| UniProt ID | ADA11_HUMAN | |
|---|---|---|
| UniProt AC | O75078 | |
| Protein Name | Disintegrin and metalloproteinase domain-containing protein 11 | |
| Gene Name | ADAM11 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 769 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein. |
|
| Protein Description | Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein.. | |
| Protein Sequence | MRLLRRWAFAALLLSLLPTPGLGTQGPAGALRWGGLPQLGGPGAPEVTEPSRLVRESSGGEVRKQQLDTRVRQEPPGGPPVHLAQVSFVIPAFNSNFTLDLELNHHLLSSQYVERHFSREGTTQHSTGAGDHCYYQGKLRGNPHSFAALSTCQGLHGVFSDGNLTYIVEPQEVAGPWGAPQGPLPHLIYRTPLLPDPLGCREPGCLFAVPAQSAPPNRPRLRRKRQVRRGHPTVHSETKYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGLPEPSDATHLFSGRTFQSTSSGAAYVGGICSLSHGGGVNEYGNMGAMAVTLAQTLGQNLGMMWNKHRSSAGDCKCPDIWLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKPLKLLDPPECGNGFVEAGEECDCGSVQECSRAGGNCCKKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLHKLDGYYCDHEQGRCYGGRCKTRDRQCQVLWGHAAADRFCYEKLNVEGTERGSCGRKGSGWVQCSKQDVLCGFLLCVNISGAPRLGDLVGDISSVTFYHQGKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLPASAFNFSTCPGSGERRICSHHGVCSNEGKCICQPDWTGKDCSIHNPLPTSPPTGETERYKGPSGTNIIIGSIAGAVLVAAIVLGGTGWGFKNIRRGRSGGA | |
| 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 |
|---|---|---|---|---|---|
| 19 | Phosphorylation | LLLSLLPTPGLGTQG HHHHHCCCCCCCCCC | 29.92 | 26853621 | |
| 24 | Phosphorylation | LPTPGLGTQGPAGAL CCCCCCCCCCCHHCH | 35.08 | 46159007 | |
| 51 | Phosphorylation | APEVTEPSRLVRESS CCCCCCHHHHEECCC | 31.82 | 17081983 | |
| 57 | Phosphorylation | PSRLVRESSGGEVRK HHHHEECCCCCCHHH | 24.58 | 10400567 | |
| 58 | Phosphorylation | SRLVRESSGGEVRKQ HHHEECCCCCCHHHH | 46.17 | 10400577 | |
| 96 | N-linked_Glycosylation | VIPAFNSNFTLDLEL EEECCCCCEEEEEEE | 34.72 | UniProtKB CARBOHYD | |
| 163 | N-linked_Glycosylation | HGVFSDGNLTYIVEP EEECCCCCEEEEECC | 33.91 | UniProtKB CARBOHYD | |
| 308 | Phosphorylation | VQDDLLETLARLMVY CCHHHHHHHHHHHHH | 26.20 | 20058876 | |
| 331 | Phosphorylation | SDATHLFSGRTFQST CCCCCEECCCEEEEC | 33.45 | 24719451 | |
| 586 | Phosphorylation | GSCGRKGSGWVQCSK CCCCCCCCCCEECCC | 32.30 | 29759185 | |
| 592 | Phosphorylation | GSGWVQCSKQDVLCG CCCCEECCCCCEEEE | 19.09 | 29759185 | |
| 605 | N-linked_Glycosylation | CGFLLCVNISGAPRL EEEEEEEECCCCCCH | 23.01 | UniProtKB CARBOHYD | |
| 673 | N-linked_Glycosylation | CLPASAFNFSTCPGS EEECHHHCCCCCCCC | 29.67 | UniProtKB CARBOHYD | |
| 687 | Phosphorylation | SGERRICSHHGVCSN CCCCEEECCCCEECC | 19.02 | 23663014 | |
| 693 | Phosphorylation | CSHHGVCSNEGKCIC ECCCCEECCCCEEEE | 35.19 | 23663014 | |
| 739 | Phosphorylation | GTNIIIGSIAGAVLV CCCEEEHHHHHHHHH | 10.00 | 46159001 |
| 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 ADA11_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ADA11_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 ADA11_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| STC2_HUMAN | STC2 | physical | 16169070 |
| 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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