| UniProt ID | KCD16_HUMAN | |
|---|---|---|
| UniProt AC | Q68DU8 | |
| Protein Name | BTB/POZ domain-containing protein KCTD16 | |
| Gene Name | KCTD16 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 428 | |
| Subcellular Localization | Cell junction, synapse, presynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane . | |
| Protein Description | Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity).. | |
| Protein Sequence | MALSGNCSRYYPREQGSAVPNSFPEVVELNVGGQVYFTRHSTLISIPHSLLWKMFSPKRDTANDLAKDSKGRFFIDRDGFLFRYILDYLRDRQVVLPDHFPEKGRLKREAEYFQLPDLVKLLTPDEIKQSPDEFCHSDFEDASQGSDTRICPPSSLLPADRKWGFITVGYRGSCTLGREGQADAKFRRVPRILVCGRISLAKEVFGETLNESRDPDRAPERYTSRFYLKFKHLERAFDMLSECGFHMVACNSSVTASFINQYTDDKIWSSYTEYVFYREPSRWSPSHCDCCCKNGKGDKEGESGTSCNDLSTSSCDSQSEASSPQETVICGPVTRQTNIQTLDRPIKKGPVQLIQQSEMRRKSDLLRTLTSGSRESNMSSKKKAVKEKLSIEEELEKCIQDFLKIKIPDRFPERKHPWQSELLRKYHL | |
| 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 |
|---|---|---|---|---|---|
| 56 | Phosphorylation | SLLWKMFSPKRDTAN HHHHHHHCCCCCCHH | 26.47 | 22210691 | |
| 84 | Phosphorylation | RDGFLFRYILDYLRD CCCHHHHHHHHHHHH | 9.86 | - | |
| 112 | Phosphorylation | RLKREAEYFQLPDLV CCHHHHHHHCCCHHH | 12.04 | 20068231 | |
| 130 | Phosphorylation | TPDEIKQSPDEFCHS CHHHHHCCCCHHCCC | 29.35 | 27732954 | |
| 137 | Phosphorylation | SPDEFCHSDFEDASQ CCCHHCCCCCCCCCC | 45.21 | 27732954 | |
| 143 | Phosphorylation | HSDFEDASQGSDTRI CCCCCCCCCCCCCEE | 47.60 | 27732954 | |
| 146 | Phosphorylation | FEDASQGSDTRICPP CCCCCCCCCCEECCH | 28.33 | 27732954 | |
| 148 | Phosphorylation | DASQGSDTRICPPSS CCCCCCCCEECCHHH | 24.51 | 27732954 | |
| 167 | Phosphorylation | DRKWGFITVGYRGSC CCCCEEEEEEECCEE | 12.96 | - | |
| 170 | Phosphorylation | WGFITVGYRGSCTLG CEEEEEEECCEECCC | 13.89 | - | |
| 185 | Malonylation | REGQADAKFRRVPRI CCCCCCCCCCCCCEE | 39.69 | 26320211 | |
| 185 | Ubiquitination | REGQADAKFRRVPRI CCCCCCCCCCCCCEE | 39.69 | 21890473 | |
| 231 | Ubiquitination | SRFYLKFKHLERAFD HHHHHHHHHHHHHHH | 45.77 | - | |
| 357 | Phosphorylation | PVQLIQQSEMRRKSD HHHHHCHHHHHHHHH | 19.58 | 28857561 | |
| 363 | Phosphorylation | QSEMRRKSDLLRTLT HHHHHHHHHHHHHHH | 31.51 | 22210691 | |
| 370 | Phosphorylation | SDLLRTLTSGSRESN HHHHHHHHHCCCCCC | 30.35 | - | |
| 373 | Phosphorylation | LRTLTSGSRESNMSS HHHHHHCCCCCCCHH | 32.42 | 22210691 | |
| 376 | Phosphorylation | LTSGSRESNMSSKKK HHHCCCCCCCHHHHH | 36.40 | - | |
| 379 | Phosphorylation | GSRESNMSSKKKAVK CCCCCCCHHHHHHHH | 43.17 | - |
| 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 KCD16_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KCD16_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 KCD16_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of KCD16_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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