UniProt ID | CAD16_HUMAN | |
---|---|---|
UniProt AC | O75309 | |
Protein Name | Cadherin-16 | |
Gene Name | CDH16 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 829 | |
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 | MVPAWLWLLCVSVPQALPKAQPAELSVEVPENYGGNFPLYLTKLPLPREGAEGQIVLSGDSGKATEGPFAMDPDSGFLLVTRALDREEQAEYQLQVTLEMQDGHVLWGPQPVLVHVKDENDQVPHFSQAIYRARLSRGTRPGIPFLFLEASDRDEPGTANSDLRFHILSQAPAQPSPDMFQLEPRLGALALSPKGSTSLDHALERTYQLLVQVKDMGDQASGHQATATVEVSIIESTWVSLEPIHLAENLKVLYPHHMAQVHWSGGDVHYHLESHPPGPFEVNAEGNLYVTRELDREAQAEYLLQVRAQNSHGEDYAAPLELHVLVMDENDNVPICPPRDPTVSIPELSPPGTEVTRLSAEDADAPGSPNSHVVYQLLSPEPEDGVEGRAFQVDPTSGSVTLGVLPLRAGQNILLLVLAMDLAGAEGGFSSTCEVEVAVTDINDHAPEFITSQIGPISLPEDVEPGTLVAMLTAIDADLEPAFRLMDFAIERGDTEGTFGLDWEPDSGHVRLRLCKNLSYEAAPSHEVVVVVQSVAKLVGPGPGPGATATVTVLVERVMPPPKLDQESYEASVPISAPAGSFLLTIQPSDPISRTLRFSLVNDSEGWLCIEKFSGEVHTAQSLQGAQPGDTYTVLVEAQDTDEPRLSASAPLVIHFLKAPPAPALTLAPVPSQYLCTPRQDHGLIVSGPSKDPDLASGHGPYSFTLGPNPTVQRDWRLQTLNGSHAYLTLALHWVEPREHIIPVVVSHNAQMWQLLVRVIVCRCNVEGQCMRKVGRMKGMPTKLSAVGILVGTLVAIGIFLILIFTHWTMSRKKDPDQPADSVPLKATV | |
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 |
---|---|---|---|---|---|
65 | O-linked_Glycosylation | SGDSGKATEGPFAMD ECCCCCCCCCCCCCC | 44.98 | OGP | |
161 | Phosphorylation | DEPGTANSDLRFHIL CCCCCCCCCEEEEEE | 35.24 | - | |
192 | Phosphorylation | RLGALALSPKGSTSL CCEEEEECCCCCCCH | 20.96 | 24719451 | |
197 | Phosphorylation | ALSPKGSTSLDHALE EECCCCCCCHHHHHH | 41.81 | 21130716 | |
198 | Phosphorylation | LSPKGSTSLDHALER ECCCCCCCHHHHHHH | 33.23 | 21130716 | |
517 | N-linked_Glycosylation | VRLRLCKNLSYEAAP EEEEEECCCCCCCCC | 32.97 | UniProtKB CARBOHYD | |
519 | Phosphorylation | LRLCKNLSYEAAPSH EEEECCCCCCCCCCC | 30.25 | - | |
534 | Phosphorylation | EVVVVVQSVAKLVGP EEEEEEEEEHHHHCC | 16.66 | - | |
602 | N-linked_Glycosylation | TLRFSLVNDSEGWLC EEEEEEEECCCCEEE | 53.00 | UniProtKB CARBOHYD | |
666 | O-linked_Glycosylation | APPAPALTLAPVPSQ CCCCCCEEECCCCCC | 23.99 | OGP | |
687 | Phosphorylation | QDHGLIVSGPSKDPD CCCCEEEECCCCCCC | 37.68 | 24043423 | |
690 | Phosphorylation | GLIVSGPSKDPDLAS CEEEECCCCCCCCCC | 53.89 | 24043423 | |
705 | O-linked_Glycosylation | GHGPYSFTLGPNPTV CCCCCEEECCCCCCC | 25.51 | OGP | |
722 | N-linked_Glycosylation | DWRLQTLNGSHAYLT CEEEEECCCCCEEEE | 53.99 | UniProtKB CARBOHYD | |
782 | Phosphorylation | GRMKGMPTKLSAVGI CCCCCCCCHHHHHHH | 35.41 | 22210691 | |
806 | Phosphorylation | IFLILIFTHWTMSRK HHHHHHHHHHHHHCC | 14.98 | - | |
809 | Phosphorylation | ILIFTHWTMSRKKDP HHHHHHHHHHCCCCC | 9.54 | - | |
811 | Phosphorylation | IFTHWTMSRKKDPDQ HHHHHHHHCCCCCCC | 33.31 | 22210691 | |
822 | Phosphorylation | DPDQPADSVPLKATV CCCCCCCCCCCCCCC | 27.95 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of CAD16_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAD16_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 CAD16_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CRYAB_HUMAN | CRYAB | physical | 18343407 | |
G6PC_HUMAN | G6PC | physical | 21988832 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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