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UniProtKB - P17612 (KAPCA_HUMAN)

Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

PRKACA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

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
Binding sitei73ATPPROSITE-ProRule annotation1
Active sitei167Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 58ATP9
Nucleotide bindingi122 – 128ATPPROSITE-ProRule annotation7
Nucleotide bindingi169 – 172ATPPROSITE-ProRule annotation4

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

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

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-983231 Factors involved in megakaryocyte development and platelet production
SABIO-RKiP17612
SignaLinkiP17612
SIGNORiP17612

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit alpha (EC:2.7.11.11)
Short name:
PKA C-alpha
Gene namesi
Name:PRKACA
Synonyms:PKACA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000072062.13
HGNCiHGNC:9380 PRKACA
MIMi601639 gene
neXtProtiNX_P17612

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

Pathology & Biotechi

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
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
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

DisGeNETi5566
MalaCardsiPRKACA
MIMi615830 phenotype
OpenTargetsiENSG00000072062
Orphaneti401920 Fibrolamellar hepatocellular carcinoma
189439 Primary pigmented nodular adrenocortical disease
PharmGKBiPA33748

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiPRKACA
DMDMi125205

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000860522 – 351cAMP-dependent protein kinase catalytic subunit alphaAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine2 Publications1
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

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

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

PTM databases

iPTMnetiP17612
PhosphoSitePlusiP17612
SwissPalmiP17612

Expressioni

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

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

Organism-specific databases

HPAiCAB010361
HPA071185

Interactioni

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

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111553, 158 interactors
CORUMiP17612
DIPiDIP-33878N
ELMiP17612
IntActiP17612, 89 interactors
MINTiP17612
STRINGi9606.ENSP00000309591

Chemistry databases

BindingDBiP17612

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP17612
SMRiP17612
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17612

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 298Protein kinasePROSITE-ProRule annotationAdd BLAST255
Domaini299 – 351AGC-kinase C-terminalAdd BLAST53

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0616 Eukaryota
ENOG410XPQQ LUCA
GeneTreeiENSGT00810000125385
HOGENOMiHOG000233033
HOVERGENiHBG108317
InParanoidiP17612
KOiK04345
OMAiHSHDIIY
OrthoDBiEOG091G10O8
PhylomeDBiP17612
TreeFamiTF313399

Family and domain databases

InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR039811 cAMP/cGMP-dep_PK
IPR011009 Kinase-like_dom_sf
IPR039035 PKA_C-alpha
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24353 PTHR24353, 1 hit
PTHR24353: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

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 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
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

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:
K7ERP6K7ERP6_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
251Annotation score:
K7ENJ5K7ENJ5_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
124Annotation score:
K7EMV1K7EMV1_HUMAN
cAMP-dependent protein kinase catal...
PRKACA
25Annotation score:

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
Alternative sequenceiVSP_0047591 – 15MGNAA…SEQES → MASNSSD in isoform 2. 3 PublicationsAdd BLAST15

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

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, 89 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
MaxQBiP17612
PaxDbiP17612
PeptideAtlasiP17612
PRIDEiP17612
ProteomicsDBi53496
53497 [P17612-2]

Protocols and materials databases

DNASUi5566
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

CTDi5566
DisGeNETi5566
EuPathDBiHostDB:ENSG00000072062.13
GeneCardsiPRKACA
HGNCiHGNC:9380 PRKACA
HPAiCAB010361
HPA071185
MalaCardsiPRKACA
MIMi601639 gene
615830 phenotype
neXtProtiNX_P17612
OpenTargetsiENSG00000072062
Orphaneti401920 Fibrolamellar hepatocellular carcinoma
189439 Primary pigmented nodular adrenocortical disease
PharmGKBiPA33748
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0616 Eukaryota
ENOG410XPQQ LUCA
GeneTreeiENSGT00810000125385
HOGENOMiHOG000233033
HOVERGENiHBG108317
InParanoidiP17612
KOiK04345
OMAiHSHDIIY
OrthoDBiEOG091G10O8
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-983231 Factors involved in megakaryocyte development and platelet production
SABIO-RKiP17612
SignaLinkiP17612
SIGNORiP17612

Miscellaneous databases

ChiTaRSiPRKACA human
EvolutionaryTraceiP17612
GeneWikiiPRKACA
GenomeRNAii5566
PROiPR:P17612
SOURCEiSearch...

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
IPR039811 cAMP/cGMP-dep_PK
IPR011009 Kinase-like_dom_sf
IPR039035 PKA_C-alpha
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24353 PTHR24353, 1 hit
PTHR24353: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
ProtoNetiSearch...

Entry informationi

Entry nameiKAPCA_HUMAN
AccessioniPrimary (citable) accession number: P17612
Secondary accession number(s): Q32P54
, Q9H2Y0, Q9NRB4, Q9NRH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 217 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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