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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
41 | Phosphorylation | WRRAPALSRVRRAWV CCCCCHHHHCCEEEE | 30.73 | 23403867 | |
227 | N-linked_Glycosylation | REVVAVYNLTLQVAD HHHEEEEEEEEEEEC | 21.68 | UniProtKB CARBOHYD | |
310 | Phosphorylation | GDPDGQFTIRTDPKT CCCCCCEEEEECCCC | 11.14 | 24719451 | |
330 | Phosphorylation | SIVKALDYESCEHYE HHEEECCHHHCCEEE | 15.59 | - | |
336 | Phosphorylation | DYESCEHYELKVSVQ CHHHCCEEEEEEEEC | 10.72 | - | |
441 | Phosphorylation | QHVLSPASPFLKGGW EEECCCCCCCCCCCE | 21.40 | 24719451 | |
531 | N-linked_Glycosylation | RLPELGRNWSLSQVN CCCCCCCCCCHHHCC | 30.78 | UniProtKB CARBOHYD | |
538 | N-linked_Glycosylation | NWSLSQVNVSHARLR CCCHHHCCCCCCCCC | 23.18 | UniProtKB CARBOHYD | |
576 | N-linked_Glycosylation | QQREQPLNVTVCRCG CCCCCCCEEEEEECC | 33.81 | UniProtKB CARBOHYD | |
632 | Ubiquitination | ALRARFWKQSRGKGL HHHHHHHHHHCCCCC | 35.37 | 22817900 | |
637 | Ubiquitination | FWKQSRGKGLLHGPQ HHHHHCCCCCCCCCC | 45.32 | 21906983 | |
801 | Phosphorylation | HQAREGLSPGALLPR HHHCCCCCCCCCCCC | 31.95 | 32142685 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAD15_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ARVC_HUMAN | ARVCF | physical | 11058098 | |
CTNB1_MOUSE | Ctnnb1 | physical | 9545347 | |
SGTA_HUMAN | SGTA | physical | 25416956 |
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. |
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