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UniProtKB - P17612 (KAPCA_HUMAN)

Entry version 238 (29 Sep 2021)
Sequence version 2 (23 Jan 2007)
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Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

PRKACA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Phosphorylates a large number of substrates in the cytoplasm and the nucleus (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984).

Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984).

Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis (PubMed:21423175).

RORA is activated by phosphorylation (PubMed:21514275).

Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (PubMed:19949837).

Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity).

Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP (PubMed:15642694, PubMed:20356841).

Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated (PubMed:17333334).

RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca2+, leading to reduced amplitude and increased frequency of store overload-induced Ca2+ release (SOICR) characterized by an increased rate of Ca2+ release and propagation velocity of spontaneous Ca2+ waves, despite reduced wave amplitude and resting cytosolic Ca2+ (PubMed:17693412).

PSMC5/RPT6 activation by phosphorylation stimulates proteasome (PubMed:17565987).

Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation (PubMed:15905176).

NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding (PubMed:15642694).

Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity).

May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity).

Phosphorylates APOBEC3G and AICDA (PubMed:16387847, PubMed:18836454).

Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490).

By similarity13 Publications

Phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically activated by various compounds, including ATP. Activated by cAMP; the nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of apo PKA, enhancing the enzyme dynamics synchronously and priming it for catalysis. Inhibited by H89 (N-[2-[[3-(4-Bromophenyl)-2-propenyl]amino]ethyl]-5-isoquinolinesulfonamide), spiroindoline, azole-based inhibitors, (3s)-amino-aminomethylbenzamide analogs, ARC-1032 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-carbamoylbutyl]hexanamide), ARC-1034 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]hexanamide), ARC-582, ARC-902 (Adc-6-aminohexanoic acid-(D-Arg)6-NH2), ARC-1012 ((2R)-6-amino-2-(6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}hexanamido)-N-(5-{[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)hexanamide) and ARC-1039 (6-{[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]formamido}-N-[(1R)-1-[(5-{[(1R)-4-carbamimidamido-1-{[(1R)-4-carbamimidamido-1-carbamoylbutyl]carbamoyl}butyl]carbamoyl}pentyl)carbamoyl]ethyl]he xanamide).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei73ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei167Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi50 – 58ATP9
Nucleotide bindingi122 – 128ATPPROSITE-ProRule annotation7
Nucleotide bindingi169 – 172ATPPROSITE-ProRule annotation4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.11, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P17612

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-111931, PKA-mediated phosphorylation of CREB
R-HSA-163358, PKA-mediated phosphorylation of key metabolic factors
R-HSA-163560, Triglyceride catabolism
R-HSA-163615, PKA activation
R-HSA-164378, PKA activation in glucagon signalling
R-HSA-180024, DARPP-32 events
R-HSA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-HSA-380259, Loss of Nlp from mitotic centrosomes
R-HSA-380270, Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284, Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320, Recruitment of NuMA to mitotic centrosomes
R-HSA-381676, Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-HSA-392517, Rap1 signalling
R-HSA-422356, Regulation of insulin secretion
R-HSA-432040, Vasopressin regulates renal water homeostasis via Aquaporins
R-HSA-4420097, VEGFA-VEGFR2 Pathway
R-HSA-442720, CREB1 phosphorylation through the activation of Adenylate Cyclase
R-HSA-512988, Interleukin-3, Interleukin-5 and GM-CSF signaling
R-HSA-5578775, Ion homeostasis
R-HSA-5610780, Degradation of GLI1 by the proteasome
R-HSA-5610783, Degradation of GLI2 by the proteasome
R-HSA-5610785, GLI3 is processed to GLI3R by the proteasome
R-HSA-5610787, Hedgehog 'off' state
R-HSA-5620912, Anchoring of the basal body to the plasma membrane
R-HSA-5621575, CD209 (DC-SIGN) signaling
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-8853659, RET signaling
R-HSA-8854518, AURKA Activation by TPX2
R-HSA-8963896, HDL assembly
R-HSA-9010642, ROBO receptors bind AKAP5
R-HSA-9022535, Loss of phosphorylation of MECP2 at T308
R-HSA-9022692, Regulation of MECP2 expression and activity
R-HSA-9634600, Regulation of glycolysis by fructose 2,6-bisphosphate metabolism
R-HSA-9660821, ADORA2B mediated anti-inflammatory cytokines production
R-HSA-9664323, FCGR3A-mediated IL10 synthesis
R-HSA-983231, Factors involved in megakaryocyte development and platelet production

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P17612

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P17612

SIGNOR Signaling Network Open Resource

More...SIGNORi		P17612

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit alpha (EC:2.7.11.11)
Short name:
PKA C-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PRKACA
Synonyms:PKACA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9380, PRKACA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601639, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P17612

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000072062

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoplasmic vesicle, Flagellum, Membrane, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Primary pigmented nodular adrenocortical disease 4 (PPNAD4)4 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071707206L → R in PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A. 4 PublicationsCorresponds to variant dbSNP:rs386352352EnsemblClinVar.1
Cardioacrofacial dysplasia 1 (CAFD1)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by dysmorphic facial features, congenital cardiac defects, primarily common atrium or atrioventricular septal defect, and limb anomalies, including short limbs, brachydactyly and postaxial polydactyly.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_085198137G → R in CAFD1; decreased interaction with regulatory subunit PRKAR2B. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi48K → R: Enhanced basal kinase activity; when associated with Q-96, L-121, A-124, K-182 and A-184. 1 Publication1
Mutagenesisi96L → Q: Enhanced basal kinase activity; when associated with R-48, L-121, A-124, K-182 and A-184. 1 Publication1
Mutagenesisi121M → L: Enhanced basal kinase activity; when associated with R-48, Q-96, A-124, K-182 and A-184. 1 Publication1
Mutagenesisi124V → A: Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, K-182 and A-184. 1 Publication1
Mutagenesisi182Q → K: Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, A-124 and A-184. 1 Publication1
Mutagenesisi184T → A: Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, A-124 and K-182. 1 Publication1
Mutagenesisi195R → A: No phosphorylation. 1 Publication1
Mutagenesisi201G → A: No phosphorylation. 1 Publication1
Mutagenesisi202T → A: No phosphorylation. 1 Publication1
Mutagenesisi205Y → A: Loss of allosteric regulation. 1 Publication1

Keywords - Diseasei

Cushing syndrome, Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		5566

MalaCards human disease database

More...MalaCardsi		PRKACA
MIMi615830, phenotype
619142, phenotype

Open Targets

More...OpenTargetsi		ENSG00000072062

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		401920, Fibrolamellar hepatocellular carcinoma
189439, Primary pigmented nodular adrenocortical disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33748

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P17612, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4101

Drug and drug target database

More...DrugBanki		DB07204, (1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINE
DB07107, (1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE
DB07857, (2R)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine
DB07860, (2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINE
DB08073, (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
DB06959, (2S)-1-(3H-Indol-3-yl)-3-{[5-(6-isoquinolinyl)-3-pyridinyl]oxy}-2-propanamine
DB07124, (2S)-1-(6H-INDOL-3-YL)-3-{[5-(7H-PYRAZOLO[3,4-C]PYRIDIN-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
DB06977, (2S)-1-{[5-(1H-Indazol-5-yl)-3-pyridinyl]oxy}-3-(7aH-indol-3-yl)-2-propanamine
DB07858, (2S)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine
DB07583, (4R,2S)-5'-(4-(4-CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)ISOQUINOLINE
DB07855, (S)-1-PHENYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB07876, (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE
DB08149, 1-[4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-yl]methanamine
DB08148, 1-[4-(4-chlorophenyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-yl]methanamine
DB08070, 2-[4-(3-METHYL-1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE
DB03374, 3,5-Diiodotyrosine
DB07458, 3-(1H-indol-3-yl)-4-{1-[2-(1-methylpyrrolidin-2-yl)ethyl]-1H-indol-3-yl}-1H-pyrrole-2,5-dione
DB02155, 3-[(3-sec-butyl-4-hydroxybenzoyl)amino]azepan-4-yl 4-(2-hydroxy-5-methoxybenzoyl)benzoate
DB08113, 3-pyridin-4-yl-1H-indazole
DB08569, 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.] PYRAZOLE
DB08150, 4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium
DB07859, 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE
DB07996, 5-(2-methylpiperazine-1-sulfonyl)isoquinoline
DB08114, 5-benzyl-1,3-thiazol-2-amine
DB07856, 6-{4-[4-(4-CHLOROPHENYL)PIPERIDIN-4-YL]PHENYL}-9H-PURINE
DB08568, A-674563
DB04098, Balanol
DB02611, Balanol Analog 1
DB01940, Balanol Analog 2
DB04522, Dexfosfoserine
DB08846, Ellagic acid
DB08162, Fasudil
DB12010, Fostamatinib
DB07995, H-89
DB04707, Hydroxyfasudil
DB07947, ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE
DB08231, Myristic acid
DB07235, N-[(1S)-2-AMINO-1-(2,4-DICHLOROBENZYL)ETHYL]-5-[2-(METHYLAMINO)PYRIMIDIN-4-YL]THIOPHENE-2-CARBOXAMIDE
DB07997, N-[2-(METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE
DB07854, N-METHYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB01919, Pentanal
DB02482, Phosphonothreonine
DB04530, S,S-(2-Hydroxyethyl)Thiocysteine
DB08756, Y-27632

DrugCentral

More...DrugCentrali		P17612

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1476

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PRKACA

Domain mapping of disease mutations (DMDM)

More...DMDMi		125205

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000860522 – 351cAMP-dependent protein kinase catalytic subunit alphaAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine2 Publications1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3Deamidated asparagineBy similarity1
Modified residuei11Phosphoserine; by autocatalysisBy similarity1
Modified residuei49PhosphothreonineCombined sources1
Modified residuei140PhosphoserineBy similarity1
Modified residuei196Phosphothreonine1 Publication1
Modified residuei198Phosphothreonine; by PDPK17 Publications1
Modified residuei331PhosphotyrosineBy similarity1
Modified residuei339PhosphoserineCombined sources6 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Asn-3 is partially deaminated to Asp giving rise to 2 major isoelectric variants, called CB and CA respectively.By similarity
Autophosphorylated. Phosphorylation is enhanced by vitamin K2. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity.8 Publications
Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficiency.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P17612

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P17612

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P17612

MaxQB - The MaxQuant DataBase

More...MaxQBi		P17612

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P17612

PeptideAtlas

More...PeptideAtlasi		P17612

PRoteomics IDEntifications database

More...PRIDEi		P17612

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53496 [P17612-1]
53497 [P17612-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P17612, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17612

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P17612

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P17612

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 is ubiquitous. Isoform 2 is sperm-specific and is enriched in pachytene spermatocytes but is not detected in round spermatids.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000072062, Expressed in heart and 241 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P17612, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P17612, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000072062, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

A number of inactive tetrameric holoenzymes are produced by the combination of homo- or heterodimers of the different regulatory subunits associated with two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. The cAMP-dependent protein kinase catalytic subunit binds PJA2. Both isoforms 1 and 2 forms activate cAMP-sensitive PKAI and PKAII holoenzymes by interacting with regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2, respectively.

Interacts with PRKAR1A and PRKAR2B (PubMed:33058759).

Interacts with NFKB1, NFKB2 and NFKBIA in platelets; these interactions are disrupted by thrombin and collagen. Binds to ABL1 in spermatozoa and with CDC25B in oocytes.

Interacts with APOBEC3G and AICDA.

Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly.

Found in a complex at least composed of MROH2B, PRKACA isoform 2 and TCP11 (By similarity).

Interacts with MROH2B (By similarity).

Isoform 2 interacts with TCP11 (By similarity).

Interacts with HSF1 (PubMed:21085490).

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P17612
With#Exp.IntAct
AICDA [Q9GZX7]3EBI-476586,EBI-3834328
AK2 [P54819]3EBI-476586,EBI-1056291
AKIP1 [Q9NQ31]4EBI-476586,EBI-517035
AKT1 [P31749]3EBI-476586,EBI-296087
ALOX5 [P09917]2EBI-476586,EBI-79934
APBB2 - isoform 2 [Q92870-2]3EBI-476586,EBI-21535880
APOBEC3G [Q9HC16]6EBI-476586,EBI-717839
APP [P05067]3EBI-476586,EBI-77613
ATXN1 [P54253]3EBI-476586,EBI-930964
ATXN3 [P54252]3EBI-476586,EBI-946046
ATXN3 [Q4VBR4]3EBI-476586,EBI-12928880
AVPI1 [Q5T686]3EBI-476586,EBI-8640233
BDNF - isoform 2 [P23560-2]3EBI-476586,EBI-12275524
CBSL [P0DN79]3EBI-476586,EBI-14245939
CCT6A [P40227]3EBI-476586,EBI-356687
CDH1 [P12830]3EBI-476586,EBI-727477
COL25A1 [Q8NE08]3EBI-476586,EBI-25836642
CSNK1D - isoform 2 [P48730-2]3EBI-476586,EBI-9087876
DPYSL4 [O14531]3EBI-476586,EBI-719542
ELAVL4 - isoform 2 [P26378-2]3EBI-476586,EBI-21603100
ETS2 [P15036]3EBI-476586,EBI-1646991
FAM104A [Q969W3]3EBI-476586,EBI-10281506
GAPDH [P04406]3EBI-476586,EBI-354056
GSK3B [P49841]7EBI-476586,EBI-373586
HSP90AA1 [P07900]4EBI-476586,EBI-296047
HTT [P42858]3EBI-476586,EBI-466029
IDH1 [O75874]3EBI-476586,EBI-715695
ITGAV [P06756]3EBI-476586,EBI-298282
KEL [P23276]3EBI-476586,EBI-746662
LRRK2 [Q5S007]6EBI-476586,EBI-5323863
MAPK8IP2 - isoform 4 [Q13387-4]3EBI-476586,EBI-12345753
PCSK7 [Q16549]3EBI-476586,EBI-8059854
PIK3R1 - isoform 2 [P27986-2]3EBI-476586,EBI-9090282
PKIB - isoform 2 [Q9C010-2]3EBI-476586,EBI-12886396
PLPP1 [O14494]3EBI-476586,EBI-2865290
PNP [P00491]3EBI-476586,EBI-712238
PRKAR1A [P10644]12EBI-476586,EBI-476431
PRKAR1B [P31321]7EBI-476586,EBI-2805516
PRKAR2B [P31323]14EBI-476586,EBI-2930670
PSMD2 [Q13200]3EBI-476586,EBI-357648
PTN [P21246]3EBI-476586,EBI-473725
RHBDD2 - isoform 3 [Q6NTF9-3]3EBI-476586,EBI-17589229
RPL37A [P61513]3EBI-476586,EBI-356793
S100B [P04271]3EBI-476586,EBI-458391
SIGMAR1 - isoform 4 [Q99720-4]3EBI-476586,EBI-25831036
SMAD3 [P84022]3EBI-476586,EBI-347161
SNRNP35 - isoform 2 [Q16560-2]3EBI-476586,EBI-12938570
SP6 [Q3SY56]3EBI-476586,EBI-11175533
STUB1 [Q9UNE7]3EBI-476586,EBI-357085
TOM1 - isoform 2 [O60784-2]3EBI-476586,EBI-12117154
TRAF3IP3 [Q9Y228]3EBI-476586,EBI-765817
USP25 [Q9UHP3]3EBI-476586,EBI-2513462
VPS29 - isoform 2 [Q9UBQ0-2]3EBI-476586,EBI-11141397
Gnao1 [P59215] from Rattus norvegicus.4EBI-476586,EBI-8071125
Prkar2b [P12369] from Rattus norvegicus.2EBI-476586,EBI-6096160

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111553, 274 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P17612

Database of interacting proteins

More...DIPi		DIP-33878N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P17612

Protein interaction database and analysis system

More...IntActi		P17612, 147 interactors

Molecular INTeraction database

More...MINTi		P17612

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000309591

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P17612

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P17612, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P17612

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P17612

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P17612

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini44 – 298Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini299 – 351AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST53

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0616, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162186

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17612

Identification of Orthologs from Complete Genome Data

More...OMAi		WWACGIL

Database of Orthologous Groups

More...OrthoDBi		963519at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P17612

TreeFam database of animal gene trees

More...TreeFami		TF313399

Family and domain databases

Conserved Domains Database

More...CDDi		cd14209, STKc_PKA, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00366

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000961, AGC-kinase_C
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
IPR044109, STKc_PKA

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00133, S_TK_X, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P17612-1) [UniParc]FASTAAdd to basket
Also known as: C-alpha-1

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL 
        60         70         80         90        100
GTGSFGRVML VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN 
       110        120        130        140        150
FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ 
       160        170        180        190        200
IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC 
       210        220        230        240        250
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK 
       260        270        280        290        300
IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT 
       310        320        330        340        350
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE 

F
Length:351
Mass (Da):40,590
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBF6D3ECD2614E5AB
GO
Isoform 2 (identifier: P17612-2) [UniParc]FASTAAdd to basket
Also known as: C-alpha-2, C-alpha-S, C(s)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGNAAAAKKGSEQES → MASNSSD

Show »
Length:343
Mass (Da):39,822
Checksum:i5AD33AECC261EA16
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A7I2V5J4A0A7I2V5J4_HUMAN
cAMP-dependent protein kinase
PRKACA
293Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q15136Q15136_HUMAN
Protein kinase A-alpha
PRKACA KIN27
207Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ERP6K7ERP6_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
251Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B7Z708B7Z708_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
230Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A7I2YQ82A0A7I2YQ82_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
134Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ENJ5K7ENJ5_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
124Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EMV1K7EMV1_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
25Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04059141L → V1 PublicationCorresponds to variant dbSNP:rs56029020Ensembl.1
Natural variantiVAR_04059246R → Q1 PublicationCorresponds to variant dbSNP:rs56085217Ensembl.1
Natural variantiVAR_085198137G → R in CAFD1; decreased interaction with regulatory subunit PRKAR2B. 1 Publication1
Natural variantiVAR_071707206L → R in PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A. 4 PublicationsCorresponds to variant dbSNP:rs386352352EnsemblClinVar.1
Natural variantiVAR_040593264S → C1 PublicationCorresponds to variant dbSNP:rs35635531Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0047591 – 15MGNAA…SEQES → MASNSSD in isoform 2. 3 PublicationsAdd BLAST15

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X07767 mRNA Translation: CAA30597.1
AK290147 mRNA Translation: BAF82836.1
DQ667173 Genomic DNA Translation: ABG25918.1
CH471106 Genomic DNA Translation: EAW84399.1
BC039846 mRNA Translation: AAH39846.1
BC108259 mRNA Translation: AAI08260.1
AF208004 mRNA Translation: AAG35720.1
AF239744 mRNA Translation: AAF76426.1
AF224718 mRNA Translation: AAF75622.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12304.1 [P17612-1]
CCDS12305.1 [P17612-2]

Protein sequence database of the Protein Information Resource

More...PIRi		S01404, OKHU2C

NCBI Reference Sequences

More...RefSeqi		NP_001291278.1, NM_001304349.1
NP_002721.1, NM_002730.3 [P17612-1]
NP_997401.1, NM_207518.2 [P17612-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000308677; ENSP00000309591; ENSG00000072062 [P17612-1]
ENST00000589994; ENSP00000466651; ENSG00000072062 [P17612-2]
ENST00000672938; ENSP00000500293; ENSG00000288516 [P17612-2]
ENST00000673550; ENSP00000499940; ENSG00000288516 [P17612-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5566

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5566

UCSC genome browser

More...UCSCi		uc002myb.4, human [P17612-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07767 mRNA Translation: CAA30597.1
AK290147 mRNA Translation: BAF82836.1
DQ667173 Genomic DNA Translation: ABG25918.1
CH471106 Genomic DNA Translation: EAW84399.1
BC039846 mRNA Translation: AAH39846.1
BC108259 mRNA Translation: AAI08260.1
AF208004 mRNA Translation: AAG35720.1
AF239744 mRNA Translation: AAF76426.1
AF224718 mRNA Translation: AAF75622.1
CCDSiCCDS12304.1 [P17612-1]
CCDS12305.1 [P17612-2]
PIRiS01404, OKHU2C
RefSeqiNP_001291278.1, NM_001304349.1
NP_002721.1, NM_002730.3 [P17612-1]
NP_997401.1, NM_207518.2 [P17612-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GU8X-ray2.20A15-351[»]
3AGLX-ray2.10A/B1-351[»]
3AGMX-ray2.00A1-351[»]
3AMAX-ray1.75A1-351[»]
3AMBX-ray2.25A1-351[»]
3L9LX-ray2.00A/B1-351[»]
3L9MX-ray1.90A/B1-351[»]
3L9NX-ray2.00A1-351[»]
3MVJX-ray2.49A/B/E1-351[»]
3NX8X-ray2.00A1-351[»]
3OOGX-ray2.00A1-351[»]
3OVVX-ray1.58A1-351[»]
3OWPX-ray1.88A1-351[»]
3OXTX-ray2.20A1-351[»]
3P0MX-ray2.03A1-351[»]
3POOX-ray1.60A1-351[»]
3VQHX-ray1.95A1-351[»]
4AE6X-ray2.10A/B16-351[»]
4AE9X-ray2.30A/B16-351[»]
4UJ1X-ray1.77A1-351[»]
4UJ2X-ray2.02A1-351[»]
4UJ9X-ray1.87A1-351[»]
4UJAX-ray1.93A1-351[»]
4UJBX-ray1.95A1-351[»]
4WB5X-ray1.64A2-351[»]
4WB6X-ray2.10A/B2-351[»]
4WB7X-ray1.90A/B16-351[»]
4WB8X-ray1.55A16-351[»]
5BX6X-ray1.89A1-351[»]
5BX7X-ray1.89A1-350[»]
5IZFX-ray2.10A1-351[»]
5IZJX-ray1.85A/B1-351[»]
5J5XX-ray2.60A1-351[»]
5N23X-ray2.09A1-351[»]
5UZKX-ray2.30A1-351[»]
6BYRX-ray3.66A/C16-351[»]
6BYSX-ray4.75A/C/E/G2-351[»]
6C0UX-ray2.65A1-351[»]
6FRXX-ray1.88A1-351[»]
6NO7X-ray3.55A/C/E/G2-351[»]
6QJ7X-ray1.69A1-351[»]
6WJFelectron microscopy7.50A/B16-351[»]
6WJGelectron microscopy6.20A/B16-351[»]
BMRBiP17612
SMRiP17612
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111553, 274 interactors
CORUMiP17612
DIPiDIP-33878N
ELMiP17612
IntActiP17612, 147 interactors
MINTiP17612
STRINGi9606.ENSP00000309591

Chemistry databases

BindingDBiP17612
ChEMBLiCHEMBL4101
DrugBankiDB07204, (1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINE
DB07107, (1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE
DB07857, (2R)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine
DB07860, (2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINE
DB08073, (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
DB06959, (2S)-1-(3H-Indol-3-yl)-3-{[5-(6-isoquinolinyl)-3-pyridinyl]oxy}-2-propanamine
DB07124, (2S)-1-(6H-INDOL-3-YL)-3-{[5-(7H-PYRAZOLO[3,4-C]PYRIDIN-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
DB06977, (2S)-1-{[5-(1H-Indazol-5-yl)-3-pyridinyl]oxy}-3-(7aH-indol-3-yl)-2-propanamine
DB07858, (2S)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine
DB07583, (4R,2S)-5'-(4-(4-CHLOROBENZYLOXY)PYRROLIDIN-2-YLMETHANESULFONYL)ISOQUINOLINE
DB07855, (S)-1-PHENYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB07876, (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE
DB08149, 1-[4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-yl]methanamine
DB08148, 1-[4-(4-chlorophenyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-yl]methanamine
DB08070, 2-[4-(3-METHYL-1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE
DB03374, 3,5-Diiodotyrosine
DB07458, 3-(1H-indol-3-yl)-4-{1-[2-(1-methylpyrrolidin-2-yl)ethyl]-1H-indol-3-yl}-1H-pyrrole-2,5-dione
DB02155, 3-[(3-sec-butyl-4-hydroxybenzoyl)amino]azepan-4-yl 4-(2-hydroxy-5-methoxybenzoyl)benzoate
DB08113, 3-pyridin-4-yl-1H-indazole
DB08569, 3-PYRIDIN-4-YL-2,4-DIHYDRO-INDENO[1,2-.C.] PYRAZOLE
DB08150, 4-(4-chlorobenzyl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperidin-4-aminium
DB07859, 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE
DB07996, 5-(2-methylpiperazine-1-sulfonyl)isoquinoline
DB08114, 5-benzyl-1,3-thiazol-2-amine
DB07856, 6-{4-[4-(4-CHLOROPHENYL)PIPERIDIN-4-YL]PHENYL}-9H-PURINE
DB08568, A-674563
DB04098, Balanol
DB02611, Balanol Analog 1
DB01940, Balanol Analog 2
DB04522, Dexfosfoserine
DB08846, Ellagic acid
DB08162, Fasudil
DB12010, Fostamatinib
DB07995, H-89
DB04707, Hydroxyfasudil
DB07947, ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE
DB08231, Myristic acid
DB07235, N-[(1S)-2-AMINO-1-(2,4-DICHLOROBENZYL)ETHYL]-5-[2-(METHYLAMINO)PYRIMIDIN-4-YL]THIOPHENE-2-CARBOXAMIDE
DB07997, N-[2-(METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE
DB07854, N-METHYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB01919, Pentanal
DB02482, Phosphonothreonine
DB04530, S,S-(2-Hydroxyethyl)Thiocysteine
DB08756, Y-27632
DrugCentraliP17612
GuidetoPHARMACOLOGYi1476

PTM databases

GlyGeniP17612, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP17612
PhosphoSitePlusiP17612
SwissPalmiP17612

Genetic variation databases

BioMutaiPRKACA
DMDMi125205

Proteomic databases

EPDiP17612
jPOSTiP17612
MassIVEiP17612
MaxQBiP17612
PaxDbiP17612
PeptideAtlasiP17612
PRIDEiP17612
ProteomicsDBi53496 [P17612-1]
53497 [P17612-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		4159, 518 antibodies

The DNASU plasmid repository

More...DNASUi		5566

Genome annotation databases

EnsembliENST00000308677; ENSP00000309591; ENSG00000072062 [P17612-1]
ENST00000589994; ENSP00000466651; ENSG00000072062 [P17612-2]
ENST00000672938; ENSP00000500293; ENSG00000288516 [P17612-2]
ENST00000673550; ENSP00000499940; ENSG00000288516 [P17612-1]
GeneIDi5566
KEGGihsa:5566
UCSCiuc002myb.4, human [P17612-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5566
DisGeNETi5566

GeneCards: human genes, protein and diseases

More...GeneCardsi		PRKACA
HGNCiHGNC:9380, PRKACA
HPAiENSG00000072062, Low tissue specificity
MalaCardsiPRKACA
MIMi601639, gene
615830, phenotype
619142, phenotype
neXtProtiNX_P17612
OpenTargetsiENSG00000072062
Orphaneti401920, Fibrolamellar hepatocellular carcinoma
189439, Primary pigmented nodular adrenocortical disease
PharmGKBiPA33748
VEuPathDBiHostDB:ENSG00000072062

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0616, Eukaryota
GeneTreeiENSGT00940000162186
InParanoidiP17612
OMAiWWACGIL
OrthoDBi963519at2759
PhylomeDBiP17612
TreeFamiTF313399

Enzyme and pathway databases

BRENDAi2.7.11.11, 2681
PathwayCommonsiP17612
ReactomeiR-HSA-111931, PKA-mediated phosphorylation of CREB
R-HSA-163358, PKA-mediated phosphorylation of key metabolic factors
R-HSA-163560, Triglyceride catabolism
R-HSA-163615, PKA activation
R-HSA-164378, PKA activation in glucagon signalling
R-HSA-180024, DARPP-32 events
R-HSA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-HSA-380259, Loss of Nlp from mitotic centrosomes
R-HSA-380270, Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284, Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320, Recruitment of NuMA to mitotic centrosomes
R-HSA-381676, Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-HSA-392517, Rap1 signalling
R-HSA-422356, Regulation of insulin secretion
R-HSA-432040, Vasopressin regulates renal water homeostasis via Aquaporins
R-HSA-4420097, VEGFA-VEGFR2 Pathway
R-HSA-442720, CREB1 phosphorylation through the activation of Adenylate Cyclase
R-HSA-512988, Interleukin-3, Interleukin-5 and GM-CSF signaling
R-HSA-5578775, Ion homeostasis
R-HSA-5610780, Degradation of GLI1 by the proteasome
R-HSA-5610783, Degradation of GLI2 by the proteasome
R-HSA-5610785, GLI3 is processed to GLI3R by the proteasome
R-HSA-5610787, Hedgehog 'off' state
R-HSA-5620912, Anchoring of the basal body to the plasma membrane
R-HSA-5621575, CD209 (DC-SIGN) signaling
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-8853659, RET signaling
R-HSA-8854518, AURKA Activation by TPX2
R-HSA-8963896, HDL assembly
R-HSA-9010642, ROBO receptors bind AKAP5
R-HSA-9022535, Loss of phosphorylation of MECP2 at T308
R-HSA-9022692, Regulation of MECP2 expression and activity
R-HSA-9634600, Regulation of glycolysis by fructose 2,6-bisphosphate metabolism
R-HSA-9660821, ADORA2B mediated anti-inflammatory cytokines production
R-HSA-9664323, FCGR3A-mediated IL10 synthesis
R-HSA-983231, Factors involved in megakaryocyte development and platelet production
SABIO-RKiP17612
SignaLinkiP17612
SIGNORiP17612

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5566, 34 hits in 1055 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PRKACA, human
EvolutionaryTraceiP17612

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PRKACA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5566
PharosiP17612, Tchem

Protein Ontology

More...PROi		PR:P17612
RNActiP17612, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000072062, Expressed in heart and 241 other tissues
ExpressionAtlasiP17612, baseline and differential
GenevisibleiP17612, HS

Family and domain databases

CDDicd14209, STKc_PKA, 1 hit
IDEALiIID00366
InterProiView protein in InterPro
IPR000961, AGC-kinase_C
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS
IPR044109, STKc_PKA
PfamiView protein in Pfam
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM00133, S_TK_X, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285, AGC_KINASE_CTER, 1 hit
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKAPCA_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P17612
Secondary accession number(s): Q32P54
, Q9H2Y0, Q9NRB4, Q9NRH9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 238 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human entries with genetic variants
    List of human entries with genetic variants
  5. Human variants curated from literature reports
    Index of human variants curated from literature reports
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families
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