cAMP-dependent protein kinase catalytic subunit beta

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Reviewed, UniProtKB/Swiss-Prot P68182 (KAPCB_RAT)

Last modified October 13, 2009. Version 58. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	Prkacb
Synonyms:	Pkacb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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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.

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General annotation (Comments)

Function	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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Activated by cAMP.
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. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Translocates into the nucleus (monomeric catalytic subunit) By similarity. The inactive holoenzyme is found in the cytoplasm By similarity.
Post-translational modification	Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form.
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.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Lipoprotein Myristate Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of meiotic cell cycle Inferred from direct assay. Source: RGD protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cAMP-dependent protein kinase complex Inferred from direct assay. Source: RGD insoluble fraction Inferred from direct assay. Source: RGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB cAMP-dependent protein kinase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein kinase A regulatory subunit binding Inferred by curator. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 351

350

cAMP-dependent protein kinase catalytic subunit beta

PRO_0000086063

Regions

Domain

44 – 298

255

Protein kinase

Domain

299 – 351

AGC-kinase C-terminal

Nucleotide binding

50 – 58

ATP By similarity

Sites

Active site

167

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Deamidated asparagine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

198

Phosphothreonine By similarity

Modified residue

267

N6-acetyllysine By similarity

Modified residue

339

Phosphoserine By similarity

Lipidation

N-myristoyl glycine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P68182-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EBAC9B8041DF9F47
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FASTA

351

40,708

        10         20         30         40         50         60 
MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL GTGSFGRVML 

        70         80         90        100        110        120 
VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE FPFLVRLEYS FKDNSNLYMV 

       130        140        150        160        170        180 
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY 

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

       250        260        270        280        290        300 
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT 

       310        320        330        340        350 
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEEIRVSI TEKCGKEFCE F

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References

[1]	"Molecular structure of the C beta catalytic subunit of rat cAMP-dependent protein kinase and differential expression of C alpha and C beta isoforms in rat tissues and cultured cells." Shuntoh H., Sakamoto N., Matsuyama S., Saitoh M., Tanaka C. Biochim. Biophys. Acta 1131:175-180(1992) [PubMed: 1610898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry." Jedrzejewski P.T., Girod A., Tholey A., Koenig N., Thullner S., Kinzel V., Bossemeyer D. Protein Sci. 7:457-469(1998) [PubMed: 9521123] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, DEAMIDATION AT ASN-3.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D10770 mRNA. Translation: BAA01601.1.
IPI	IPI00560492.
PIR	OKRTCB. JQ1139.
RefSeq	NP_001071113.1.
UniGene	Rn.202491
3D structure databases
HSSP	HSSP built from PDB template 1CTP based on UniProtKB P36887.
ModBase	Search...
Protein-protein interaction databases
STRING	P68182.
PTM databases
PhosphoSite	P68182.
Genome annotation databases
Ensembl	ENSRNOT00000045967; ENSRNOP00000043572; ENSRNOG00000004978; Rattus norvegicus. [Genome view]
GeneID	293508.
KEGG	rno:293508.
UCSC	D10770. rat.
Organism-specific databases
CTD	293508.
RGD	1310574. Prkacb.
Phylogenomic databases
HOVERGEN	P68182.
Enzyme and pathway databases
BRENDA	2.7.11.11. 248.
Gene expression databases
ArrayExpress	P68182.
Genevestigator	P68182.
GermOnline	ENSRNOG00000004978. Rattus norvegicus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
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 Resources
NextBio	636274.

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Entry information

Entry name

KAPCB_RAT

Accession

Primary (citable) accession number: P68182
Secondary accession number(s): P05206

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents