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Protein

cAMP-dependent protein kinase catalytic subunit alpha

Gene

Prkaca

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity2 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73ATP1
Active sitei167Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 58ATP9
Nucleotide bindingi122 – 128ATP7
Nucleotide bindingi169 – 172ATP4

GO - Molecular functioni

GO - Biological processi

  • cellular response to glucose stimulus Source: MGI
  • cellular response to parathyroid hormone stimulus Source: MGI
  • intracellular signal transduction Source: Reactome
  • mesoderm formation Source: MGI
  • modulation of synaptic transmission Source: MGI
  • mRNA processing Source: MGI
  • negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
  • neural tube closure Source: MGI
  • peptidyl-serine phosphorylation Source: MGI
  • peptidyl-threonine phosphorylation Source: MGI
  • positive regulation of cell cycle arrest Source: UniProtKB
  • positive regulation of protein export from nucleus Source: MGI
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: MGI
  • regulation of bicellular tight junction assembly Source: MGI
  • regulation of osteoblast differentiation Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • regulation of protein processing Source: MGI
  • sperm capacitation Source: UniProtKB
  • triglyceride catabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.11. 3474.
ReactomeiR-MMU-163358. PKA-mediated phosphorylation of key metabolic factors.
R-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-180024. DARPP-32 events.
R-MMU-194223. HDL-mediated lipid transport.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-MMU-392517. Rap1 signalling.
R-MMU-422356. Regulation of insulin secretion.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5578775. Ion homeostasis.
R-MMU-5610783. Degradation of GLI2 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5621575. CD209 (DC-SIGN) signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-8854518. AURKA Activation by TPX2.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:97592. Prkaca.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane By similarity
  • Nucleus By similarity
  • Mitochondrion 1 Publication
  • Membrane By similarity; Lipid-anchor By similarity

  • Note: Translocates into the nucleus (monomeric catalytic subunit) (By similarity). 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
Isoform 2 :

GO - Cellular componenti

  • centrosome Source: MGI
  • ciliary base Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • motile cilium Source: UniProtKB-KW
  • neuromuscular junction Source: MGI
  • nuclear speck Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • plasma membrane raft Source: MGI
  • sperm midpiece Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Frequent early postnatal lethality. Survivals are runted accompanied with mature sperm exhibiting defective forward motility.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi198T → D: No phosphorylation by PDPK1. 1
Mutagenesisi286K → P: Impaired inhibition by the R-subunit. 1 Publication1
Mutagenesisi328F → A: Reduced catalytic activity and impaired inhibition by the R-subunit. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000860532 – 351cAMP-dependent protein kinase catalytic subunit alphaAdd BLAST350

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei3Deamidated asparagine; partial1 Publication1
Modified residuei11Phosphoserine; by autocatalysis2 Publications1
Modified residuei49PhosphothreonineBy similarity1
Modified residuei140Phosphoserine1 Publication1 Publication1
Modified residuei196PhosphothreonineBy similarity1
Modified residuei198Phosphothreonine; by PDPK13 Publications1
Modified residuei202PhosphothreonineBy similarity1
Modified residuei331Phosphotyrosine1 Publication1
Modified residuei339Phosphoserine1 Publication1

Post-translational modificationi

Autophosphorylated. Phosphorylation is enhanced by vitamin K2 (By similarity). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity.By similarity2 Publications
Asn-3 is partially deaminated to Asp-3 giving rise to 2 major isoelectric variants, called CB and CA respectively.
When myristoylated, Ser-11 is autophosphorylated probably in conjunction with deamidation of Asn-3.2 Publications
Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiP05132.
MaxQBiP05132.
PaxDbiP05132.
PeptideAtlasiP05132.
PRIDEiP05132.

PTM databases

iPTMnetiP05132.
PhosphoSitePlusiP05132.

Expressioni

Tissue specificityi

Isoform 2 is sperm specific.

Developmental stagei

Accumulates in oocytes before fertilization but fades out after fertilization.1 Publication

Gene expression databases

BgeeiENSMUSG00000005469.
CleanExiMM_PRKACA.
GenevisibleiP05132. MM.

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. Protein kinase A holoenzyme is comprised of two catalytic (C) and two regulatory (R) subunits which keep the enzyme in an inhibited state before activation by cyclic-AMP. 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 (By similarity). Interacts with RAB13; downstream effector of RAB13 involved in tight junction assembly (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Prkar2bP313243EBI-400564,EBI-455340

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202192. 20 interactors.
DIPiDIP-6086N.
IntActiP05132. 13 interactors.
MINTiMINT-4051347.
STRINGi10090.ENSMUSP00000005606.

Chemistry databases

BindingDBiP05132.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 7Combined sources5
Turni9 – 12Combined 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 – 96Combined sources11
Beta strandi107 – 112Combined sources6
Beta strandi114 – 122Combined sources9
Helixi129 – 136Combined sources8
Helixi141 – 160Combined sources20
Beta strandi162 – 164Combined sources3
Helixi170 – 172Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi181 – 183Combined sources3
Helixi186 – 188Combined sources3
Helixi203 – 205Combined sources3
Helixi208 – 211Combined sources4
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
Beta strandi321 – 326Combined sources6
Turni345 – 350Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APMX-ray2.00E2-351[»]
1ATPX-ray2.20E2-351[»]
1BKXX-ray2.60A2-351[»]
1BX6X-ray2.10A2-351[»]
1FMOX-ray2.20E2-351[»]
1J3HX-ray2.90A/B2-351[»]
1JBPX-ray2.20E2-351[»]
1JLUX-ray2.25E2-351[»]
1L3RX-ray2.00E2-351[»]
1PVKmodel-B16-351[»]
1RDQX-ray1.26E2-351[»]
1RE8X-ray2.10A2-351[»]
1REJX-ray2.20A2-351[»]
1REKX-ray2.30A2-351[»]
1SYKX-ray2.80A/B2-351[»]
2CPKX-ray2.70E2-351[»]
2ERZX-ray2.20E1-351[»]
2QCSX-ray2.20A2-351[»]
2QURX-ray2.50A2-351[»]
2QVSX-ray2.50E2-351[»]
3FHIX-ray2.00A2-351[»]
3FJQX-ray1.60E2-351[»]
3IDBX-ray1.62A2-351[»]
3IDCX-ray2.70A2-351[»]
3J4Qelectron microscopy35.00D/E1-351[»]
3J4Relectron microscopy35.00D/E1-351[»]
3O7LX-ray2.80B/D2-351[»]
3OW3X-ray1.90A2-351[»]
3PVBX-ray3.30A7-351[»]
3QALX-ray1.70E2-351[»]
3QAMX-ray1.92E2-351[»]
3TNPX-ray2.30C/F2-351[»]
3TNQX-ray3.10B2-351[»]
3X2UX-ray2.40A1-351[»]
3X2VX-ray1.77A1-351[»]
3X2WX-ray1.70A1-351[»]
4DFXX-ray1.35E2-351[»]
4DFYX-ray3.00A/E1-351[»]
4DFZX-ray2.00E2-351[»]
4DG0X-ray2.00E2-351[»]
4DG2X-ray2.00E2-351[»]
4DG3X-ray1.80E1-351[»]
4DH1X-ray2.00A16-351[»]
4DH3X-ray2.20A2-351[»]
4DH5X-ray2.20A2-351[»]
4DH7X-ray1.80A2-351[»]
4DH8X-ray2.30A2-351[»]
4DINX-ray3.70A2-351[»]
4HPTX-ray2.15E2-351[»]
4HPUX-ray1.55E2-351[»]
4IACX-ray2.15A2-351[»]
4IADX-ray1.90A2-351[»]
4IAFX-ray2.20A2-351[»]
4IAIX-ray1.55A2-351[»]
4IAKX-ray1.60A2-351[»]
4IAYX-ray2.00A2-351[»]
4IAZX-ray1.85A2-351[»]
4IB0X-ray1.87A2-351[»]
4IB1X-ray1.63A2-351[»]
4IB3X-ray2.20A2-351[»]
4NTSX-ray2.90A/B2-351[»]
4NTTX-ray3.50A/B2-351[»]
4O21X-ray1.95A16-351[»]
4O22X-ray1.70A16-351[»]
4WBBX-ray2.80B2-351[»]
4X6QX-ray2.52C2-351[»]
4X6RX-ray2.40A2-351[»]
4XW4X-ray1.82A15-351[»]
4XW5X-ray1.95A15-351[»]
4XW6X-ray1.90A15-351[»]
ProteinModelPortaliP05132.
SMRiP05132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05132.

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.
InParanoidiP05132.
KOiK04345.
OMAiNAATANK.
OrthoDBiEOG091G10O8.
PhylomeDBiP05132.
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: P05132-1) [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 WETPSQNTAQ LDQFDRIKTL
60 70 80 90 100
GTGSFGRVML VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN
110 120 130 140 150
FPFLVKLEFS FKDNSNLYMV MEYVAGGEMF 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 NEKCGKEFTE

F
Length:351
Mass (Da):40,571
Last modified:January 23, 2007 - v3
Checksum:i02F85D66EB21A1FA
GO
Isoform 2 (identifier: P05132-2) [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 → MASSSND

Show »
Length:343
Mass (Da):39,803
Checksum:iEC2012B8F9A59DB7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33T → D in AAA39936 (PubMed:3456589).Curated1
Sequence conflicti287N → D in AAA39936 (PubMed:3456589).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0047601 – 15MGNAA…SEQES → MASSSND in isoform 2. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19960
, M18240, M18241, M19953, M19954, M19955, M19956, M19957, M19958, M19959 Genomic DNA. Translation: AAA39937.1.
M12303 mRNA. Translation: AAA39936.1.
BC003238 mRNA. Translation: AAH03238.1.
BC054834 mRNA. Translation: AAH54834.1.
AF239743 mRNA. Translation: AAF76425.1.
CCDSiCCDS22463.1. [P05132-1]
PIRiA28619. OKMSCA.
RefSeqiNP_001264827.1. NM_001277898.1. [P05132-2]
NP_032880.1. NM_008854.5. [P05132-1]
UniGeneiMm.19111.

Genome annotation databases

EnsembliENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
ENSMUST00000211558; ENSMUSP00000147256; ENSMUSG00000005469. [P05132-2]
GeneIDi18747.
KEGGimmu:18747.
UCSCiuc009mll.3. mouse. [P05132-1]
uc009mlm.2. mouse. [P05132-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19960
, M18240, M18241, M19953, M19954, M19955, M19956, M19957, M19958, M19959 Genomic DNA. Translation: AAA39937.1.
M12303 mRNA. Translation: AAA39936.1.
BC003238 mRNA. Translation: AAH03238.1.
BC054834 mRNA. Translation: AAH54834.1.
AF239743 mRNA. Translation: AAF76425.1.
CCDSiCCDS22463.1. [P05132-1]
PIRiA28619. OKMSCA.
RefSeqiNP_001264827.1. NM_001277898.1. [P05132-2]
NP_032880.1. NM_008854.5. [P05132-1]
UniGeneiMm.19111.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APMX-ray2.00E2-351[»]
1ATPX-ray2.20E2-351[»]
1BKXX-ray2.60A2-351[»]
1BX6X-ray2.10A2-351[»]
1FMOX-ray2.20E2-351[»]
1J3HX-ray2.90A/B2-351[»]
1JBPX-ray2.20E2-351[»]
1JLUX-ray2.25E2-351[»]
1L3RX-ray2.00E2-351[»]
1PVKmodel-B16-351[»]
1RDQX-ray1.26E2-351[»]
1RE8X-ray2.10A2-351[»]
1REJX-ray2.20A2-351[»]
1REKX-ray2.30A2-351[»]
1SYKX-ray2.80A/B2-351[»]
2CPKX-ray2.70E2-351[»]
2ERZX-ray2.20E1-351[»]
2QCSX-ray2.20A2-351[»]
2QURX-ray2.50A2-351[»]
2QVSX-ray2.50E2-351[»]
3FHIX-ray2.00A2-351[»]
3FJQX-ray1.60E2-351[»]
3IDBX-ray1.62A2-351[»]
3IDCX-ray2.70A2-351[»]
3J4Qelectron microscopy35.00D/E1-351[»]
3J4Relectron microscopy35.00D/E1-351[»]
3O7LX-ray2.80B/D2-351[»]
3OW3X-ray1.90A2-351[»]
3PVBX-ray3.30A7-351[»]
3QALX-ray1.70E2-351[»]
3QAMX-ray1.92E2-351[»]
3TNPX-ray2.30C/F2-351[»]
3TNQX-ray3.10B2-351[»]
3X2UX-ray2.40A1-351[»]
3X2VX-ray1.77A1-351[»]
3X2WX-ray1.70A1-351[»]
4DFXX-ray1.35E2-351[»]
4DFYX-ray3.00A/E1-351[»]
4DFZX-ray2.00E2-351[»]
4DG0X-ray2.00E2-351[»]
4DG2X-ray2.00E2-351[»]
4DG3X-ray1.80E1-351[»]
4DH1X-ray2.00A16-351[»]
4DH3X-ray2.20A2-351[»]
4DH5X-ray2.20A2-351[»]
4DH7X-ray1.80A2-351[»]
4DH8X-ray2.30A2-351[»]
4DINX-ray3.70A2-351[»]
4HPTX-ray2.15E2-351[»]
4HPUX-ray1.55E2-351[»]
4IACX-ray2.15A2-351[»]
4IADX-ray1.90A2-351[»]
4IAFX-ray2.20A2-351[»]
4IAIX-ray1.55A2-351[»]
4IAKX-ray1.60A2-351[»]
4IAYX-ray2.00A2-351[»]
4IAZX-ray1.85A2-351[»]
4IB0X-ray1.87A2-351[»]
4IB1X-ray1.63A2-351[»]
4IB3X-ray2.20A2-351[»]
4NTSX-ray2.90A/B2-351[»]
4NTTX-ray3.50A/B2-351[»]
4O21X-ray1.95A16-351[»]
4O22X-ray1.70A16-351[»]
4WBBX-ray2.80B2-351[»]
4X6QX-ray2.52C2-351[»]
4X6RX-ray2.40A2-351[»]
4XW4X-ray1.82A15-351[»]
4XW5X-ray1.95A15-351[»]
4XW6X-ray1.90A15-351[»]
ProteinModelPortaliP05132.
SMRiP05132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202192. 20 interactors.
DIPiDIP-6086N.
IntActiP05132. 13 interactors.
MINTiMINT-4051347.
STRINGi10090.ENSMUSP00000005606.

Chemistry databases

BindingDBiP05132.

PTM databases

iPTMnetiP05132.
PhosphoSitePlusiP05132.

Proteomic databases

EPDiP05132.
MaxQBiP05132.
PaxDbiP05132.
PeptideAtlasiP05132.
PRIDEiP05132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
ENSMUST00000211558; ENSMUSP00000147256; ENSMUSG00000005469. [P05132-2]
GeneIDi18747.
KEGGimmu:18747.
UCSCiuc009mll.3. mouse. [P05132-1]
uc009mlm.2. mouse. [P05132-2]

Organism-specific databases

CTDi5566.
MGIiMGI:97592. Prkaca.

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP05132.
KOiK04345.
OMAiNAATANK.
OrthoDBiEOG091G10O8.
PhylomeDBiP05132.
TreeFamiTF313399.

Enzyme and pathway databases

BRENDAi2.7.11.11. 3474.
ReactomeiR-MMU-163358. PKA-mediated phosphorylation of key metabolic factors.
R-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-180024. DARPP-32 events.
R-MMU-194223. HDL-mediated lipid transport.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-MMU-392517. Rap1 signalling.
R-MMU-422356. Regulation of insulin secretion.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling.
R-MMU-5578775. Ion homeostasis.
R-MMU-5610783. Degradation of GLI2 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5610787. Hedgehog 'off' state.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5621575. CD209 (DC-SIGN) signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-8854518. AURKA Activation by TPX2.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiPrkaca. mouse.
EvolutionaryTraceiP05132.
PROiP05132.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005469.
CleanExiMM_PRKACA.
GenevisibleiP05132. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P05132
Secondary accession number(s): Q9JID0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 205 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. 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.