Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9C196
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9C196-F1 | Predicted | AlphaFoldDB |
No variants for Q9C196
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9C196 | |||||
No associated diseases with Q9C196
6 regional properties for Q9C196
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cyclic nucleotide-binding domain | 160 - 290 | IPR000595-1 |
| domain | Cyclic nucleotide-binding domain | 292 - 410 | IPR000595-2 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 188 - 204 | IPR018488-1 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 236 - 253 | IPR018488-2 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 319 - 335 | IPR018488-3 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 357 - 374 | IPR018488-4 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cAMP-dependent protein kinase complex | An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cAMP binding | Binding to cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate). |
| cAMP-dependent protein kinase regulator activity | Modulation of the activity of the enzyme cAMP-dependent protein kinase. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| regulation of protein phosphorylation | Any process that modulates the frequency, rate or extent of addition of phosphate groups into an amino acid in a protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAESAFPSAQ | QPLRVGTKDD | KAAAFQKISE | EDEYEVTSPT | DPTFRSANAA | AASSSTGSPF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FGGSYGENSG | PIRFNRSPFD | NGPREEDEEG | ADEFPPEDIR | PTGAANQGFP | NNYALGRRTS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VSAESLNPTS | AGSDSWTPPY | HEKTEEQLSR | LKTAVSSNFL | FSHLDDDQFK | SVLDALVEKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IPAKGIKVIS | QGDAGDYFYI | VENGHFDFMI | HPSGSVQPGP | DGMGNKVGSV | GPGGSFGELA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LMYNAPRAAT | VVSVDPKSTL | WALDRITFRR | ILMDSAFQRR | RMYEAFLEEV | PLLSSLKPYE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RAKIADALDA | IKYPAGSTII | AEGDPGDAFY | LLESGEADAF | KNGVEGPVKS | YKRGDYFGEL |
| 370 | 380 | 390 | 400 | 410 | |
| ALLDDKPRAA | SIVAKTDVKV | AKLGRDGFKR | LLGPVEDIMR | RAEYESNPVP | A |