ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05132


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name KAPCA_MOUSE
Primary accession number P05132
Secondary accession number Q9JID0
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 122)
Name and origin of the protein
Protein name cAMP-dependent protein kinase catalytic subunit alpha
Synonyms PKA C-alpha
EC 2.7.11.11
Gene name
Name: Prkaca
Synonyms: Pkaca
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=2833513 [NCBI, ExPASy, EBI, Israel, Japan]
Chrivia J.C., Uhler M.D., McKnight G.S.;
"Characterization of genomic clones coding for the C alpha and C beta subunits of mouse cAMP-dependent protein kinase.";
J. Biol. Chem. 263:5739-5744(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3456589 [NCBI, ExPASy, EBI, Israel, Japan]
Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G., McKnight G.S.;
"Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE OF 1-153 (ISOFORM 2).
TISSUE=Testis;
PubMed=10982398 [NCBI, ExPASy, EBI, Israel, Japan]
San Agustin J.T., Wilkerson C.G., Witman G.B.;
"The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative C-alpha mRNA expressed specifically in spermatogenic cells.";
Mol. Biol. Cell 11:3031-3044(2000).
[5]
MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION AT ASN-3.
DOI=10.1021/bi0021277; PubMed=11141074 [NCBI, ExPASy, EBI, Israel, Japan]
Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
"Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of cAMP-dependent protein kinase.";
Biochemistry 40:225-231(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.M400085-MCP200; PubMed=15345747 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=1862342 [NCBI, ExPASy, EBI, Israel, Japan]
Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H., Taylor S.S., Sowadski J.M.;
"Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.";
Science 253:407-414(1991).
[9]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
DOI=10.1021/bi00060a005; PubMed=8443157 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H., Taylor S.S., Sowadski J.M.;
"Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor.";
Biochemistry 32:2154-2161(1993).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
DOI=10.1021/bi961947+; PubMed=9109651 [NCBI, ExPASy, EBI, Israel, Japan]
Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.;
"Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine.";
Biochemistry 36:4438-4448(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1016/S0969-2126(97)00246-3; PubMed=9261084 [NCBI, ExPASy, EBI, Israel, Japan]
Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.;
"A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility.";
Structure 5:921-935(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M19960; AAA39937.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18240; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18241; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19953; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19954; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19955; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19956; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19957; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19958; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19959; AAA39937.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12303; AAA39936.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003238; AAH03238.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054834; AAH54834.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF239743; AAF76425.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28619; OKMSCA.
RefSeq NP_032880.1; -.
UniGene Mm.19111
3D structure databases
PDB
1APM; X-ray; 2.00 A; E=1-351.[ExPASy / RCSB / EBI]
1ATP; X-ray; 2.20 A; E=1-351.[ExPASy / RCSB / EBI]
1BKX; X-ray; 2.60 A; A=1-351.[ExPASy / RCSB / EBI]
1BX6; X-ray; 2.10 A; A=1-351.[ExPASy / RCSB / EBI]
1FMO; X-ray; 2.20 A; E=1-351.[ExPASy / RCSB / EBI]
1J3H; X-ray; 2.90 A; A/B=1-351.[ExPASy / RCSB / EBI]
1JBP; X-ray; 2.20 A; E=2-351.[ExPASy / RCSB / EBI]
1JLU; X-ray; 2.25 A; E=1-351.[ExPASy / RCSB / EBI]
1L3R; X-ray; 2.00 A; E=1-351.[ExPASy / RCSB / EBI]
1PVK; Model; -; B=16-351.[ExPASy / RCSB / EBI]
1RDQ; X-ray; 1.26 A; E=1-351.[ExPASy / RCSB / EBI]
1RE8; X-ray; 2.10 A; A=1-351.[ExPASy / RCSB / EBI]
1REJ; X-ray; 2.20 A; A=1-351.[ExPASy / RCSB / EBI]
1REK; X-ray; 2.30 A; A=1-351.[ExPASy / RCSB / EBI]
1SYK; X-ray; 2.80 A; A/B=1-351.[ExPASy / RCSB / EBI]
1U7E; X-ray; 2.00 A; A=1-351.[ExPASy / RCSB / EBI]
2CPK; X-ray; 2.70 A; E=1-351.[ExPASy / RCSB / EBI]
2ERZ; X-ray; 2.20 A; E=1-351.[ExPASy / RCSB / EBI]
2QCS; X-ray; 2.20 A; A=2-351.[ExPASy / RCSB / EBI]
2QVS; X-ray; 2.50 A; E=2-351.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1APM; -.
1ATP; -.
1BKX; -.
1BX6; -.
1FMO; -.
1J3H; -.
1JBP; -.
1JLU; -.
1L3R; -.
1PVK; -.
1RDQ; -.
1RE8; -.
1REJ; -.
1REK; -.
1SYK; -.
1U7E; -.
2CPK; -.
2ERZ; -.
2QCS; -.
2QVS; -.
ModBase P05132.
Protein-protein interaction databases
DIP DIP:6086N; -.
IntAct P05132; -.
PTM databases
PhosphoSite P05132; -.
Organism-specific databases
MGI MGI:97592; Prkaca.
Gene expression databases
ArrayExpress P05132; -.
CleanEx MM_PRKACA; -.
GermOnline ENSMUSG00000005469; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0031594; Cellular component: neuromuscular junction (inferred from direct assay from MGI).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from MGI).
GO:0004691; Molecular function: cAMP-dependent protein kinase activity (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0001707; Biological process: mesoderm formation (inferred from genetic interaction from MGI).
GO:0046827; Biological process: positive regulation of protein export from nucleus (inferred from mutant phenotype from MGI).
GO:0046777; Biological process: protein amino acid autophosphorylation (inferred from direct assay from MGI).
GO:0050804; Biological process: regulation of synaptic transmission (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000961; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05132.
ProtoNet P05132.
Genome annotation databases
Ensembl ENSMUSG00000005469; Mus musculus. [Contig view]
GeneID 18747; -.
KEGG mmu:18747; -.
Phylogenomic databases
HOGENOM P05132; -.
HOVERGEN P05132; -.
Other
LinkHub P05132; -.
NextBio 294909; -.
SOURCE Prkaca; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; cAMP; Cytoplasm; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   351  350     cAMP-dependent protein kinase catalytic subunit alpha. PRO_0000086053
DOMAIN   44   298  255     Protein kinase. 
DOMAIN   299   351  53     AGC-kinase C-terminal. 
NP_BIND   50    58  9     ATP. 
ACT_SITE   167   167        Proton acceptor. 
BINDING   73    73        ATP. 
MOD_RES   3     3        Deamidated asparagine; partial. 
MOD_RES   11    11        Phosphoserine; by autocatalysis. 
MOD_RES   35    35        Phosphoserine. 
MOD_RES   140   140        Phosphoserine. 
MOD_RES   196   196        Phosphothreonine. 
MOD_RES   198   198        Phosphothreonine. 
MOD_RES   202   202        Phosphothreonine (By similarity). 
MOD_RES   339   339        Phosphoserine. 
LIPID   2     2        N-myristoyl glycine. 
VAR_SEQ   1    15        MGNAAAAKKGSEQES -> MASSSND (in isoform 2). VSP_004760
MUTAGEN   198   198        T->D: No phosphorylation by PDPK1. 
CONFLICT   33    33        T -> D (in Ref. 2; AAA39936). 
CONFLICT   287   287        N -> D (in Ref. 2; AAA39936). 
HELIX   16    32  17      
HELIX   41    43  3      
STRAND   44    52  9      
STRAND   57    63  7      
TURN   64    66  3      
STRAND   69    76  8      
HELIX   77    82  6      
HELIX   86    96  11      
STRAND   107   112  6      
STRAND   114   122  9      
HELIX   129   136  8      
HELIX   141   160  20      
HELIX   170   172  3      
STRAND   173   175  3      
STRAND   181   183  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   286   289  4      
HELIX   290   293  4      
HELIX   296   298  3      
HELIX   303   307  5      
TURN   345   350  6      
Sequence information
Length: 351 AA [This is the length of the unprocessed precursor] Molecular weight: 40571 Da [This is the MW of the unprocessed precursor] CRC64: 02F85D66EB21A1FA [This is a checksum on the sequence]
        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 

P05132 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!