Q5REL1 · KAP0_PONAB
- ProteincAMP-dependent protein kinase type I-alpha regulatory subunit
- GenePRKAR1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids381 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 137-254 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: LFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVS | ||||||
Binding site | 202 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 211 | 3',5'-cyclic AMP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 255-381 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: ILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV | ||||||
Binding site | 326 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 335 | 3',5'-cyclic AMP 2 (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cAMP-dependent protein kinase complex | |
Cellular Component | plasma membrane | |
Molecular Function | cAMP binding | |
Molecular Function | cAMP-dependent protein kinase regulator activity | |
Biological Process | regulation of protein phosphorylation |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended namecAMP-dependent protein kinase type I-alpha regulatory subunit
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo
Accessions
- Primary accessionQ5REL1
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000293482 | 1-381 | cAMP-dependent protein kinase type I-alpha regulatory subunit | |||
Sequence: MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV | ||||||
Modified residue | 3 | Phosphoserine | ||||
Sequence: S | ||||||
Disulfide bond | 18 | Interchain (with C-39) | ||||
Sequence: C | ||||||
Disulfide bond | 39 | Interchain (with C-18) | ||||
Sequence: C | ||||||
Modified residue | 75 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 77 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 83 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 101 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 258 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.
Keywords
- PTM
Interaction
Subunit
The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. Interacts with PRKACA and PRKACB (By similarity).
PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with CBFA2T3. Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity).
Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA (By similarity).
PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with CBFA2T3. Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity).
Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-135 | Dimerization and phosphorylation | ||||
Sequence: MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKN | ||||||
Region | 64-96 | Disordered | ||||
Sequence: QIQNLQKAGTRTDSREDEISPPPPNPVVKGRRR | ||||||
Motif | 96-100 | Pseudophosphorylation motif | ||||
Sequence: RRGAI |
Sequence similarities
Belongs to the cAMP-dependent kinase regulatory chain family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length381
- Mass (Da)42,982
- Last updated2007-07-10 v2
- Checksum2D04F08CE8857A6D
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5TD21 | A0A8I5TD21_PONAB | PRKAR1A | 427 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; CAH93424 | ||||
Sequence: A → V | ||||||
Sequence conflict | 77 | in Ref. 1; CAH89796 | ||||
Sequence: S → P | ||||||
Sequence conflict | 89 | in Ref. 1; CAH93424 | ||||
Sequence: P → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR857513 EMBL· GenBank· DDBJ | CAH89796.1 EMBL· GenBank· DDBJ | mRNA | ||
CR860291 EMBL· GenBank· DDBJ | CAH92431.1 EMBL· GenBank· DDBJ | mRNA | ||
CR861364 EMBL· GenBank· DDBJ | CAH93424.1 EMBL· GenBank· DDBJ | mRNA |