Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05132 (KAPCA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-dependent protein kinase catalytic subunit alpha

Short name=PKA C-alpha
EC=2.7.11.11
Gene names
Name:Prkaca
Synonyms:Pkaca
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.11

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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. Ref.21

Subunit structure

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. Ref.10 Ref.11 Ref.19

Subcellular location

Cytoplasm. Cell membrane By similarity. Nucleus By similarity. Mitochondrion. 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. Ref.9

Isoform 2: Cell projectionciliumflagellum By similarity. Note: Expressed in the midpiece region of the sperm flagellum By similarity. Ref.9

Tissue specificity

Isoform 2 is sperm specific. Ref.8

Developmental stage

Accumulates in oocytes before fertilization but fades out after fertilization. Ref.9

Post-translational modification

Autophosphorylated. Phosphorylation is enhanced by vitamin K2 By similarity. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity. Ref.5 Ref.6 Ref.12

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. Ref.5 Ref.6 Ref.12

Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficienncy. Ref.5 Ref.6 Ref.12

Disruption phenotype

Frequent early postnatal lethality. Survivals are runted accompanied with mature sperm exhibiting defective forward motility. Ref.7

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cilium
Cytoplasm
Flagellum
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
cAMP
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to parathyroid hormone stimulus

Inferred from mutant phenotype PubMed 19723499. Source: MGI

mesoderm formation

Inferred from genetic interaction PubMed 12004056. Source: MGI

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle arrest

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of protein export from nucleus

Inferred from mutant phenotype PubMed 17043310. Source: MGI

protein autophosphorylation

Inferred from direct assay PubMed 17855365PubMed 18191828. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 15465019PubMed 16481613PubMed 17855365PubMed 18191828PubMed 18202122PubMed 19056373PubMed 9218452. Source: MGI

regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of proteasomal protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic transmission

Inferred from mutant phenotype PubMed 15590926. Source: MGI

regulation of tight junction assembly

Inferred from electronic annotation. Source: Ensembl

sperm capacitation

Inferred from direct assay Ref.11. Source: UniProtKB

   Cellular_componentAMP-activated protein kinase complex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 12004056PubMed 9218452. Source: MGI

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 12931191. Source: MGI

neuromuscular junction

Inferred from direct assay PubMed 8794865. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 9218452. Source: MGI

plasma membrane

Inferred from direct assay PubMed 16782699. Source: MGI

sperm midpiece

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase activity

Inferred from direct assay PubMed 12200423. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 15465019PubMed 17855365PubMed 18202122. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05132-1)

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.
Isoform 2 (identifier: P05132-2)

Also known as: C-alpha-2; C-alpha-S; C(s);

The sequence of this isoform differs from the canonical sequence as follows:
     2-15: GNAAAAKKGSEQES → MASSSND

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 351350cAMP-dependent protein kinase catalytic subunit alpha
PRO_0000086053

Regions

Domain44 – 298255Protein kinase
Domain299 – 35153AGC-kinase C-terminal
Nucleotide binding50 – 589ATP
Nucleotide binding122 – 1287ATP
Nucleotide binding169 – 1724ATP

Sites

Active site1671Proton acceptor
Binding site731ATP

Amino acid modifications

Modified residue31Deamidated asparagine; partial Ref.6
Modified residue111Phosphoserine; by autocatalysis Ref.6
Modified residue491Phosphothreonine By similarity
Modified residue1401Phosphoserine
Modified residue1961Phosphothreonine By similarity
Modified residue1981Phosphothreonine; by PDPK1 Ref.5
Modified residue2021Phosphothreonine By similarity
Modified residue3311Phosphotyrosine Ref.12
Modified residue3391Phosphoserine
Lipidation21N-myristoyl glycine Ref.6

Natural variations

Alternative sequence2 – 1514GNAAA…SEQES → MASSSND in isoform 2.
VSP_004760

Experimental info

Mutagenesis1981T → D: No phosphorylation by PDPK1.
Mutagenesis2861K → P: Impaired inhibition by the R-subunit. Ref.19
Mutagenesis3281F → A: Reduced catalytic activity and impaired inhibition by the R-subunit. Ref.19
Sequence conflict331T → D in AAA39936. Ref.2
Sequence conflict2871N → D in AAA39936. Ref.2

Secondary structure

............................................................ 351
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (C-alpha-1) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 02F85D66EB21A1FA

FASTA35140,571
        10         20         30         40         50         60 
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDQFDRIKTL GTGSFGRVML 

        70         80         90        100        110        120 
VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV 

       130        140        150        160        170        180 
MEYVAGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY 

       190        200        210        220        230        240 
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF 

       250        260        270        280        290        300 
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT 

       310        320        330        340        350 
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F 

« Hide

Isoform 2 (C-alpha-2) (C-alpha-S) (C(s)) [UniParc].

Checksum: 67F650302774793D
Show »

FASTA34439,934

References

« Hide 'large scale' references
[1]"Characterization of genomic clones coding for the C alpha and C beta subunits of mouse cAMP-dependent protein kinase."
Chrivia J.C., Uhler M.D., McKnight G.S.
J. Biol. Chem. 263:5739-5744(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]"Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase."
Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G., McKnight G.S.
Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative C-alpha mRNA expressed specifically in spermatogenic cells."
San Agustin J.T., Wilkerson C.G., Witman G.B.
Mol. Biol. Cell 11:3031-3044(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153 (ISOFORM 2).
Tissue: Testis.
[5]"Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase."
Cheng X., Ma Y., Moore M., Hemmings B.A., Taylor S.S.
Proc. Natl. Acad. Sci. U.S.A. 95:9849-9854(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-198 BY PDPK1.
[6]"Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of cAMP-dependent protein kinase."
Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.
Biochemistry 40:225-231(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, DEAMIDATION AT ASN-3.
[7]"Mutation of the Calpha subunit of PKA leads to growth retardation and sperm dysfunction."
Skaalhegg B.S., Huang Y., Su T., Idzerda R.L., McKnight G.S., Burton K.A.
Mol. Endocrinol. 16:630-639(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"Sperm-specific protein kinase A catalytic subunit Calpha2 orchestrates cAMP signaling for male fertility."
Nolan M.A., Babcock D.F., Wennemuth G., Brown W., Burton K.A., McKnight G.S.
Proc. Natl. Acad. Sci. U.S.A. 101:13483-13488(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SPERMATOZOA CAPACITATION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2).
[9]"Developmentally acquired PKA localisation in mouse oocytes and embryos."
Webb R.J., Tinworth L., Thomas G.M., Zaccolo M., Carroll J.
Dev. Biol. 317:36-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[10]"Protein kinase A regulates resumption of meiosis by phosphorylation of Cdc25B in mammalian oocytes."
Pirino G., Wescott M.P., Donovan P.J.
Cell Cycle 8:665-670(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MEIOSIS RESUMPTION, FUNCTION AS CDC25B KINASE, INTERACTION WITH CDC25B.
[11]"Phosphorylation and consequent stimulation of the tyrosine kinase c-Abl by PKA in mouse spermatozoa; its implications during capacitation."
Baker M.A., Hetherington L., Curry B., Aitken R.J.
Dev. Biol. 333:57-66(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SPERMATOZOA CAPACITATION, FUNCTION AS ABL1 KINASE, INTERACTION WITH ABL1.
[12]"Direct modulation of the protein kinase A catalytic subunit alpha by growth factor receptor tyrosine kinases."
Caldwell G.B., Howe A.K., Nickl C.K., Dostmann W.R., Ballif B.A., Deming P.B.
J. Cell. Biochem. 113:39-48(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-331.
[13]"Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase."
Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H., Taylor S.S., Sowadski J.M.
Science 253:407-414(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[14]"Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor."
Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H., Taylor S.S., Sowadski J.M.
Biochemistry 32:2154-2161(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
[15]"Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine."
Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.
Biochemistry 36:4438-4448(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
[16]"A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility."
Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.
Structure 5:921-935(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[17]"PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation."
Kim C., Cheng C.Y., Saldanha S.A., Taylor S.S.
Cell 130:1032-1043(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.
[18]"PKA type IIalpha holoenzyme reveals a combinatorial strategy for isoform diversity."
Wu J., Brown S.H., von Daake S., Taylor S.S.
Science 318:274-279(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
[19]"Contribution of non-catalytic core residues to activity and regulation in protein kinase A."
Yang J., Kennedy E.J., Wu J., Deal M.S., Pennypacker J., Ghosh G., Taylor S.S.
J. Biol. Chem. 284:6241-6248(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT, MUTAGENESIS OF LYS-286 AND PHE-328.
[20]"Novel isoform-specific interfaces revealed by PKA RIIbeta holoenzyme structures."
Brown S.H.J., Wu J., Kim C., Alberto K., Taylor S.S.
J. Mol. Biol. 393:1070-1082(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS.
[21]"Dynamics connect substrate recognition to catalysis in protein kinase A."
Masterson L.R., Cheng C., Yu T., Tonelli M., Kornev A., Taylor S.S., Veglia G.
Nat. Chem. Biol. 6:821-828(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND SUBSTRATE PEPTIDE, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19960 expand/collapse EMBL AC list , 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.
PIROKMSCA. A28619.
RefSeqNP_001264827.1. NM_001277898.1.
NP_032880.1. NM_008854.5.
UniGeneMm.19111.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortalP05132.
SMRP05132. Positions 2-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202192. 17 interactions.
DIPDIP-6086N.
IntActP05132. 13 interactions.
MINTMINT-4051347.
STRING10090.ENSMUSP00000005606.

Chemistry

BindingDBP05132.

PTM databases

PhosphoSiteP05132.

Proteomic databases

PaxDbP05132.
PRIDEP05132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
GeneID18747.
KEGGmmu:18747.
UCSCuc009mll.2. mouse. [P05132-1]
uc009mlm.1. mouse. [P05132-2]

Organism-specific databases

CTD5566.
MGIMGI:97592. Prkaca.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074358.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidP05132.
KOK04345.
OMAMASNPND.
OrthoDBEOG7VX8WD.
PhylomeDBP05132.
TreeFamTF313399.

Enzyme and pathway databases

BRENDA2.7.11.11. 3474.
ReactomeREACT_188937. Metabolism.

Gene expression databases

BgeeP05132.
CleanExMM_PRKACA.
GenevestigatorP05132.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSPRKACA. mouse.
EvolutionaryTraceP05132.
NextBio294909.
PROP05132.
SOURCESearch...

Entry information

Entry nameKAPCA_MOUSE
AccessionPrimary (citable) accession number: P05132
Secondary accession number(s): Q9JID0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot