Q5REL1
Gene name |
PRKAR1A |
Protein name |
cAMP-dependent protein kinase type I-alpha regulatory subunit |
Names |
|
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100171685 |
EC number |
|
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
137-253 (Cyclic nucleotide-binding domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5REL1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5REL1-F1 | Predicted | AlphaFoldDB |
No variants for Q5REL1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5REL1 | |||||
No associated diseases with Q5REL1
7 regional properties for Q5REL1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cyclic nucleotide-binding domain | 137 - 253 | IPR000595-1 |
| domain | Cyclic nucleotide-binding domain | 255 - 376 | IPR000595-2 |
| domain | cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain | 25 - 62 | IPR003117 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 164 - 180 | IPR018488-1 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 200 - 217 | IPR018488-2 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 282 - 298 | IPR018488-3 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 324 - 341 | IPR018488-4 |
2 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
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 |
| MESGSTAASE | EARSLRECEL | YVQKHNIQAL | LKDSIVQLCT | ARPERPMAFL | REYFERLEKE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EAKQIQNLQK | AGTRTDSRED | EISPPPPNPV | VKGRRRRGAI | SAEVYTEEDA | ASYVRKVIPK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DYKTMAALAK | AIEKNVLFSH | LDDNERSDIF | DAMFSVSFIA | GETVIQQGDE | GDNFYVIDQG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ETDVYVNNEW | ATSVGEGGSF | GELALIYGTP | RAATVKAKTN | VKLWGIDRDS | YRRILMGSTL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RKRKMYEEFL | SKVSILESLD | KWERLTVADA | LEPVQFEDGQ | KIVVQGEPGD | EFFIILEGSA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AVLQRRSENE | EFVEVGRLGP | SDYFGEIALL | MNRPRAATVV | ARGPLKCVKL | DRPRFERVLG |
| 370 | 380 | ||||
| PCSDILKRNI | QQYNSFVSLS | V |