Tag | Content |
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CPLM ID | CPLM-009849 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | cAMP-dependent protein kinase catalytic subunit beta |
Protein Synonyms/Alias | PKA C-beta |
Gene Name | Prkacb |
Gene Synonyms/Alias | Pkacb |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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24 | KEFLAKAKEDFLRKW | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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. NP_BIND 50 58 ATP (By similarity). ACT_SITE 167 167 Proton acceptor (By similarity). BINDING 73 73 ATP (By similarity). MOD_RES 3 3 Deamidated asparagine (By similarity). MOD_RES 11 11 Phosphoserine (By similarity). MOD_RES 49 49 Phosphothreonine (By similarity). MOD_RES 69 69 Phosphotyrosine (By similarity). MOD_RES 140 140 Phosphoserine (By similarity). MOD_RES 196 196 Phosphothreonine (By similarity). MOD_RES 198 198 Phosphothreonine (By similarity). MOD_RES 202 202 Phosphothreonine (By similarity). MOD_RES 331 331 Phosphotyrosine (By similarity). MOD_RES 339 339 Phosphoserine (By similarity). LIPID 2 2 N-myristoyl glycine (By similarity). |
Keyword | ATP-binding; cAMP; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 351 AA |
Protein Sequence | MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL GTGSFGRVML 60 VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE FPFLVRLEYS 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 YEEEEIRVSI TEKCGKEFCE F 351 |
Gene Ontology | GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD. GO:0005813; C:centrosome; IEA:Compara. GO:0005829; C:cytosol; TAS:Reactome. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0034237; F:protein kinase A regulatory subunit binding; IC:RGD. GO:0051447; P:negative regulation of meiotic cell cycle; IDA:RGD. GO:0097338; P:response to clozapine; IEP:RGD. |
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