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P22612

- KAPCG_HUMAN

UniProt

P22612 - KAPCG_HUMAN

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Protein

cAMP-dependent protein kinase catalytic subunit gamma

Gene

PRKACG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Phosphorylates a large number of substrates in the cytoplasm and the nucleus.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by cAMP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATPPROSITE-ProRule annotation
Active sitei167 – 1671Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 589ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase activity Source: ProtInc

GO - Biological processi

  1. activation of phospholipase C activity Source: Reactome
  2. activation of protein kinase A activity Source: Reactome
  3. blood coagulation Source: Reactome
  4. carbohydrate metabolic process Source: Reactome
  5. cellular response to glucagon stimulus Source: Reactome
  6. energy reserve metabolic process Source: Reactome
  7. epidermal growth factor receptor signaling pathway Source: Reactome
  8. fibroblast growth factor receptor signaling pathway Source: Reactome
  9. gluconeogenesis Source: Reactome
  10. glucose metabolic process Source: Reactome
  11. innate immune response Source: Reactome
  12. intracellular signal transduction Source: Reactome
  13. male gonad development Source: ProtInc
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. regulation of insulin secretion Source: Reactome
  16. signal transduction Source: Reactome
  17. small molecule metabolic process Source: Reactome
  18. spermatogenesis Source: ProtInc
  19. transmembrane transport Source: Reactome
  20. triglyceride catabolic process Source: Reactome
  21. water transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.11. 2681.
ReactomeiREACT_1520. Gluconeogenesis.
REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
REACT_15334. DARPP-32 events.
REACT_15497. PKA-mediated phosphorylation of CREB.
REACT_15530. PKA activation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18325. Regulation of insulin secretion.
REACT_1946. PKA activation in glucagon signalling.
REACT_20625. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23898. Rap1 signalling.
REACT_24023. Regulation of water balance by renal Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
SignaLinkiP22612.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase catalytic subunit gamma (EC:2.7.11.11)
Short name:
PKA C-gamma
Gene namesi
Name:PRKACG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:9382. PRKACG.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 351350cAMP-dependent protein kinase catalytic subunit gammaPRO_0000086064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei198 – 1981Phosphothreonine; by autocatalysisBy similarity
Modified residuei339 – 3391Phosphoserine; by autocatalysisBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP22612.
PaxDbiP22612.
PRIDEiP22612.

PTM databases

PhosphoSiteiP22612.

Expressioni

Tissue specificityi

Testis specific. But important tissues such as brain and ovary have not been analyzed for the content of transcript.

Gene expression databases

BgeeiP22612.
CleanExiHS_PRKACG.
GenevestigatoriP22612.

Organism-specific databases

HPAiCAB004530.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi111555. 11 interactions.
IntActiP22612. 3 interactions.
MINTiMINT-3009782.
STRINGi9606.ENSP00000366488.

Structurei

3D structure databases

ProteinModelPortaliP22612.
SMRiP22612. Positions 14-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 298255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35153AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074358.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP22612.
KOiK04345.
OMAiFHEPDIT.
OrthoDBiEOG7VX8WD.
PhylomeDBiP22612.
TreeFamiTF313399.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22612-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGNAPAKKDT EQEESVNEFL AKARGDFLYR WGNPAQNTAS SDQFERLRTL
60 70 80 90 100
GMGSFGRVML VRHQETGGHY AMKILNKQKV VKMKQVEHIL NEKRILQAID
110 120 130 140 150
FPFLVKLQFS FKDNSYLYLV MEYVPGGEMF SRLQRVGRFS EPHACFYAAQ
160 170 180 190 200
VVLAVQYLHS LDLIHRDLKP ENLLIDQQGY LQVTDFGFAK RVKGRTWTLC
210 220 230 240 250
GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAVGFPPFY ADQPIQIYEK
260 270 280 290 300
IVSGRVRFPS KLSSDLKHLL RSLLQVDLTK RFGNLRNGVG DIKNHKWFAT
310 320 330 340 350
TSWIAIYEKK VEAPFIPKYT GPGDASNFDD YEEEELRISI NEKCAKEFSE

F
Length:351
Mass (Da):40,434
Last modified:January 23, 2007 - v3
Checksum:iE66BB4BFB8AF9B50
GO

Sequence cautioni

The sequence AAC41690.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451A → P in AAH39888. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti251 – 2511I → N.1 Publication
VAR_040595
Natural varianti268 – 2681H → D.3 Publications
Corresponds to variant rs3730386 [ dbSNP | Ensembl ].
VAR_033902

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6625.1.
PIRiB34724. OKHUCG.
RefSeqiNP_002723.2. NM_002732.3.
UniGeneiHs.158029.

Genome annotation databases

EnsembliENST00000377276; ENSP00000366488; ENSG00000165059.
GeneIDi5568.
KEGGihsa:5568.
UCSCiuc004agy.3. human.

Polymorphism databases

DMDMi33860173.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6625.1.
PIRi B34724. OKHUCG.
RefSeqi NP_002723.2. NM_002732.3.
UniGenei Hs.158029.

3D structure databases

ProteinModelPortali P22612.
SMRi P22612. Positions 14-351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111555. 11 interactions.
IntActi P22612. 3 interactions.
MINTi MINT-3009782.
STRINGi 9606.ENSP00000366488.

Chemistry

BindingDBi P22612.
ChEMBLi CHEMBL2094138.
GuidetoPHARMACOLOGYi 1478.

PTM databases

PhosphoSitei P22612.

Polymorphism databases

DMDMi 33860173.

Proteomic databases

MaxQBi P22612.
PaxDbi P22612.
PRIDEi P22612.

Protocols and materials databases

DNASUi 5568.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377276 ; ENSP00000366488 ; ENSG00000165059 .
GeneIDi 5568.
KEGGi hsa:5568.
UCSCi uc004agy.3. human.

Organism-specific databases

CTDi 5568.
GeneCardsi GC09M071627.
H-InvDB HIX0025746.
HGNCi HGNC:9382. PRKACG.
HPAi CAB004530.
MIMi 176893. gene.
neXtProti NX_P22612.
PharmGKBi PA33750.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074358.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi P22612.
KOi K04345.
OMAi FHEPDIT.
OrthoDBi EOG7VX8WD.
PhylomeDBi P22612.
TreeFami TF313399.

Enzyme and pathway databases

BRENDAi 2.7.11.11. 2681.
Reactomei REACT_1520. Gluconeogenesis.
REACT_1525. PKA-mediated phosphorylation of key metabolic factors.
REACT_15334. DARPP-32 events.
REACT_15497. PKA-mediated phosphorylation of CREB.
REACT_15530. PKA activation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18325. Regulation of insulin secretion.
REACT_1946. PKA activation in glucagon signalling.
REACT_20625. CREB phosphorylation through the activation of Adenylate Cyclase.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23898. Rap1 signalling.
REACT_24023. Regulation of water balance by renal Aquaporins.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.
SignaLinki P22612.

Miscellaneous databases

GeneWikii PRKACG.
GenomeRNAii 5568.
NextBioi 21578.
PROi P22612.
SOURCEi Search...

Gene expression databases

Bgeei P22612.
CleanExi HS_PRKACG.
Genevestigatori P22612.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiKAPCG_HUMAN
AccessioniPrimary (citable) accession number: P22612
Secondary accession number(s): O60850, Q5VZ02, Q86YI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3