P05132 (KAPCA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase catalytic subunit alpha
Short name=PKA C-alpha
EC=2.7.11.11

Gene names

Name:	Prkaca
Synonyms:	Pkaca

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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, TRPC1 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+. TRPC1 activation by phosphorylation promotes Ca2+ influx, essential for the increase in permeability induced by thrombin in confluent endothelial monolayers. PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Regulates negatively tight junction (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. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. 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 By similarity. Ref.9 Ref.12 Ref.13
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.22
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. Ref.12 Ref.13 Ref.20
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.11
Tissue specificity	Isoform 2 is sperm specific. Ref.9
Developmental stage	Accumulates in oocytes before fertilization but fades out after fertilization. Ref.11
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 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
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 component	Cell membrane Cytoplasm Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of cell cycle arrest Inferred from direct assay Ref.12. 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 regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara regulation of proteasomal protein catabolic process Inferred from electronic annotation. Source: Compara regulation of synaptic transmission Inferred from mutant phenotype PubMed 15590926. Source: MGI regulation of tight junction assembly Inferred from electronic annotation. Source: Compara sperm capacitation Inferred from direct assay Ref.13. Source: UniProtKB
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara 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 plasma membrane Inferred from direct assay PubMed 16782699. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase activity Inferred from direct assay PubMed 12200423. Source: UniProtKB
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:
     1-15: MGNAAAAKKGSEQES → MASSSND

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 351

350

cAMP-dependent protein kinase catalytic subunit alpha

PRO_0000086053

Regions

Domain

44 – 298

255

Protein kinase

Domain

299 – 351

53

AGC-kinase C-terminal

Nucleotide binding

50 – 58

9

ATP

Nucleotide binding

122 – 128

7

ATP

Nucleotide binding

169 – 172

4

ATP

Sites

Active site

167

1

Proton acceptor

Binding site

73

1

ATP

Amino acid modifications

Modified residue

3

1

Deamidated asparagine; partial Ref.6

Modified residue

11

1

Phosphoserine; by autocatalysis Ref.6

Modified residue

35

1

Phosphoserine Ref.10

Modified residue

49

1

Phosphothreonine By similarity

Modified residue

140

1

Phosphoserine

Modified residue

196

1

Phosphothreonine Ref.8

Modified residue

198

1

Phosphothreonine; by PDPK1 Ref.5

Modified residue

202

1

Phosphothreonine By similarity

Modified residue

339

1

Phosphoserine

Lipidation

2

1

N-myristoyl glycine Ref.6

Natural variations

Alternative sequence

1 – 15

15

MGNAA…SEQES → MASSSND in isoform 2.

VSP_004760

Experimental info

Mutagenesis

198

1

T → D: No phosphorylation by PDPK1.

Mutagenesis

286

1

K → P: Impaired inhibition by the R-subunit. Ref.20

Mutagenesis

328

1

F → A: Reduced catalytic activity and impaired inhibition by the R-subunit. Ref.20

Sequence conflict

33

1

T → D in AAA39936. Ref.2

Sequence conflict

287

1

N → D in AAA39936. Ref.2

Secondary structure

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351

Helix Strand Turn

Details...

Helix

3 – 7

5

Turn

9 – 12

4

Helix

16 – 32

17

Helix

41 – 43

3

Beta strand

44 – 52

9

Beta strand

57 – 63

7

Turn

64 – 66

3

Beta strand

69 – 76

8

Helix

77 – 82

6

Helix

86 – 96

11

Beta strand

107 – 112

6

Beta strand

114 – 122

9

Helix

129 – 136

8

Helix

141 – 160

20

Beta strand

162 – 164

3

Helix

170 – 172

3

Beta strand

173 – 175

3

Beta strand

181 – 183

3

Helix

186 – 188

3

Helix

203 – 205

3

Helix

208 – 211

4

Helix

219 – 234

16

Helix

244 – 253

10

Helix

264 – 273

10

Turn

278 – 280

3

Turn

282 – 284

3

Turn

286 – 289

4

Helix

290 – 293

4

Helix

296 – 298

3

Helix

303 – 307

5

Beta strand

321 – 326

6

Turn

345 – 350

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (C-alpha-1) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 02F85D66EB21A1FA	FASTA	351	40,571
	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
	Isoform 2 (C-alpha-2) (C-alpha-S) (C(s)) [UniParc]. Checksum: EC2012B8F9A59DB7	FASTA	343	39,803
	10 20 30 40 50 60 MASSSNDVKE FLAKAKEDFL KKWETPSQNT AQLDQFDRIK TLGTGSFGRV MLVKHKESGN 70 80 90 100 110 120 HYAMKILDKQ KVVKLKQIEH TLNEKRILQA VNFPFLVKLE FSFKDNSNLY MVMEYVAGGE 130 140 150 160 170 180 MFSHLRRIGR FSEPHARFYA AQIVLTFEYL HSLDLIYRDL KPENLLIDQQ GYIQVTDFGF 190 200 210 220 230 240 AKRVKGRTWT LCGTPEYLAP EIILSKGYNK AVDWWALGVL IYEMAAGYPP FFADQPIQIY 250 260 270 280 290 300 EKIVSGKVRF PSHFSSDLKD LLRNLLQVDL TKRFGNLKNG VNDIKNHKWF ATTDWIAIYQ 310 320 330 340 RKVEAPFIPK FKGPGDTSNF DDYEEEEIRV SINEKCGKEF TEF

References

	« Hide 'large scale' referencesShow '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]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, MASS SPECTROMETRY. Tissue: Embryonic brain.
[9]	"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, TISSUE SPECIFICITY.
[10]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Tissue: Liver.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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).
[15]	"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.
[16]	"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.
[17]	"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).
[18]	"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.
[19]	"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).
[20]	"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.
[21]	"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.
[22]	"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 , 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.

IPI

IPI00227900.
IPI00230005.

PIR

OKMSCA. A28619.

RefSeq

NP_032880.1. NM_008854.4.

UniGene

Mm.19111.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APM	X-ray	2.00	E	2-350	[»]
1ATP	X-ray	2.20	E	2-350	[»]
1BKX	X-ray	2.60	A	2-351	[»]
1BX6	X-ray	2.10	A	2-350	[»]
1FMO	X-ray	2.20	E	2-351	[»]
1J3H	X-ray	2.90	A/B	2-350	[»]
1JBP	X-ray	2.20	E	2-351	[»]
1JLU	X-ray	2.25	E	2-351	[»]
1L3R	X-ray	2.00	E	2-351	[»]
1PVK	model	-	B	16-351	[»]
1RDQ	X-ray	1.26	E	2-350	[»]
1RE8	X-ray	2.10	A	2-350	[»]
1REJ	X-ray	2.20	A	2-350	[»]
1REK	X-ray	2.30	A	2-350	[»]
1SYK	X-ray	2.80	A/B	2-351	[»]
2CPK	X-ray	2.70	E	2-351	[»]
2ERZ	X-ray	2.20	E	1-351	[»]
2QCS	X-ray	2.20	A	2-351	[»]
2QUR	X-ray	2.50	A	2-351	[»]
2QVS	X-ray	2.50	E	2-351	[»]
3FHI	X-ray	2.00	A	2-351	[»]
3FJQ	X-ray	1.60	E	2-351	[»]
3IDB	X-ray	1.62	A	2-351	[»]
3IDC	X-ray	2.70	A	2-351	[»]
3O7L	X-ray	2.80	B/D	2-351	[»]
3OW3	X-ray	1.90	A	2-351	[»]
3PVB	X-ray	3.30	A	7-351	[»]
3QAL	X-ray	1.70	E	2-351	[»]
3QAM	X-ray	1.92	E	2-351	[»]
4DFX	X-ray	1.35	E	2-351	[»]
4DFY	X-ray	3.00	A/E	1-351	[»]
4DFZ	X-ray	2.00	E	2-351	[»]
4DG0	X-ray	2.00	E	2-351	[»]
4DG2	X-ray	2.00	E	2-351	[»]
4DG3	X-ray	1.80	E	1-351	[»]
4DH1	X-ray	2.00	A	2-351	[»]
4DH3	X-ray	2.20	A	2-351	[»]
4DH5	X-ray	2.20	A	2-351	[»]
4DH7	X-ray	1.80	A	2-351	[»]
4DH8	X-ray	2.30	A	2-351	[»]
4DIN	X-ray	3.70	A	2-351	[»]
4HPT	X-ray	2.15	E	2-351	[»]
4HPU	X-ray	1.55	E	2-351	[»]

ProteinModelPortal

P05132.

SMR

P05132. Positions 2-351.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6086N.

IntAct

P05132. 5 interactions.

MINT

MINT-4051347.

STRING

10090.ENSMUSP00000005606.

PTM databases

PhosphoSite

P05132.

Proteomic databases

PaxDb

P05132.

PRIDE

P05132.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469.

GeneID

18747.

KEGG

mmu:18747.

UCSC

uc009mll.2. mouse.
uc009mlm.1. mouse.

Organism-specific databases

CTD

5566.

MGI

MGI:97592. Prkaca.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00550000074358.

HOGENOM

HOG000233033.

HOVERGEN

HBG108317.

InParanoid

P05132.

KO

K04345.

OMA

GQHFAMK.

OrthoDB

EOG4RXZ0C.

Enzyme and pathway databases

BRENDA

2.7.11.11. 3474.

Reactome

REACT_112621. Metabolism.

Gene expression databases

Bgee

P05132.

CleanEx

MM_PRKACA.

Genevestigator

P05132.

GermOnline

ENSMUSG00000005469. Mus musculus.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05132.

ChEMBL

CHEMBL4991.

ChiTaRS

PRKACA. mouse.

EvolutionaryTrace

P05132.

NextBio

294909.

SOURCE

Search...

Entry information

Entry name

KAPCA_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 168 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program