CAD15_HUMAN - dbPTM
CAD15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAD15_HUMAN
UniProt AC P55291
Protein Name Cadherin-15
Gene Name CDH15
Organism Homo sapiens (Human).
Sequence Length 814
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 MDAAFLLVLGLLAQSLCLSLGVPGWRRPTTLYPWRRAPALSRVRRAWVIPPISVSENHKRLPYPLVQIKSDKQQLGSVIYSIQGPGVDEEPRGVFSIDKFTGKVFLNAMLDREKTDRFRLRAFALDLGGSTLEDPTDLEIVVVDQNDNRPAFLQEAFTGRVLEGAVPGTYVTRAEATDADDPETDNAALRFSILQQGSPELFSIDELTGEIRTVQVGLDREVVAVYNLTLQVADMSGDGLTATASAIITLDDINDNAPEFTRDEFFMEAIEAVSGVDVGRLEVEDRDLPGSPNWVARFTILEGDPDGQFTIRTDPKTNEGVLSIVKALDYESCEHYELKVSVQNEAPLQAAALRAERGQAKVRVHVQDTNEPPVFQENPLRTSLAEGAPPGTLVATFSARDPDTEQLQRLSYSKDYDPEDWLQVDAATGRIQTQHVLSPASPFLKGGWYRAIVLAQDDASQPRTATGTLSIEILEVNDHAPVLAPPPPGSLCSEPHQGPGLLLGATDEDLPPHGAPFHFQLSPRLPELGRNWSLSQVNVSHARLRPRHQVPEGLHRLSLLLRDSGQPPQQREQPLNVTVCRCGKDGVCLPGAAALLAGGTGLSLGALVIVLASALLLLVLVLLVALRARFWKQSRGKGLLHGPQDDLRDNVLNYDEQGGGEEDQDAYDISQLRHPTALSLPLGPPPLRRDAPQGRLHPQPPRVLPTSPLDIADFINDGLEAADSDPSVPPYDTALIYDYEGDGSVAGTLSSILSSQGDEDQDYDYLRDWGPRFARLADMYGHPCGLEYGARWDHQAREGLSPGALLPRHRGRTA
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
41PhosphorylationWRRAPALSRVRRAWV
CCCCCHHHHCCEEEE
30.7323403867
227N-linked_GlycosylationREVVAVYNLTLQVAD
HHHEEEEEEEEEEEC
21.68UniProtKB CARBOHYD
310PhosphorylationGDPDGQFTIRTDPKT
CCCCCCEEEEECCCC
11.1424719451
330PhosphorylationSIVKALDYESCEHYE
HHEEECCHHHCCEEE
15.59-
336PhosphorylationDYESCEHYELKVSVQ
CHHHCCEEEEEEEEC
10.72-
441PhosphorylationQHVLSPASPFLKGGW
EEECCCCCCCCCCCE
21.4024719451
531N-linked_GlycosylationRLPELGRNWSLSQVN
CCCCCCCCCCHHHCC
30.78UniProtKB CARBOHYD
538N-linked_GlycosylationNWSLSQVNVSHARLR
CCCHHHCCCCCCCCC
23.18UniProtKB CARBOHYD
576N-linked_GlycosylationQQREQPLNVTVCRCG
CCCCCCCEEEEEECC
33.81UniProtKB CARBOHYD
632UbiquitinationALRARFWKQSRGKGL
HHHHHHHHHHCCCCC
35.3722817900
637UbiquitinationFWKQSRGKGLLHGPQ
HHHHHCCCCCCCCCC
45.3221906983
801PhosphorylationHQAREGLSPGALLPR
HHHCCCCCCCCCCCC
31.9532142685

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 CAD15_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAD15_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 CAD15_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARVC_HUMANARVCFphysical
11058098
CTNB1_MOUSECtnnb1physical
9545347
SGTA_HUMANSGTAphysical
25416956

Drug and Disease Associations
Kegg Disease
H00773 Non-syndromic autosomal dominant mental retardation
OMIM Disease
Note=A chromosomal aberration involving CDH15 and KIRREL3 is found in a patient with severe mental retardation and dysmorphic facial features. Translocation t(11
16)(q24.2
q24).
612580
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAD15_HUMAN

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Related Literatures of Post-Translational Modification

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