| UniProt ID | CAD12_HUMAN | |
|---|---|---|
| UniProt AC | P55289 | |
| Protein Name | Cadherin-12 | |
| Gene Name | CDH12 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 794 | |
| 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 | MLTRNCLSLLLWVLFDGGLLTPLQPQPQQTLATEPRENVIHLPGQRSHFQRVKRGWVWNQFFVLEEYVGSEPQYVGKLHSDLDKGEGTVKYTLSGDGAGTVFTIDETTGDIHAIRSLDREEKPFYTLRAQAVDIETRKPLEPESEFIIKVQDINDNEPKFLDGPYVATVPEMSPVGAYVLQVKATDADDPTYGNSARVVYSILQGQPYFSIDPKTGVIRTALPNMDREVKEQYQVLIQAKDMGGQLGGLAGTTIVNITLTDVNDNPPRFPKSIFHLKVPESSPIGSAIGRIRAVDPDFGQNAEIEYNIVPGDGGNLFDIVTDEDTQEGVIKLKKPLDFETKKAYTFKVEASNLHLDHRFHSAGPFKDTATVKISVLDVDEPPVFSKPLYTMEVYEDTPVGTIIGAVTAQDLDVGSSAVRYFIDWKSDGDSYFTIDGNEGTIATNELLDRESTAQYNFSIIASKVSNPLLTSKVNILINVLDVNEFPPEISVPYETAVCENAKPGQIIQIVSAADRDLSPAGQQFSFRLSPEAAIKPNFTVRDFRNNTAGIETRRNGYSRRQQELYFLPVVIEDSSYPVQSSTNTMTIRVCRCDSDGTILSCNVEAIFLPVGLSTGALIAILLCIVILLAIVVLYVALRRQKKKDTLMTSKEDIRDNVIHYDDEGGGEEDTQAFDIGALRNPKVIEENKIRRDIKPDSLCLPRQRPPMEDNTDIRDFIHQRLQENDVDPTAPPYDSLATYAYEGSGSVAESLSSIDSLTTEADQDYDYLTDWGPRFKVLADMFGEEESYNPDKVT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 126 | Phosphorylation | REEKPFYTLRAQAVD CCCCCCEEEEEEEEE | 15.33 | 24719451 | |
| 200 | Phosphorylation | GNSARVVYSILQGQP CCCHHHHHHHHCCCC | 6.27 | - | |
| 233 | Phosphorylation | DREVKEQYQVLIQAK CHHHHHHHHHHHHHH | 11.15 | - | |
| 256 | N-linked_Glycosylation | LAGTTIVNITLTDVN CCCCEEEEEEEECCC | 20.06 | UniProtKB CARBOHYD | |
| 286 | Phosphorylation | PESSPIGSAIGRIRA CCCCCCCHHHEEEEE | 19.89 | 17924679 | |
| 340 | Phosphorylation | KKPLDFETKKAYTFK CCCCCCCCCEEEEEE | 37.53 | - | |
| 385 | Phosphorylation | VDEPPVFSKPLYTME CCCCCCCCCCEEEEE | 33.33 | 24719451 | |
| 456 | N-linked_Glycosylation | RESTAQYNFSIIASK CCCCCCCCEEEEEEC | 16.47 | UniProtKB CARBOHYD | |
| 525 | Phosphorylation | SPAGQQFSFRLSPEA CCCCCCEEEEECHHH | 12.72 | 24719451 | |
| 529 | Phosphorylation | QQFSFRLSPEAAIKP CCEEEEECHHHCCCC | 19.21 | 29449344 | |
| 537 | N-linked_Glycosylation | PEAAIKPNFTVRDFR HHHCCCCCCEEEECC | 39.97 | UniProtKB CARBOHYD | |
| 539 | Phosphorylation | AAIKPNFTVRDFRNN HCCCCCCEEEECCCC | 22.67 | 29083192 | |
| 545 | N-linked_Glycosylation | FTVRDFRNNTAGIET CEEEECCCCCCCCEE | 50.64 | UniProtKB CARBOHYD | |
| 547 | Phosphorylation | VRDFRNNTAGIETRR EEECCCCCCCCEECC | 29.79 | 25332170 | |
| 641 | Trimethylation | YVALRRQKKKDTLMT HHHHHHHHHCCCCCC | 61.04 | - | |
| 641 | Methylation | YVALRRQKKKDTLMT HHHHHHHHHCCCCCC | 61.04 | - | |
| 642 | Trimethylation | VALRRQKKKDTLMTS HHHHHHHHCCCCCCC | 47.76 | - | |
| 642 | Methylation | VALRRQKKKDTLMTS HHHHHHHHCCCCCCC | 47.76 | - | |
| 648 | Phosphorylation | KKKDTLMTSKEDIRD HHCCCCCCCHHHHHH | 39.50 | 29449344 | |
| 649 | Phosphorylation | KKDTLMTSKEDIRDN HCCCCCCCHHHHHHC | 21.78 | 29449344 | |
| 787 | Phosphorylation | DMFGEEESYNPDKVT HHHCCCHHCCCCCCC | 33.23 | - |
| 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 CAD12_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAD12_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 CAD12_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CAD12_HUMAN !! | ||||
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND MASSSPECTROMETRY. | |
