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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-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.12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme 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

  • ATP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase activity Source: BHF-UCL
  • protein kinase A regulatory subunit binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: MGI
  • protein serine/threonine kinase activity Source: Reactome
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01051-MONOMER.
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. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-163615. PKA activation.
R-HSA-164378. PKA activation in glucagon signalling.
R-HSA-180024. DARPP-32 events.
R-HSA-194223. HDL-mediated lipid transport.
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-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, 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-70263. Gluconeogenesis.
R-HSA-8853659. RET signaling.
R-HSA-8854518. AURKA Activation by TPX2.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SABIO-RKP17612.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9380. PRKACA.

Subcellular locationi

  • Cytoplasm
  • Cell membrane
  • Nucleus By similarity
  • Mitochondrion By similarity
  • Membrane Curated; Lipid-anchor Curated

  • Note: Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes (By similarity).By similarity
Isoform 2 :

GO - Cellular componenti

  • calcium channel complex Source: BHF-UCL
  • cAMP-dependent protein kinase complex Source: UniProtKB
  • centrosome Source: UniProtKB
  • ciliary base Source: Reactome
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • motile cilium Source: UniProtKB-KW
  • neuromuscular junction Source: Ensembl
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleotide-activated protein kinase complex Source: BHF-UCL
  • nucleus Source: UniProtKB
  • plasma membrane raft Source: UniProtKB
  • sperm midpiece Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, 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 rs386352352dbSNPEnsembl.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.
PharmGKBiPA33748.

Chemistry databases

ChEMBLiCHEMBL4101.
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 residuei202Phosphothreonine1 Publication1
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.

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.
CleanExiHS_PRKACA.
ExpressionAtlasiP17612. baseline and differential.
GenevisibleiP17612. HS.

Organism-specific databases

HPAiCAB010361.

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKIP1Q9NQ314EBI-476586,EBI-517035
ALOX5P099172EBI-476586,EBI-79934
GSK3BP498415EBI-476586,EBI-373586
LRRK2Q5S0076EBI-476586,EBI-5323863
PRKAR1AP106445EBI-476586,EBI-476431
PRKAR1BP313214EBI-476586,EBI-2805516
PRKAR2BP313239EBI-476586,EBI-2930670
Prkar2bP123692EBI-476586,EBI-6096160From a different organism.

GO - Molecular functioni

  • protein kinase A regulatory subunit binding Source: BHF-UCL
  • protein kinase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111553. 139 interactors.
DIPiDIP-33878N.
IntActiP17612. 75 interactors.
MINTiMINT-95365.
STRINGi9606.ENSP00000309591.

Chemistry databases

BindingDBiP17612.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi16 – 32Combined sources17
Helixi41 – 43Combined sources3
Beta strandi44 – 52Combined sources9
Beta strandi57 – 63Combined sources7
Turni64 – 66Combined sources3
Beta strandi69 – 76Combined sources8
Helixi77 – 82Combined sources6
Helixi86 – 98Combined sources13
Beta strandi107 – 112Combined sources6
Beta strandi114 – 122Combined sources9
Helixi129 – 136Combined sources8
Helixi141 – 160Combined sources20
Helixi170 – 172Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi181 – 183Combined sources3
Helixi186 – 188Combined sources3
Helixi203 – 205Combined sources3
Helixi208 – 211Combined sources4
Beta strandi212 – 214Combined sources3
Helixi219 – 234Combined sources16
Helixi244 – 253Combined sources10
Helixi264 – 273Combined sources10
Turni278 – 280Combined sources3
Turni282 – 284Combined sources3
Turni286 – 289Combined sources4
Helixi290 – 293Combined sources4
Helixi296 – 298Combined sources3
Helixi303 – 307Combined sources5
Turni345 – 350Combined sources6

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[»]
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

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

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

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

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

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04059141L → V.1 PublicationCorresponds to variant rs56029020dbSNPEnsembl.1
Natural variantiVAR_04059246R → Q.1 PublicationCorresponds to variant rs56085217dbSNPEnsembl.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 rs386352352dbSNPEnsembl.1
Natural variantiVAR_040593264S → C.1 PublicationCorresponds to variant rs35635531dbSNPEnsembl.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

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[»]
ProteinModelPortaliP17612.
SMRiP17612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111553. 139 interactors.
DIPiDIP-33878N.
IntActiP17612. 75 interactors.
MINTiMINT-95365.
STRINGi9606.ENSP00000309591.

Chemistry databases

BindingDBiP17612.
ChEMBLiCHEMBL4101.
GuidetoPHARMACOLOGYi1476.

PTM databases

iPTMnetiP17612.
PhosphoSitePlusiP17612.
SwissPalmiP17612.

Polymorphism and mutation databases

BioMutaiPRKACA.
DMDMi125205.

Proteomic databases

EPDiP17612.
MaxQBiP17612.
PaxDbiP17612.
PeptideAtlasiP17612.
PRIDEiP17612.

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.
GeneCardsiPRKACA.
HGNCiHGNC:9380. PRKACA.
HPAiCAB010361.
MalaCardsiPRKACA.
MIMi601639. gene.
615830. phenotype.
neXtProtiNX_P17612.
OpenTargetsiENSG00000072062.
Orphaneti401920. Fibrolamellar hepatocellular carcinoma.
PharmGKBiPA33748.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS01051-MONOMER.
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. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-HSA-163615. PKA activation.
R-HSA-164378. PKA activation in glucagon signalling.
R-HSA-180024. DARPP-32 events.
R-HSA-194223. HDL-mediated lipid transport.
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-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, 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-70263. Gluconeogenesis.
R-HSA-8853659. RET signaling.
R-HSA-8854518. AURKA Activation by TPX2.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SABIO-RKP17612.
SignaLinkiP17612.
SIGNORiP17612.

Miscellaneous databases

ChiTaRSiPRKACA. human.
EvolutionaryTraceiP17612.
GeneWikiiPRKACA.
GenomeRNAii5566.
PROiP17612.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072062.
CleanExiHS_PRKACA.
ExpressionAtlasiP17612. baseline and differential.
GenevisibleiP17612. HS.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAPCA_HUMAN
AccessioniPrimary (citable) accession number: P17612
Secondary accession number(s): Q32P54
, Q9H2Y0, Q9NRB4, Q9NRH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 196 of the entry and version 2 of the sequence. [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. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.