P22612 (KAPCG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

PRKACG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
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.
Tissue specificity	Testis specific. But important tissues such as brain and ovary have not been analyzed for the content of transcript.
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.
Sequence caution	The sequence AAC41690.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of phospholipase C activity Traceable author statement. Source: Reactome activation of protein kinase A activity Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cellular response to glucagon stimulus Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome gluconeogenesis Traceable author statement. Source: Reactome intracellular protein kinase cascade Traceable author statement. Source: Reactome male gonad development Traceable author statement Ref.2. Source: ProtInc nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome spermatogenesis Traceable author statement Ref.2. Source: ProtInc transmembrane transport Traceable author statement. Source: Reactome triglyceride catabolic process Traceable author statement. Source: Reactome water transport Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 351	350	cAMP-dependent protein kinase catalytic subunit gamma		PRO_0000086064
Regions
	Domain	44 – 298	255	Protein kinase
	Domain	299 – 351	53	AGC-kinase C-terminal
	Nucleotide binding	50 – 58	9	ATP By similarity
Sites
	Active site	167	1	Proton acceptor By similarity
	Binding site	73	1	ATP By similarity
Amino acid modifications
	Modified residue	198	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	339	1	Phosphoserine; by autocatalysis By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
Natural variations
	Natural variant	251	1	I → N. Ref.6		VAR_040595
	Natural variant	268	1	H → D. Ref.1 Ref.3 Ref.6 Corresponds to variant rs3730386 [ dbSNP | Ensembl ].		VAR_033902
Experimental info
	Sequence conflict	345	1	A → P in AAH39888. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P22612 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E66BB4BFB8AF9B50	FASTA	351	40,434
	10 20 30 40 50 60 MGNAPAKKDT EQEESVNEFL AKARGDFLYR WGNPAQNTAS SDQFERLRTL GMGSFGRVML 70 80 90 100 110 120 VRHQETGGHY AMKILNKQKV VKMKQVEHIL NEKRILQAID FPFLVKLQFS FKDNSYLYLV 130 140 150 160 170 180 MEYVPGGEMF SRLQRVGRFS EPHACFYAAQ VVLAVQYLHS LDLIHRDLKP ENLLIDQQGY 190 200 210 220 230 240 LQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAVGFPPFY 250 260 270 280 290 300 ADQPIQIYEK IVSGRVRFPS KLSSDLKHLL RSLLQVDLTK RFGNLRNGVG DIKNHKWFAT 310 320 330 340 350 TSWIAIYEKK VEAPFIPKYT GPGDASNFDD YEEEELRISI NEKCAKEFSE F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis -- representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase." Beebe S.J., Oyen O., Sandberg M., Froysa A., Hansson V., Jahnsen T. Mol. Endocrinol. 4:465-475(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-268. Tissue: Testis.
[2]	"The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon." Reinton N., Haugen T.B., Orstavik S., Skalhegg B.S., Hansson V., Jahnsen T., Tasken K. Genomics 49:290-297(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	SeattleSNPs variation discovery resource Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-268.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Brain.
[6]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-251 AND ASP-268.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34182 mRNA. Translation: AAC41690.1. Different initiation. AJ001597 Genomic DNA. Translation: CAA04863.1. DQ667175 Genomic DNA. Translation: ABG25920.1. AL162730 Genomic DNA. Translation: CAH71828.1. BC039888 mRNA. Translation: AAH39888.1.
IPI	IPI00219592.
PIR	OKHUCG. B34724.
RefSeq	NP_002723.2. NM_002732.3.
UniGene	Hs.158029.
3D structure databases
ProteinModelPortal	P22612.
ModBase	Search...
Protein-protein interaction databases
IntAct	P22612. 3 interactions.
STRING	9606.ENSP00000366488.
PTM databases
PhosphoSite	P22612.
Polymorphism databases
DMDM	33860173.
Proteomic databases
PaxDb	P22612.
PRIDE	P22612.
Protocols and materials databases
DNASU	5568.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377276; ENSP00000366488; ENSG00000165059.
GeneID	5568.
KEGG	hsa:5568.
UCSC	uc004agy.3. human.
Organism-specific databases
CTD	5568.
GeneCards	GC09M071627.
H-InvDB	HIX0025746.
HGNC	HGNC:9382. PRKACG.
HPA	CAB004530.
MIM	176893. gene.
neXtProt	NX_P22612.
PharmGKB	PA33750.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
InParanoid	P22612.
KO	K04345.
OMA	RFYAMKV.
OrthoDB	EOG4J118D.
PhylomeDB	P22612.
Enzyme and pathway databases
BRENDA	2.7.11.11. 2681.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
Bgee	P22612.
CleanEx	HS_PRKACG.
Genevestigator	P22612.
GermOnline	ENSG00000165059. Homo sapiens.
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	P22612.
ChEMBL	CHEMBL2743.
GenomeRNAi	5568.
NextBio	21578.
SOURCE	Search...

Entry information

Entry name

KAPCG_HUMAN

Accession

Primary (citable) accession number: P22612
Secondary accession number(s): O60850, Q5VZ02, Q86YI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.