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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATP
Active sitei167 – 1671Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATP
Nucleotide bindingi122 – 1287ATP
Nucleotide bindingi169 – 1724ATP

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 meiotic cell cycle Source: Ensembl
  • 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 cell proliferation Source: Ensembl
  • 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 cellular respiration Source: Ensembl
  • regulation of osteoblast differentiation Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • regulation of protein processing Source: MGI
  • regulation of synaptic transmission, glutamatergic Source: Ensembl
  • 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-4420097. VEGFA-VEGFR2 Pathway.
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

  • cAMP-dependent protein kinase complex Source: Ensembl
  • centrosome Source: MGI
  • ciliary base Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: Ensembl
  • mitochondrion Source: MGI
  • neuromuscular junction Source: MGI
  • neuron projection Source: Ensembl
  • nuclear speck Source: MGI
  • nucleoplasm Source: Reactome
  • nucleotide-activated protein kinase complex Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: MGI
  • plasma membrane raft Source: MGI
  • sperm midpiece Source: MGI
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981T → D: No phosphorylation by PDPK1.
Mutagenesisi286 – 2861K → P: Impaired inhibition by the R-subunit. 1 Publication
Mutagenesisi328 – 3281F → A: Reduced catalytic activity and impaired inhibition by the R-subunit. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit alphaPRO_0000086053Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei3 – 31Deamidated asparagine; partial1 Publication
Modified residuei11 – 111Phosphoserine; by autocatalysis2 Publications
Modified residuei49 – 491PhosphothreonineBy similarity
Modified residuei140 – 1401Phosphoserine1 Publication1 Publication
Modified residuei196 – 1961PhosphothreonineBy similarity
Modified residuei198 – 1981Phosphothreonine; by PDPK13 Publications
Modified residuei202 – 2021PhosphothreonineBy similarity
Modified residuei331 – 3311Phosphotyrosine1 Publication
Modified residuei339 – 3391Phosphoserine1 Publication

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.
PhosphoSiteiP05132.

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 interactions.
DIPiDIP-6086N.
IntActiP05132. 13 interactions.
MINTiMINT-4051347.
STRINGi10090.ENSMUSP00000005606.

Chemistry

BindingDBiP05132.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 75Combined sources
Turni9 – 124Combined sources
Helixi16 – 3217Combined sources
Helixi41 – 433Combined sources
Beta strandi44 – 529Combined sources
Beta strandi57 – 637Combined sources
Turni64 – 663Combined sources
Beta strandi69 – 768Combined sources
Helixi77 – 826Combined sources
Helixi86 – 9611Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi114 – 1229Combined sources
Helixi129 – 1368Combined sources
Helixi141 – 16020Combined sources
Beta strandi162 – 1643Combined sources
Helixi170 – 1723Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi181 – 1833Combined sources
Helixi186 – 1883Combined sources
Helixi203 – 2053Combined sources
Helixi208 – 2114Combined sources
Helixi219 – 23416Combined sources
Helixi244 – 25310Combined sources
Helixi264 – 27310Combined sources
Turni278 – 2803Combined sources
Turni282 – 2843Combined sources
Turni286 – 2894Combined sources
Helixi290 – 2934Combined sources
Helixi296 – 2983Combined sources
Helixi303 – 3075Combined sources
Beta strandi321 – 3266Combined sources
Turni345 – 3506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-351.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 298255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35153AGC-kinase C-terminalAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331T → D in AAA39936 (PubMed:3456589).Curated
Sequence conflicti287 – 2871N → D in AAA39936 (PubMed:3456589).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MGNAA…SEQES → MASSSND in isoform 2. 1 PublicationVSP_004760Add
BLAST

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]
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
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. Positions 2-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP05132.

PTM databases

iPTMnetiP05132.
PhosphoSiteiP05132.

Proteomic databases

EPDiP05132.
MaxQBiP05132.
PaxDbiP05132.
PeptideAtlasiP05132.
PRIDEiP05132.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
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-4420097. VEGFA-VEGFR2 Pathway.
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: September 7, 2016
This is version 203 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.