CAD18_HUMAN - dbPTM
CAD18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAD18_HUMAN
UniProt AC Q13634
Protein Name Cadherin-18
Gene Name CDH18
Organism Homo sapiens (Human).
Sequence Length 790
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 MKITSTSCICPVLVCLCFVQRCYGTAHHSSIKVMRNQTKHIEGETEVHHRPKRGWVWNQFFVLEEHMGPDPQYVGKLHSNSDKGDGSVKYILTGEGAGTIFIIDDTTGDIHSTKSLDREQKTHYVLHAQAIDRRTNKPLEPESEFIIKVQDINDNAPKFTDGPYIVTVPEMSDMGTSVLQVTATDADDPTYGNSARVVYSILQGQPYFSVDPKTGVIRTALHNMDREAREHYSVVIQAKDMAGQVGGLSGSTTVNITLTDVNDNPPRFPQKHYQLYVPESAQVGSAVGKIKANDADTGSNADMTYSIINGDGMGIFSISTDKETREGILSLKKPLNYEKKKSYTLNIEGANTHLDFRFSHLGPFKDATMLKIIVGDVDEPPLFSMPSYLMEVYENAKIGTVVGTVLAQDPDSTNSLVRYFINYNVEDDRFFNIDANTGTIRTTKVLDREETPWYNITVTASEIDNPDLLSHVTVGIRVLDVNDNPPELAREYDIIVCENSKPGQVIHTISATDKDDFANGPRFNFFLDERLPVNPNFTLKDNEDNTASILTRRRRFSRTVQDVYYLPIMISDGGIPSLSSSSTLTIRVCACERDGRVRTCHAEAFLSSAGLSTGALIAILLCVLILLAIVVLFITLRRSKKEPLIISEEDVRENVVTYDDEGGGEEDTEAFDITALRNPSAAEELKYRRDIRPEVKLTPRHQTSSTLESIDVQEFIKQRLAEADLDPSVPPYDSLQTYAYEGQRSEAGSISSLDSATTQSDQDYHYLGDWGPEFKKLAELYGEIESERTT
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
36N-linked_GlycosylationSSIKVMRNQTKHIEG
HHHHEEECCCCCEEC
35.46UniProtKB CARBOHYD
87PhosphorylationNSDKGDGSVKYILTG
CCCCCCCEEEEEEEC
21.8522617229
199PhosphorylationGNSARVVYSILQGQP
CCCHHHHHHHHCCCC
6.27-
214PhosphorylationYFSVDPKTGVIRTAL
CEEECCCCCHHHHHH
41.9122210691
255N-linked_GlycosylationLSGSTTVNITLTDVN
CCCCEEEEEEEEECC
21.31UniProtKB CARBOHYD
305PhosphorylationGSNADMTYSIINGDG
CCCCCCEEEEECCCC
7.4030576142
306PhosphorylationSNADMTYSIINGDGM
CCCCCEEEEECCCCC
14.0730576142
317PhosphorylationGDGMGIFSISTDKET
CCCCEEEEEECCCCC
17.4430576142
330PhosphorylationETREGILSLKKPLNY
CCHHHHHHCCCCCCC
35.9024719451
365UbiquitinationFSHLGPFKDATMLKI
EHHCCCCCCCEEEEE
49.972190698
388PhosphorylationPLFSMPSYLMEVYEN
CCCCCCHHHHHHHHH
12.2819658100
455N-linked_GlycosylationREETPWYNITVTASE
CCCCCCEEEEEEHHH
21.42UniProtKB CARBOHYD
536N-linked_GlycosylationERLPVNPNFTLKDNE
CCCCCCCCCEECCCC
37.01UniProtKB CARBOHYD
548PhosphorylationDNEDNTASILTRRRR
CCCCCCHHHHHHHHH
18.9824719451
639PhosphorylationLFITLRRSKKEPLII
HHHHHHHCCCCCEEE
41.46-
647PhosphorylationKKEPLIISEEDVREN
CCCCEEECHHHHHHC
28.12-
674PhosphorylationDTEAFDITALRNPSA
CCCEEEEEECCCCCH
22.8324719451
786PhosphorylationELYGEIESERTT---
HHHHHHHCCCCC---
37.73-

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 CAD18_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAD18_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 CAD18_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAD18_HUMANCDH18physical
10207020
MYOG_HUMANMYOGphysical
21988832

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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAD18_HUMAN

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Related Literatures of Post-Translational Modification

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