UniProt ID | CADH5_MOUSE | |
---|---|---|
UniProt AC | P55284 | |
Protein Name | Cadherin-5 | |
Gene Name | Cdh5 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 784 | |
Subcellular Localization |
Cell junction . Cell membrane Single-pass type I membrane protein . Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions (By similarity). |
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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. This cadherin may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction.. | |
Protein Sequence | MQRLTELATALGAFLGLLAVAAMAGPNFPQIDTPNMLPAHHRQKRDWIWNQMHIDEEKNESLPHYVGKIKSNVNRQNAKYVLQGEFAGKIFGVDANTGNVLAYERLDREKVSEYFLTALIVDKNTNKNLEQPSSFTVKVHDINDNWPVFSHQVFNASVPEMSAIGTSVIRVTAVDADDPTVAGHATVLYQIVKGNEYFSIDNSGLIFTKIKNLDREKQAEYKIVVETQDALGLRGESGTATVMIRLEDINDNFPVFTQSTYTFSVPEDIRVGKPLGFLTVVDPDEPQNRMTKYSIMQGEYRDTFTIETDPKRNEGIIKPTKSLDYEVIQQYTFYIEATDPTIRYEYLSSTSGKNKAMVTINVLDVDEPPVFQRHFYHFKLPENQKKPLIGTVVAKDPDKAQRSIGYSIRKTSDRGQFFRITKQGNIYNEKELDRETYAWYNLTVEANELDSRGNPVGKESIVQVYIEVLDENDNPPEFAQPYEPKVCENAAQGKLVVQISATDKDVVPVNPKFKFALKNEDSNFTLINNHDNTANITVKYGQFNREHAKFHYLPVLISDNGVPSLTGTSTLTVGVCKCNEQGEFTFCEEMAAQAGVSIQALVAIFLCILTITVITLLIILRRRIRKQAHAHSKSALEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRGGSTKPLRSTMDARPAVYTQVQKPPRLAPGLHGGPREMATMIDVKKEEADNDGGGPPYDTLHIYGYEGAESIAESLSSLSTNSSDSDIDYDFLNDWGPRFKMLAELYGSDPQEELII | |
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 |
---|---|---|---|---|---|
59 | N-linked_Glycosylation | MHIDEEKNESLPHYV CCCCHHHCCCCCHHH | 47.58 | - | |
114 | Phosphorylation | DREKVSEYFLTALIV CHHHHHHHHHHEEEE | 9.07 | 26239621 | |
117 | Phosphorylation | KVSEYFLTALIVDKN HHHHHHHHEEEEECC | 14.98 | 26239621 | |
155 | N-linked_Glycosylation | VFSHQVFNASVPEMS EEEEEEEECCCCCHH | 32.23 | - | |
293 | Phosphorylation | PQNRMTKYSIMQGEY CCCCCCEEEEECCCC | 8.35 | - | |
294 | Phosphorylation | QNRMTKYSIMQGEYR CCCCCEEEEECCCCC | 17.09 | - | |
300 | Phosphorylation | YSIMQGEYRDTFTIE EEEECCCCCCCEEEE | 22.18 | 29895711 | |
308 | Phosphorylation | RDTFTIETDPKRNEG CCCEEEECCCCCCCC | 54.47 | 29895711 | |
320 | Phosphorylation | NEGIIKPTKSLDYEV CCCCCCCCCCCCHHH | 28.41 | 21454597 | |
407 | Phosphorylation | AQRSIGYSIRKTSDR HHHHHCEEEEECCCC | 15.65 | 29514104 | |
441 | N-linked_Glycosylation | RETYAWYNLTVEANE CCEEEEEEEEEEHHH | 20.66 | - | |
523 | N-linked_Glycosylation | ALKNEDSNFTLINNH EEECCCCCEEEEECC | 46.36 | - | |
535 | N-linked_Glycosylation | NNHDNTANITVKYGQ ECCCCCCEEEEEECC | 28.55 | - | |
645 | Phosphorylation | IHEQLVTYDEEGGGE HHHHHEEECCCCCCE | 17.55 | 22817900 | |
658 | Phosphorylation | GEMDTTSYDVSVLNS CEEECCEEEEEHHCC | 20.48 | 20530207 | |
665 | Phosphorylation | YDVSVLNSVRGGSTK EEEEHHCCCCCCCCC | 14.72 | - | |
685 | Phosphorylation | MDARPAVYTQVQKPP CCCCCCCEECCCCCC | 8.12 | 22817900 | |
686 | Phosphorylation | DARPAVYTQVQKPPR CCCCCCEECCCCCCC | 18.70 | 29472430 | |
690 | Ubiquitination | AVYTQVQKPPRLAPG CCEECCCCCCCCCCC | 59.12 | 22790023 | |
731 | Phosphorylation | PYDTLHIYGYEGAES CCCCEEEECCCHHHH | 11.69 | 22817900 | |
733 | Phosphorylation | DTLHIYGYEGAESIA CCEEEECCCHHHHHH | 8.33 | 22817900 | |
776 | Phosphorylation | MLAELYGSDPQEELI HHHHHHCCCCCHHCC | 32.34 | 20047332 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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685 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CADH5_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of CADH5_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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