| UniProt ID | CADH6_HUMAN | |
|---|---|---|
| UniProt AC | P55285 | |
| Protein Name | Cadherin-6 | |
| Gene Name | CDH6 | |
| 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 | MRTYRYFLLLFWVGQPYPTLSTPLSKRTSGFPAKKRALELSGNSKNELNRSKRSWMWNQFFLLEEYTGSDYQYVGKLHSDQDRGDGSLKYILSGDGAGDLFIINENTGDIQATKRLDREEKPVYILRAQAINRRTGRPVEPESEFIIKIHDINDNEPIFTKEVYTATVPEMSDVGTFVVQVTATDADDPTYGNSAKVVYSILQGQPYFSVESETGIIKTALLNMDRENREQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQSTYQFKTPESSPPGTPIGRIKASDADVGENAEIEYSITDGEGLDMFDVITDQETQEGIITVKKLLDFEKKKVYTLKVEASNPYVEPRFLYLGPFKDSATVRIVVEDVDEPPVFSKLAYILQIREDAQINTTIGSVTAQDPDAARNPVKYSVDRHTDMDRIFNIDSGNGSIFTSKLLDRETLLWHNITVIATEINNPKQSSRVPLYIKVLDVNDNAPEFAEFYETFVCEKAKADQLIQTLHAVDKDDPYSGHQFSFSLAPEAASGSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCACDHHGNMQSCHAEALIHPTGLSTGALVAILLCIVILLVTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPEAIEDNKLRRDIVPEALFLPRRTPTARDNTDVRDFINQRLKENDTDPTAPPYDSLATYAYEGTGSVADSLSSLESVTTDADQDYDYLSDWGPRFKKLADMYGGVDSDKDS | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MRTYRYFLLLFWV --CCCEEEHHHHHHC | 6.54 | 24719451 | |
| 28 | O-linked_Glycosylation | STPLSKRTSGFPAKK CCCHHHCCCCCCHHH | 36.62 | 30620550 | |
| 29 | O-linked_Glycosylation | TPLSKRTSGFPAKKR CCHHHCCCCCCHHHH | 42.33 | 30620550 | |
| 35 | Methylation | TSGFPAKKRALELSG CCCCCHHHHHHHHCC | 45.04 | - | |
| 44 | Phosphorylation | ALELSGNSKNELNRS HHHHCCCCHHHHCHH | 40.14 | 23612710 | |
| 49 | N-linked_Glycosylation | GNSKNELNRSKRSWM CCCHHHHCHHHHHHH | 39.75 | UniProtKB CARBOHYD | |
| 90 | Phosphorylation | RGDGSLKYILSGDGA CCCCCEEEEEECCCC | 16.64 | 22210691 | |
| 143 | Phosphorylation | GRPVEPESEFIIKIH CCCCCCCCEEEEEEE | 48.82 | 27251275 | |
| 255 | N-linked_Glycosylation | LSGTTTVNITLTDVN CCCCEEEEEEEECCC | 21.31 | UniProtKB CARBOHYD | |
| 285 | Phosphorylation | PESSPPGTPIGRIKA CCCCCCCCCCEEEEC | 19.94 | 18785766 | |
| 343 | Phosphorylation | DFEKKKVYTLKVEAS CCCCCEEEEEEEEEC | 18.42 | 22817900 | |
| 350 | Phosphorylation | YTLKVEASNPYVEPR EEEEEEECCCCCCCC | 25.49 | 30631047 | |
| 360 | Phosphorylation | YVEPRFLYLGPFKDS CCCCCEEEEECCCCC | 13.60 | 21406692 | |
| 367 | Phosphorylation | YLGPFKDSATVRIVV EEECCCCCCEEEEEE | 26.82 | 21406692 | |
| 369 | Phosphorylation | GPFKDSATVRIVVED ECCCCCCEEEEEEEC | 17.80 | 21406692 | |
| 399 | N-linked_Glycosylation | IREDAQINTTIGSVT HHCCCCCCCEEEEEE | 21.06 | 16335952 | |
| 425 | Phosphorylation | KYSVDRHTDMDRIFN EEEEECCCCHHHEEE | 33.63 | - | |
| 437 | N-linked_Glycosylation | IFNIDSGNGSIFTSK EEEEECCCCCEEEHH | 45.02 | UniProtKB CARBOHYD | |
| 455 | N-linked_Glycosylation | RETLLWHNITVIATE CCHHHEECEEEEEEE | 21.75 | UniProtKB CARBOHYD | |
| 536 | N-linked_Glycosylation | PEAASGSNFTIQDNK CCCCCCCCCEEECCC | 41.42 | UniProtKB CARBOHYD | |
| 648 | Phosphorylation | KKEPLIISKEDIRDN HCCCCEEEHHHHHHC | 24.01 | 28060719 | |
| 649 | Ubiquitination | KEPLIISKEDIRDNI CCCCEEEHHHHHHCC | 49.34 | 32142685 | |
| 669 | Phosphorylation | EGGGEEDTQAFDIGT CCCCCCCCCEEECCC | 25.69 | 28857561 | |
| 687 | Ubiquitination | PEAIEDNKLRRDIVP HHHHCCCCCCCCCCC | 56.55 | 32142685 | |
| 703 | Phosphorylation | ALFLPRRTPTARDNT HHCCCCCCCCCCCCC | 26.69 | 22199227 | |
| 705 | Phosphorylation | FLPRRTPTARDNTDV CCCCCCCCCCCCCCH | 33.44 | 22199227 | |
| 781 | Phosphorylation | FKKLADMYGGVDSDK HHHHHHHHCCCCCCC | 15.98 | 28060719 | |
| 786 | Phosphorylation | DMYGGVDSDKDS--- HHHCCCCCCCCC--- | 44.12 | 28355574 | |
| 790 | Phosphorylation | GVDSDKDS------- CCCCCCCC------- | 48.11 | 29970186 |
| 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 CADH6_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CADH6_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 CADH6_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CADH6_HUMAN | CDH6 | physical | 10207020 | |
| CAD18_HUMAN | CDH18 | physical | 10207020 |
| 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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| N-linked Glycosylation | |
| Reference | PubMed |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399, AND MASSSPECTROMETRY. | |