Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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. 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. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. 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. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. 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+. PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. 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. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490).13 Publications

<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 ‘Function’ 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 ‘Function’ 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 ‘Function’ 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 ‘Function’ 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

GO - Biological processi

<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

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 CREB 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-70171 Glycolysis
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-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000072062.13

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

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 mutations 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.
See also OMIM:615830
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

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 mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
5566

MalaCards human disease database

More...
MalaCardsi
PRKACA
MIMi615830 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4101

Drug and drug target database

More...
DrugBanki
DB07107 (1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE
DB06959 (1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-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
DB06977 (2S)-1-{[5-(1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}-3-[(7AS)-7AH-INDOL-3-YL]PROPAN-2-AMINE
DB08568 (2S)-1-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}-3-PHENYLPROPAN-2-AMINE
DB07858 (2S)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE
DB08756 (R)-TRANS-4-(1-AMINOETHYL)-N-(4-PYRIDYL) CYCLOHEXANECARBOXAMIDE
DB07855 (S)-1-PHENYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB07876 (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE
DB08070 2-[4-(3-METHYL-1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE
DB08113 3-pyridin-4-yl-1H-indazole
DB07859 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE
DB07996 5-(2-methylpiperazine-1-sulfonyl)isoquinoline
DB07856 6-{4-[4-(4-CHLOROPHENYL)PIPERIDIN-4-YL]PHENYL}-9H-PURINE
DB04098 Balanol
DB02611 Balanol Analog 1
DB01940 Balanol Analog 2
DB02155 Balanol Analog 8
DB08846 Ellagic Acid
DB04707 HYDROXYFASUDIL
DB07947 ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE
DB08231 MYRISTIC ACID
DB07995 N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE SULFONAMIDE
DB07997 N-[2-(METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE
DB07854 N-METHYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB01919 Pentanal
DB04522 Phosphonoserine
DB02482 Phosphonothreonine

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1476

Polymorphism and mutation 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.<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 efficienncy.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

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 human proteome resource

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

PTM databases

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 227 organ(s), highest expression level in muscle of leg

CleanEx database of gene expression profiles

More...
CleanExi
HS_PRKACA

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
CAB010361
HPA071185

<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 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 similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111553, 158 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, 90 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

<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

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[»]
6C0UX-ray2.65A1-351[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P17612

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

More...
SMRi
P17612

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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-terminalAdd 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0616 Eukaryota
ENOG410XPQQ LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000162186

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233033

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG108317

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17612

KEGG Orthology (KO)

More...
KOi
K04345

Identification of Orthologs from Complete Genome Data

More...
OMAi
HSHDIIY

Database of Orthologous Groups

More...
OrthoDBi
1647595at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P17612

TreeFam database of animal gene trees

More...
TreeFami
TF313399

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR039035 PKA_C-alpha
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR24353:SF82 PTHR24353:SF82, 1 hit

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>.<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 4 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 'canonical' 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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q15136Q15136_HUMAN
Protein kinase A-alpha
PRKACA KIN27
207Annotation 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>
K7ERP6K7ERP6_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
251Annotation 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>
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_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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.631630

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000308677; ENSP00000309591; ENSG00000072062 [P17612-1]
ENST00000589994; ENSP00000466651; ENSG00000072062 [P17612-2]

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, Polymorphism

<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]
UniGeneiHs.631630

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
6C0UX-ray2.65A1-351[»]
ProteinModelPortaliP17612
SMRiP17612
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111553, 158 interactors
CORUMiP17612
DIPiDIP-33878N
ELMiP17612
IntActiP17612, 90 interactors
MINTiP17612
STRINGi9606.ENSP00000309591

Chemistry databases

BindingDBiP17612
ChEMBLiCHEMBL4101
DrugBankiDB07107 (1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE
DB06959 (1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-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
DB06977 (2S)-1-{[5-(1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}-3-[(7AS)-7AH-INDOL-3-YL]PROPAN-2-AMINE
DB08568 (2S)-1-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}-3-PHENYLPROPAN-2-AMINE
DB07858 (2S)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE
DB08756 (R)-TRANS-4-(1-AMINOETHYL)-N-(4-PYRIDYL) CYCLOHEXANECARBOXAMIDE
DB07855 (S)-1-PHENYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB07876 (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE
DB08070 2-[4-(3-METHYL-1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE
DB08113 3-pyridin-4-yl-1H-indazole
DB07859 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE
DB07996 5-(2-methylpiperazine-1-sulfonyl)isoquinoline
DB07856 6-{4-[4-(4-CHLOROPHENYL)PIPERIDIN-4-YL]PHENYL}-9H-PURINE
DB04098 Balanol
DB02611 Balanol Analog 1
DB01940 Balanol Analog 2
DB02155 Balanol Analog 8
DB08846 Ellagic Acid
DB04707 HYDROXYFASUDIL
DB07947 ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE
DB08231 MYRISTIC ACID
DB07995 N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE SULFONAMIDE
DB07997 N-[2-(METHYLAMINO)ETHYL]-5-ISOQUINOLINESULFONAMIDE
DB07854 N-METHYL-1-[4-(9H-PURIN-6-YL)PHENYL]METHANAMINE
DB01919 Pentanal
DB04522 Phosphonoserine
DB02482 Phosphonothreonine
GuidetoPHARMACOLOGYi1476

PTM databases

iPTMnetiP17612
PhosphoSitePlusiP17612
SwissPalmiP17612

Polymorphism and mutation databases

BioMutaiPRKACA
DMDMi125205

Proteomic databases

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

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5566
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308677; ENSP00000309591; ENSG00000072062 [P17612-1]
ENST00000589994; ENSP00000466651; ENSG00000072062 [P17612-2]
GeneIDi5566
KEGGihsa:5566
UCSCiuc002myb.4 human [P17612-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5566
DisGeNETi5566
EuPathDBiHostDB:ENSG00000072062.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PRKACA
HGNCiHGNC:9380 PRKACA
HPAiCAB010361
HPA071185
MalaCardsiPRKACA
MIMi601639 gene
615830 phenotype
neXtProtiNX_P17612
OpenTargetsiENSG00000072062
Orphaneti401920 Fibrolamellar hepatocellular carcinoma
189439 Primary pigmented nodular adrenocortical disease
PharmGKBiPA33748

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0616 Eukaryota
ENOG410XPQQ LUCA
GeneTreeiENSGT00940000162186
HOGENOMiHOG000233033
HOVERGENiHBG108317
InParanoidiP17612
KOiK04345
OMAiHSHDIIY
OrthoDBi1647595at2759
PhylomeDBiP17612
TreeFamiTF313399

Enzyme and pathway databases

BRENDAi2.7.11.11 2681
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 CREB 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-70171 Glycolysis
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-983231 Factors involved in megakaryocyte development and platelet production
SABIO-RKiP17612
SignaLinkiP17612
SIGNORiP17612

Miscellaneous databases

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

Protein Ontology

More...
PROi
PR:P17612

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000072062 Expressed in 227 organ(s), highest expression level in muscle of leg
CleanExiHS_PRKACA
ExpressionAtlasiP17612 baseline and differential
GenevisibleiP17612 HS

Family and domain databases

InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR039035 PKA_C-alpha
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24353:SF82 PTHR24353:SF82, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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: January 16, 2019
This is version 219 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, Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again