CADH3_HUMAN - dbPTM
CADH3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CADH3_HUMAN
UniProt AC P22223
Protein Name Cadherin-3
Gene Name CDH3
Organism Homo sapiens (Human).
Sequence Length 829
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..
Protein Sequence MGLPRGPLASLLLLQVCWLQCAASEPCRAVFREAEVTLEAGGAEQEPGQALGKVFMGCPGQEPALFSTDNDDFTVRNGETVQERRSLKERNPLKIFPSKRILRRHKRDWVVAPISVPENGKGPFPQRLNQLKSNKDRDTKIFYSITGPGADSPPEGVFAVEKETGWLLLNKPLDREEIAKYELFGHAVSENGASVEDPMNISIIVTDQNDHKPKFTQDTFRGSVLEGVLPGTSVMQVTATDEDDAIYTYNGVVAYSIHSQEPKDPHDLMFTIHRSTGTISVISSGLDREKVPEYTLTIQATDMDGDGSTTTAVAVVEILDANDNAPMFDPQKYEAHVPENAVGHEVQRLTVTDLDAPNSPAWRATYLIMGGDDGDHFTITTHPESNQGILTTRKGLDFEAKNQHTLYVEVTNEAPFVLKLPTSTATIVVHVEDVNEAPVFVPPSKVVEVQEGIPTGEPVCVYTAEDPDKENQKISYRILRDPAGWLAMDPDSGQVTAVGTLDREDEQFVRNNIYEVMVLAMDNGSPPTTGTGTLLLTLIDVNDHGPVPEPRQITICNQSPVRQVLNITDKDLSPHTSPFQAQLTDDSDIYWTAEVNEEGDTVVLSLKKFLKQDTYDVHLSLSDHGNKEQLTVIRATVCDCHGHVETCPGPWKGGFILPVLGAVLALLFLLLVLLLLVRKKRKIKEPLLLPEDDTRDNVFYYGEEGGGEEDQDYDITQLHRGLEARPEVVLRNDVAPTIIPTPMYRPRPANPDEIGNFIIENLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASDQDQDYDYLNEWGSRFKKLADMYGGGEDD
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
115PhosphorylationDWVVAPISVPENGKG
CEEEEECCCCCCCCC		30.4724719451
133PhosphorylationQRLNQLKSNKDRDTK
HHHHHHHCCCCCCCC		58.67-
139PhosphorylationKSNKDRDTKIFYSIT
HCCCCCCCCEEEEEE		27.25-
143PhosphorylationDRDTKIFYSITGPGA
CCCCCEEEEEECCCC		11.57-
189PhosphorylationELFGHAVSENGASVE
HHHCEECCCCCCCCC		26.5722210691
200N-linked_GlycosylationASVEDPMNISIIVTD
CCCCCCCEEEEEEEC		30.18UniProtKB CARBOHYD
202PhosphorylationVEDPMNISIIVTDQN
CCCCCEEEEEEECCC		10.9722210691
308PhosphorylationTDMDGDGSTTTAVAV
EECCCCCCEEEEEEE		27.5928857561
309PhosphorylationDMDGDGSTTTAVAVV
ECCCCCCEEEEEEEE		33.4228857561
310PhosphorylationMDGDGSTTTAVAVVE
CCCCCCEEEEEEEEE		17.9228857561
311PhosphorylationDGDGSTTTAVAVVEI
CCCCCEEEEEEEEEE		21.1528857561
350PhosphorylationGHEVQRLTVTDLDAP
CCEEEEEEEECCCCC		24.4522210691
352PhosphorylationEVQRLTVTDLDAPNS
EEEEEEEECCCCCCC		26.1322210691
359PhosphorylationTDLDAPNSPAWRATY
ECCCCCCCCCEEEEE		18.22-
391PhosphorylationESNQGILTTRKGLDF
CCCCCEEEEECCCCE		23.7222210691
392PhosphorylationSNQGILTTRKGLDFE
CCCCEEEEECCCCEE		27.2622210691
492PhosphorylationWLAMDPDSGQVTAVG
CEEECCCCCCEEEEE		36.19-
566N-linked_GlycosylationSPVRQVLNITDKDLS
CCCEEEECCCCCCCC		35.94UniProtKB CARBOHYD
605PhosphorylationEGDTVVLSLKKFLKQ
CCCEEEEEHHHHHCC		26.9124719451
620PhosphorylationDTYDVHLSLSDHGNK
CEEEEEEECCCCCCH		15.7928355574
631PhosphorylationHGNKEQLTVIRATVC
CCCHHHEEEEEEEEE		17.3723312004
682 (in isoform 2)Ubiquitination-67.9921906983
682 (in isoform 1)Ubiquitination-67.9921906983
682UbiquitinationLLVRKKRKIKEPLLL
HHHHHHCCCCCCCCC		67.9921906983
684 (in isoform 2)Ubiquitination-57.2121906983
684 (in isoform 1)Ubiquitination-57.2121906983
684UbiquitinationVRKKRKIKEPLLLPE
HHHHCCCCCCCCCCC		57.2121906983
694PhosphorylationLLLPEDDTRDNVFYY
CCCCCCCCCCCEEEE		52.8527966365
700PhosphorylationDTRDNVFYYGEEGGG
CCCCCEEEECCCCCC		13.2827259358
701PhosphorylationTRDNVFYYGEEGGGE
CCCCEEEECCCCCCC		13.4427259358
713PhosphorylationGGEEDQDYDITQLHR
CCCCCCCCCHHHHHC		12.0125106551
716PhosphorylationEDQDYDITQLHRGLE
CCCCCCHHHHHCHHH		23.3726356563
741PhosphorylationVAPTIIPTPMYRPRP
CCCCCCCCCCCCCCC		15.4123312004
744PhosphorylationTIIPTPMYRPRPANP
CCCCCCCCCCCCCCH		20.7623312004
818UbiquitinationEWGSRFKKLADMYGG
HHHHHHHHHHHHHCC		46.312190698
818 (in isoform 1)Ubiquitination-46.3121906983
823PhosphorylationFKKLADMYGGGEDD-
HHHHHHHHCCCCCC-		17.11-
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 CADH3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CADH3_HUMAN !!
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 CADH3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CADH1_HUMANCDH1physical
10910767
CADH3_HUMANCDH3physical
10910767
CTNA1_HUMANCTNNA1physical
10910767
CTNB1_HUMANCTNNB1physical
10910767
PLAK_HUMANJUPphysical
10910767
CTND1_HUMANCTNND1physical
23180380
CTNB1_HUMANCTNNB1physical
23180380
Drug and Disease Associations
Kegg Disease
H00639 Ectodermal dysplasia, ectrodactyly, and macular dystrophy (EEM syndrome)
H00785 Congenital hypotrichosis with juvenile macular dystrophy
OMIM Disease
601553Hypotrichosis congenital with juvenile macular dystrophy (HJMD)
225280Ectodermal dysplasia, ectrodactyly, and macular dystrophy syndrome (EEMS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CADH3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-713, AND MASSSPECTROMETRY.

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