Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9823-00867
Entry Name
UniProt Accession
Theoretical PI
8.79
Molecular Weight
40593.71
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
cAMP-dependent protein kinase catalytic subunit beta
Protein Synonyms/Alias
PKA C-beta; 2.7.11.11;
Gene Name
PRKACB
Gene Synonyms/Alias
Created Date
01-NOV-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNAATAKK
[1]
N-Myristoylation
Organism
Sus scrofa (Pig)
NCBI Taxa ID
9823
Reference
[1] Jedrzejewski PT, Girod A, Tholey A, König N, Thullner S, Kinzel V, Bossemeyer D. A conserved deamidation site at Asn 2 in the catalytic subunit of mammaliancAMP-dependent protein kinase detected by capillary LC-MS and tandem massspectrometry. Protein Sci. 1998 Feb;7(2):457-69.[PMID:9521123]
Functional Description
Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. 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 (By similarity).
Sequence Annotation
Domain: 44 298 Protein kinase.
Domain: 299 351 AGC-kinase C-terminal.
Nucleotide-binding: 50 58 ATP.
Active site: 167 167 Proton acceptor.
Binding site: 73 73 ATP.
Modified residue: 3 3 Deamidated asparagine; partial.
Modified residue: 11 11 Phosphoserine.
Modified residue: 49 49 Phosphothreonine.
Modified residue: 69 69 Phosphotyrosine.
Modified residue: 140 140 Phosphoserine.
Modified residue: 196 196 Phosphothreonine.
Modified residue: 198 198 Phosphothreonine.
Modified residue: 202 202 Phosphothreonine.
Modified residue: 331 331 Phosphotyrosine.
Modified residue: 339 339 Phosphoserine.
Protein Length
351 AA.
Protein Sequence
(Canonical)
MGNAATAKKG SEVESVKEFL AKAKEDFLKK WENPAPNNAG LEDFERKKTL GTGSFGRVML  60
VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEFS FKDNSNLYMV  120
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY  180
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF  240
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT  300
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCGKEFCE F           351
FASTA
(Canonical)
>LipidDB-9823-00867|P05383
MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVML
VKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFAT
TDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCGKEFCEF
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; ISS:UniProtKB
GO:0004691; F:cAMP-dependent protein kinase activity; ISS:UniProtKB
GO:0000287; F:magnesium ion binding; ISS:UniProtKB
GO:0006468; P:protein phosphorylation; ISS:UniProtKB
Interpro
InterPro; IPR000961; AGC-kinase_C
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF00069; Pkinase;
SMART
SMART; SM00133; S_TK_X;
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS51285; AGC_KINASE_CTER;
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS