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
2 structures for P11141
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3DQG | X-ray | 172 A | A/B/C/D | 418-565 | PDB |
| AF-P11141-F1 | Predicted | AlphaFoldDB |
No variants for P11141
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P11141 | |||||
No associated diseases with P11141
7 regional properties for P11141
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cyclic nucleotide-binding domain | 184 - 300 | IPR000595-1 |
| domain | Cyclic nucleotide-binding domain | 302 - 416 | IPR000595-2 |
| domain | cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain | 7 - 45 | IPR003117 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 211 - 227 | IPR018488-1 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 247 - 264 | IPR018488-2 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 329 - 345 | IPR018488-3 |
| conserved_site | Cyclic nucleotide-binding, conserved site | 366 - 383 | IPR018488-4 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| misfolded protein binding | Binding to a misfolded protein. |
| protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
| unfolded protein binding | Binding to an unfolded protein. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to unfolded protein | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus. |
| chaperone cofactor-dependent protein refolding | The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. |
| mitochondrial unfolded protein response | The series of molecular signals generated as a consequence of the presence of unfolded proteins in the mitochondrial matrix; results in transcriptional upregulation of nuclear genes encoding mitochondrial stress proteins. |
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P77319 | hscC | Chaperone protein HscC | Escherichia coli (strain K12) | PR |
| P0A6Y8 | dnaK | Chaperone protein DnaK | Escherichia coli (strain K12) | SS |
| P38646 | HSPA9 | Stress-70 protein, mitochondrial | Homo sapiens (Human) | SS |
| P09446 | hsp-1 | Heat shock protein hsp-1 | Caenorhabditis elegans | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLSARSFLSS | ARTIARSSLM | SARSLSDKPK | GHVIGIDLGT | TNSCVSIMEG | KTPKVIENAE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GVRTTPSTVA | FTADGERLVG | APAKRQAVTN | SANTLFATKR | LIGRRYEDPE | VQKDLKVVPY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KIVKASNGDA | WVEAQGKVYS | PSQVGAFVLM | KMKETAESYL | GTTVNNAVVT | VPAYFNDSQR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QATKDAGQIS | GLNVLRVINE | PTAAALAYGL | DKDAGDKIIA | VYDLGGGTFD | VSILEIQKGV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FEVKSTNGDT | FLGGEDFDHA | LVHHLVGEFK | KEQGVDLTKD | PQAMQRLREA | AEKAKCELSS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TTQTDINLPY | ITMDQSGPKH | LNLKLTRAKF | EQIVGDLIKR | TIEPCRKALH | DAEVKSSQIA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DVLLVGGMSR | MPKVQATVQE | IFGKVPSKAV | NPDEAVAMGA | AIQGAVLAGD | VTDVLLLDVT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PLSLGIETLG | GIMTKLITRN | TTIPTKKSQV | FSTAADGQTQ | VQIKVFQGER | EMATSNKLLG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QFSLVGIPPA | PRGVPQVEVT | FDIDANGIVN | VSARDRGTGK | EQQIVIQSSG | GLSKDQIENM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IKEAEKNAAE | DAKRKELVEV | INQAEGIIHD | TEAKMTEFAD | QLPKDECEAL | RTKIADTKKI |
| 610 | 620 | 630 | 640 | 650 | |
| LDNKDNETPE | AIKEACNTLQ | QQSLKLFEAA | YKNMAAKNSG | GDAQEAKTAE | EPKKEQN |