CAD15_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAD15_MOUSE
• UniProt AC: P33146
• Protein Name: Cadherin-15
• Gene Name: Cdh15
• Organism: Mus musculus (Mouse).
• Sequence Length: 784
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein.
• Protein Description: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation..
• Protein Sequence: MGSALLLALGLLAQSLGLSWAVPEPKPSTLYPWRRASAPGRVRRAWVIPPISVSENHKRLPYPLVQIKSDKQQLGSVIYSIQGPGVDEEPRNVFSIDKFTGRVYLNATLDREKTDRFRLRAFALDLGGSTLEDPTDLEIVVVDQNDNRPAFLQDVFRGRILEGAIPGTFVTRAEATDADDPETDNAALRFSILEQGSPEFFSIDEHTGEIRTVQVGLDREVVAVYNLTLQVADMSGDGLTATASAIISIDDINDNAPEFTKDEFFMEAAEAVSGVDVGRLEVEDKDLPGSPNWVARFTILEGDPDGQFKIYTDPKTNEGVLSVVKPLDYESREQYELRVSVQNEAPLQAAAPRARRGQTRVSVWVQDTNEAPVFPENPLRTSIAEGAPPGTSVATFSARDPDTEQLQRISYSKDYDPEDWLQVDGATGRIQTQRVLSPASPFLKDGWYRAIILALDNAIPPSTATGTLSIEILEVNDHAPALALPPSGSLCSEPDQGPGLLLGATDEDLPPHGAPFHFQLNPRVPDLGRNWSVSQINVSHARLRLRHQVSEGLHRLSLLLQDSGEPPQQREQTLNVTVCRCGSDGTCLPGAAALRGGGVGVSLGALVIVLASTVVLLVLILLAALRTRFRGHSRGKSLLHGLQEDLRDNILNYDEQGGGEEDQDAYDINQLRHPVEPRATSRSLGRPPLRRDAPFSYVPQPHRVLPTSPSDIANFISDGLEAADSDPSVPPYDTALIYDYEGDGSVAGTLSSILSSLGDEDQDYDYLRDWGPRFARLADMYGHQ

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
106	N-linked_Glycosylation	FTGRVYLNATLDREK CCCEEEEEEEECHHH	17.12	19656770
202	Phosphorylation	QGSPEFFSIDEHTGE CCCCCCEEEECCCCC	34.16	25338131
226	N-linked_Glycosylation	REVVAVYNLTLQVAD CHHEEEEEEEEEEEC	21.68	-
290	Phosphorylation	EDKDLPGSPNWVARF CCCCCCCCCCEEEEE	17.08	26026062
329	Phosphorylation	SVVKPLDYESREQYE EEEEECCCCCCCEEE	24.40	21454597
331	Phosphorylation	VKPLDYESREQYELR EEECCCCCCCEEEEE	34.58	21454597
530	N-linked_Glycosylation	RVPDLGRNWSVSQIN CCCCCCCCCEEEEEE	33.31	-
537	N-linked_Glycosylation	NWSVSQINVSHARLR CCEEEEEECHHHHHH	22.92	19656770
575	N-linked_Glycosylation	QQREQTLNVTVCRCG HHHCEEEEEEEEECC	30.70	-
633	Phosphorylation	RTRFRGHSRGKSLLH HHHHCCCHHHHHHHH	45.62	27717184
637	Phosphorylation	RGHSRGKSLLHGLQE CCCHHHHHHHHHHHH	38.70	24899341
683	Phosphorylation	EPRATSRSLGRPPLR CCCCCCCCCCCCCCC	34.64	29899451

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

Oops, there are no upstream regulatory protein records of CAD15_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAD15_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CAD15_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARVC_MOUSE	Arvcf	physical	11719554

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-106 AND ASN-537, AND MASSSPECTROMETRY.
PubMed: 19656770