSTKQKVALCSQVALGMEHLSNNRFVHKDLAARNCLISAQRQVKVSALGLSKDVYNSEYYHFRQAWVPLRWMSPEAVLEGDFSTKSDVWAFGVLMWEVFTHGEMPHGGQADDEVLADLQAGKARLPQPEGCPSKLYRLMQRCWAPNPKDRPSFSEIASTLGDSPADSKQ
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
75PhosphorylationERRFAQGSSLSFAAV
CHHHCCCCCCEEEHH		18.9428059163
78PhosphorylationFAQGSSLSFAAVDRL
HCCCCCCEEEHHHHH		18.1328059163
88PhosphorylationAVDRLQDSGAFQCVA
HHHHHHHCCCEEEEE		21.04-
98N-linked_GlycosylationFQCVARDNVTGEEVR
EEEEEECCCCCCCCC		27.9119349973
108N-linked_GlycosylationGEEVRSTNASFNIKW
CCCCCCCCCEEEEEE		34.5319656770
166PhosphorylationTPLSDDQSTHTVSSR
CCCCCCCCCCCCCHH		29.2028973931
176N-linked_GlycosylationTVSSRERNLTLRPAS
CCCHHCCCEEECCCC		32.40-
178PhosphorylationSSRERNLTLRPASPE
CHHCCCEEECCCCHH		25.0324719451
206N-linked_GlycosylationGQACSSQNFTLSVAD
HHHHHCCCCEEEECC		33.54-
260N-linked_GlycosylationEDETPITNRSRPPHL
CCCCCCCCCCCCCCC		40.42-
275N-linked_GlycosylationRRAVVFANGSLLLTQ
CEEEEECCCCEEEEE		29.1719349973
397N-linked_GlycosylationGQRRQDVNITVATVP
CCCCCCCCEEEEECC		32.2919656770
455N-linked_GlycosylationSRFEVSKNGTLRINS
CCEEECCCCEEEECE		40.97-
553PhosphorylationTLHFARVTRDDAGNY
CEEEEEEECCCCCCE		23.8730635358
559N-linked_GlycosylationVTRDDAGNYTCIASN
EECCCCCCEEEEECC		30.5719349973
560PhosphorylationTRDDAGNYTCIASNE
ECCCCCCEEEEECCC		11.3230635358
561PhosphorylationRDDAGNYTCIASNEP
CCCCCCEEEEECCCC		11.0530635358
565PhosphorylationGNYTCIASNEPQGQI
CCEEEEECCCCCCCE		23.0930635358
638N-linked_GlycosylationPRMHIFQNGSLVIHD
CCEEEEECCCEEEEE		31.13-
776PhosphorylationPATNKRHSAGDRMHF
CCCCCCCCCCCCCCC		37.6726824392
891PhosphorylationNKDEKLKSQPLSTKQ
CCCHHHHCCCCCHHH		47.6825338131
921AcetylationSNNRFVHKDLAARNC
HCCCCCCHHHHHHHC		49.4922826441
944PhosphorylationKVSALGLSKDVYNSE
HHHHHCCCCCCCCCC		25.63-
1045PhosphorylationPNPKDRPSFSEIAST
CCCCCCCCHHHHHHH		42.1529514104
1051PhosphorylationPSFSEIASTLGDSPA
CCHHHHHHHHCCCCC		29.8125338131
1052PhosphorylationSFSEIASTLGDSPAD
CHHHHHHHHCCCCCC		26.2425338131
1056PhosphorylationIASTLGDSPADSKQ-
HHHHHCCCCCCCCC-		21.8626824392
1060PhosphorylationLGDSPADSKQ-----
HCCCCCCCCC-----		34.7529514104
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 PTK7_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTK7_MOUSE !!
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 PTK7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PTK7_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTK7_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98; ASN-275; ASN-397 ANDASN-559, AND MASS SPECTROMETRY.
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-108 AND ASN-397, AND MASSSPECTROMETRY.

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