Reviewed, UniProtKB/Swiss-Prot P22612 (KAPCG_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Gene Ontology (GO)
Biological process	hormone-mediated signaling Inferred from Experiment. Source: Reactome male gonad development Ref.2 Traceable author statement. Source: ProtInc protein kinase cascade Inferred from Experiment. Source: Reactome spermatogenesis Ref.2 Traceable author statement. Source: ProtInc
Molecular function	cAMP-dependent protein kinase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 351	350	cAMP-dependent protein kinase catalytic subunit gamma
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
	Natural variant	268	1	H → D: dbSNP rs3730386.
Experimental info
	Sequence conflict	345	1	A → P in AAH39888. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P22612-1 [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: 2342480] [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: 9598317] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	SeattleSNPs program for genomic applications 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: 15164053] [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: 15489334] [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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-251 AND ASP-268.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	OKHUCG. B34724.
RefSeq	NP_002723.2.
UniGene	Hs.158029
3D structure databases
HSSP	HSSP built from PDB template 1CTP based on UniProtKB P36887.
SMR	P22612. Positions 13-351.
ModBase	Search...
PTM databases
PhosphoSite	P22612.
Genome annotation databases
Ensembl	ENSG00000165059. Homo sapiens. [Contig view]
GeneID	5568.
KEGG	hsa:5568.
Organism-specific databases
HGNC	HGNC:9382. PRKACG.
HPA	CAB004530.
MIM	176893. gene.
PharmGKB	PA33750.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P22612.
HOVERGEN	P22612.
Enzyme and pathway databases
Reactome	REACT_1505. Integration of energy metabolism. REACT_602. Lipid and lipoprotein metabolism.
Gene expression databases
ArrayExpress	P22612.
CleanEx	HS_PRKACG.
GermOnline	ENSG00000165059. Homo sapiens.
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]
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]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	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:	July 22, 2008
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)