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P22612

- KAPCG_HUMAN

UniProt

P22612 - KAPCG_HUMAN

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
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    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. 8 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.
    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_dom.
    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

    MGNAPAKKDT EQEESVNEFL AKARGDFLYR WGNPAQNTAS SDQFERLRTL    50
    GMGSFGRVML VRHQETGGHY AMKILNKQKV VKMKQVEHIL NEKRILQAID 100
    FPFLVKLQFS FKDNSYLYLV MEYVPGGEMF SRLQRVGRFS EPHACFYAAQ 150
    VVLAVQYLHS LDLIHRDLKP ENLLIDQQGY LQVTDFGFAK RVKGRTWTLC 200
    GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAVGFPPFY ADQPIQIYEK 250
    IVSGRVRFPS KLSSDLKHLL RSLLQVDLTK RFGNLRNGVG DIKNHKWFAT 300
    TSWIAIYEKK VEAPFIPKYT GPGDASNFDD YEEEELRISI NEKCAKEFSE 350
    F 351
    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. 8 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

    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.
    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_dom.
    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

    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 1, 2014
    This is version 144 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