| UniProt ID | CADH9_HUMAN | |
|---|---|---|
| UniProt AC | Q9ULB4 | |
| Protein Name | Cadherin-9 | |
| Gene Name | CDH9 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 789 | |
| 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 | MRTYHYIPLFIWTYMFHTVDTILLQEKPNSYLSSKKIAGLTKDDGKMLRRTKRGWMWNQFFLLEEYTGTDTQYVGKLHTDQDKGDGNLKYILTGDGAGSLFVIDENTGDIHAAKKLDREEKSLYILRAKAIDRKTGRQVEPESEFIIKIHDINDNEPKFTKDLYTASVPEMSGVGTSVIQVTATDADDANYGNSAKVVYSILQGQPYFSVDPESGIIKTALPDMSRENREQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNNNPPRFPQSTYQFNSPESVPLGTHLGRIKANDPDVGENAEMEYSIAEGDGADMFDVITDKDTQEGIITVKQNLDFENQMLYTLRVDASNTHPDPRFLHLGPFKDTAVVKISVEDIDEPPVFTKVSYLIEVDEDVKEGSIIGQVTAYDPDARNNLIKYSVDRHTDMDRIFGIHSENGSIFTLKALDRESSPWHNITVTATEINNPKQSSHIPVFIRILDINDHAPEFAMYYETFVCENAKPGQLIQTVSVMDKDDPPRGHKFFFEPVPEFTLNPNFTIVDNKDNTAGIMTRKDGYSRNKMSTYLLPILIFDNDYPIQSSTGTLTIRVCACDNQGNMQSCTAEALILSAGLSTGALVAILLCVLILLILVVLFAALKRQRKKEPLIISKDDVRDNIVTYNDEGGGEEDTQAFDIGTLRNPEAREDSKLRRDVMPETIFQIRRTVPLWENIDVQDFIHRRLKENDADPSAPPYDSLATYAYEGNDSIADSLSSLESLTADCNQDYDYLSDWGPRFKKLADMYGGDDSDRD | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MRTYHYIPLF -----CCCCCCCCHH | 17.22 | 25002506 | |
| 4 | Phosphorylation | ----MRTYHYIPLFI ----CCCCCCCCHHH | 5.14 | 25002506 | |
| 6 | Phosphorylation | --MRTYHYIPLFIWT --CCCCCCCCHHHHH | 8.20 | 25002506 | |
| 13 | Phosphorylation | YIPLFIWTYMFHTVD CCCHHHHHHHHCCHH | 10.57 | 25002506 | |
| 14 | Phosphorylation | IPLFIWTYMFHTVDT CCHHHHHHHHCCHHH | 5.25 | 25002506 | |
| 18 | Phosphorylation | IWTYMFHTVDTILLQ HHHHHHCCHHHHHHC | 14.60 | 25002506 | |
| 21 | Phosphorylation | YMFHTVDTILLQEKP HHHCCHHHHHHCCCC | 14.80 | 25002506 | |
| 30 | Phosphorylation | LLQEKPNSYLSSKKI HHCCCCCCCCCCCCC | 35.66 | 24043423 | |
| 31 | Phosphorylation | LQEKPNSYLSSKKIA HCCCCCCCCCCCCCC | 19.76 | 24043423 | |
| 33 | Phosphorylation | EKPNSYLSSKKIAGL CCCCCCCCCCCCCCE | 31.70 | 24043423 | |
| 34 | Phosphorylation | KPNSYLSSKKIAGLT CCCCCCCCCCCCCEE | 35.06 | 24043423 | |
| 46 | 2-Hydroxyisobutyrylation | GLTKDDGKMLRRTKR CEECCCCCCHHHHCC | 41.58 | - | |
| 93 | Phosphorylation | GNLKYILTGDGAGSL CCEEEEEECCCCCEE | 24.54 | - | |
| 99 | Phosphorylation | LTGDGAGSLFVIDEN EECCCCCEEEEEECC | 20.35 | - | |
| 107 | Phosphorylation | LFVIDENTGDIHAAK EEEEECCCCCCCHHH | 33.90 | - | |
| 122 | Phosphorylation | KLDREEKSLYILRAK CCCHHHHHHHHEEHH | 29.68 | 19413330 | |
| 164 | Phosphorylation | PKFTKDLYTASVPEM CCCCCCEEECCCCCC | 15.47 | 23532336 | |
| 191 | Phosphorylation | TDADDANYGNSAKVV CCCCCCCCCCCHHHH | 21.29 | 23532336 | |
| 255 | N-linked_Glycosylation | LSGTTTVNITLTDVN CCCCEEEEEEEEECC | 21.31 | UniProtKB CARBOHYD | |
| 343 | Phosphorylation | DFENQMLYTLRVDAS CCCCCEEEEEEEECC | 9.82 | - | |
| 344 | Phosphorylation | FENQMLYTLRVDASN CCCCEEEEEEEECCC | 12.25 | 24719451 | |
| 387 | Phosphorylation | PPVFTKVSYLIEVDE CCEEEEEEEEEEECC | 18.77 | - | |
| 388 | Phosphorylation | PVFTKVSYLIEVDED CEEEEEEEEEEECCC | 18.06 | - | |
| 419 | Phosphorylation | ARNNLIKYSVDRHTD CCCCEEEEECCCCCC | 13.61 | 24719451 | |
| 420 | Phosphorylation | RNNLIKYSVDRHTDM CCCEEEEECCCCCCH | 16.73 | 24719451 | |
| 437 | N-linked_Glycosylation | IFGIHSENGSIFTLK EEEEEECCCCEEEEE | 53.15 | UniProtKB CARBOHYD | |
| 455 | N-linked_Glycosylation | RESSPWHNITVTATE CCCCCCCCEEEEEEE | 27.97 | UniProtKB CARBOHYD | |
| 536 | N-linked_Glycosylation | PEFTLNPNFTIVDNK CCCCCCCCCEEEECC | 45.69 | UniProtKB CARBOHYD | |
| 560 | Ubiquitination | KDGYSRNKMSTYLLP CCCCCCCCCCCCEEE | 32.87 | - | |
| 648 | Phosphorylation | KKEPLIISKDDVRDN CCCCCEEECHHHCCC | 24.04 | 22199227 | |
| 781 | Phosphorylation | FKKLADMYGGDDSDR HHHHHHHHCCCCCCC | 20.64 | - | |
| 786 | Phosphorylation | DMYGGDDSDRD---- HHHCCCCCCCC---- | 39.01 | 28857561 |
| 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 CADH9_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CADH9_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 CADH9_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MEOX2_HUMAN | MEOX2 | physical | 24722188 |
| 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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