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P05129

- KPCG_HUMAN

UniProt

P05129 - KPCG_HUMAN

Protein

Protein kinase C gamma type

Gene

PRKCG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 3 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress By similarity. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage.By similarity1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Binds 3 calcium ions per subunit. The ions are bound to the C2 domain.

    Enzyme regulationi

    Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-514 (activation loop of the kinase domain), Thr-655 (turn motif) and Thr-674 (hydrophobic region), need to be phosphorylated for its full activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi186 – 1861Calcium 1; via carbonyl oxygen
    Metal bindingi187 – 1871Calcium 1
    Metal bindingi187 – 1871Calcium 2
    Metal bindingi193 – 1931Calcium 2
    Metal bindingi246 – 2461Calcium 1
    Metal bindingi246 – 2461Calcium 2
    Metal bindingi247 – 2471Calcium 2; via carbonyl oxygen
    Metal bindingi248 – 2481Calcium 1
    Metal bindingi248 – 2481Calcium 2
    Metal bindingi248 – 2481Calcium 3
    Metal bindingi251 – 2511Calcium 3
    Metal bindingi252 – 2521Calcium 3; via carbonyl oxygen
    Metal bindingi254 – 2541Calcium 1
    Metal bindingi254 – 2541Calcium 3
    Binding sitei380 – 3801ATPPROSITE-ProRule annotation
    Active sitei480 – 4801Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri35 – 8551Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri100 – 15051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi357 – 3659ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium-dependent protein kinase C activity Source: Ensembl
    3. protein kinase activity Source: HGNC
    4. protein kinase C activity Source: ProtInc
    5. protein serine/threonine/tyrosine kinase activity Source: MGI
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. blood coagulation Source: Reactome
    3. cell death Source: UniProtKB-KW
    4. chemosensory behavior Source: Ensembl
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. fibroblast growth factor receptor signaling pathway Source: Reactome
    7. innate immune response Source: Reactome
    8. innervation Source: Ensembl
    9. intracellular signal transduction Source: InterPro
    10. learning or memory Source: Ensembl
    11. negative regulation of neuron apoptotic process Source: UniProtKB
    12. negative regulation of protein catabolic process Source: HGNC
    13. negative regulation of protein ubiquitination Source: HGNC
    14. neurotrophin TRK receptor signaling pathway Source: Reactome
    15. phosphorylation Source: HGNC
    16. platelet activation Source: Reactome
    17. positive regulation of mismatch repair Source: HGNC
    18. protein autophosphorylation Source: Ensembl
    19. protein phosphorylation Source: ProtInc
    20. response to morphine Source: UniProtKB
    21. response to pain Source: UniProtKB
    22. signal transduction Source: Reactome
    23. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_1178. Disinhibition of SNARE formation.
    REACT_1280. Response to elevated platelet cytosolic Ca2+.
    REACT_172599. WNT5A-dependent internalization of FZD4.
    REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    REACT_19333. G alpha (z) signalling events.
    REACT_9000. Calmodulin induced events.
    SignaLinkiP05129.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C gamma type (EC:2.7.11.13)
    Short name:
    PKC-gamma
    Gene namesi
    Name:PRKCG
    Synonyms:PKCG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9402. PRKCG.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectiondendrite By similarity
    Note: Translocates to synaptic membranes on stimulation.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytosol Source: UniProtKB
    3. dendrite Source: UniProtKB
    4. nucleus Source: Ensembl
    5. perinuclear region of cytoplasm Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. synaptic membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia 14 (SCA14) [MIM:605361]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA14 is an autosomal dominant cerebellar ataxia (ADCA).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011H → Y in SCA14. 1 Publication
    VAR_017060
    Natural varianti119 – 1191S → P in SCA14. 1 Publication
    VAR_017061
    Natural varianti128 – 1281G → D in SCA14. 1 Publication
    VAR_017062

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi605361. phenotype.
    Orphaneti98763. Spinocerebellar ataxia type 14.
    PharmGKBiPA33766.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 697697Protein kinase C gamma typePRO_0000055689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
    Modified residuei514 – 5141Phosphothreonine; by PDPK1Curated
    Modified residuei648 – 6481Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei655 – 6551Phosphothreonine; by autocatalysisBy similarity
    Modified residuei674 – 6741Phosphothreonine; by autocatalysisBy similarity
    Modified residuei675 – 6751Phosphotyrosine; by SYKBy similarity

    Post-translational modificationi

    Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4.By similarity
    Ubiquitinated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP05129.
    PeptideAtlasiP05129.
    PRIDEiP05129.

    PTM databases

    PhosphoSiteiP05129.

    Miscellaneous databases

    PMAP-CutDBP05129.

    Expressioni

    Tissue specificityi

    Expressed in Purkinje cells of the cerebellar cortex.1 Publication

    Gene expression databases

    ArrayExpressiP05129.
    BgeeiP05129.
    CleanExiHS_PRKCG.
    GenevestigatoriP05129.

    Organism-specific databases

    HPAiCAB013051.

    Interactioni

    Subunit structurei

    Interacts with GRIA4 By similarity. Interacts with CDCP1. Interacts with TP53INP1 and p53/TP53.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi111568. 24 interactions.
    DIPiDIP-39795N.
    IntActiP05129. 7 interactions.
    MINTiMINT-222801.
    STRINGi9606.ENSP00000263431.

    Structurei

    Secondary structure

    1
    697
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni50 – 523
    Beta strandi57 – 593
    Turni67 – 693
    Helixi75 – 806
    Turni86 – 894
    Beta strandi160 – 16910
    Beta strandi172 – 18211
    Beta strandi194 – 2018
    Beta strandi222 – 2309
    Helixi233 – 2375
    Beta strandi239 – 2468
    Beta strandi249 – 2513
    Beta strandi254 – 2629
    Helixi263 – 2686
    Beta strandi271 – 2766
    Helixi280 – 2834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E73NMR-A36-105[»]
    2UZPX-ray2.00A/B/C154-295[»]
    ProteinModelPortaliP05129.
    SMRiP05129. Positions 36-683.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05129.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini170 – 26091C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 614264Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 68571AGC-kinase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri35 – 8551Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri100 – 15051Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108317.
    InParanoidiP05129.
    KOiK02677.
    OrthoDBiEOG77M8QM.
    PhylomeDBiP05129.
    TreeFamiTF351133.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00130. C1_1. 2 hits.
    PF00168. C2. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000550. PKC_alpha. 1 hit.
    PRINTSiPR00360. C2DOMAIN.
    PR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS50004. C2. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05129-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGLGPGVGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS    50
    HCTDFIWGIG KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK 100
    HKFRLHSYSS PTFCDHCGSL LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC 150
    GVDHTERRGR LQLEIRAPTA DEIHVTVGEA RNLIPMDPNG LSDPYVKLKL 200
    IPDPRNLTKQ KTRTVKATLN PVWNETFVFN LKPGDVERRL SVEVWDWDRT 250
    SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ 300
    KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDPKRCFFG ASPGRLHISD 350
    FSFLMVLGKG SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK 400
    RVLALGGRGP GGRPHFLTQL HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG 450
    KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD LKLDNVMLDA EGHIKITDFG 500
    MCKENVFPGT TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS FGVLLYEMLA 550
    GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS 600
    GPDGEPTIRA HGFFRWIDWE RLERLEIPPP FRPRPCGRSG ENFDKFFTRA 650
    APALTPPDRL VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM 697
    Length:697
    Mass (Da):78,448
    Last modified:February 1, 1994 - v3
    Checksum:i3F911B5BEF713C41
    GO
    Isoform 2 (identifier: P05129-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MAGLGPGVGDSEGGPRPLFC → MPRICDLRVSRRWEGPPDGR
         21-133: Missing.
         553-588: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:548
    Mass (Da):62,030
    Checksum:iB3234AB0DAC43461
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti314 – 3174RVRM → VSRT in AAA60102. (PubMed:3755548)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti101 – 1011H → Y in SCA14. 1 Publication
    VAR_017060
    Natural varianti119 – 1191S → P in SCA14. 1 Publication
    VAR_017061
    Natural varianti128 – 1281G → D in SCA14. 1 Publication
    VAR_017062
    Natural varianti141 – 1411R → C.1 Publication
    VAR_008755
    Natural varianti415 – 4151H → Q.1 Publication
    VAR_008756
    Natural varianti523 – 5231A → D.1 Publication
    VAR_008757
    Natural varianti659 – 6591R → S.1 Publication
    VAR_008758

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020MAGLG…RPLFC → MPRICDLRVSRRWEGPPDGR in isoform 2. 1 PublicationVSP_056467Add
    BLAST
    Alternative sequencei21 – 133113Missing in isoform 2. 1 PublicationVSP_056468Add
    BLAST
    Alternative sequencei553 – 58836Missing in isoform 2. 1 PublicationVSP_056469Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF345987 mRNA. Translation: AAK13533.1.
    AK303741 mRNA. Translation: BAH14036.1.
    AC008440 Genomic DNA. No translation available.
    BC047876 mRNA. Translation: AAH47876.1.
    M13977 mRNA. Translation: AAA60102.1.
    Z15114 mRNA. Translation: CAA78820.1.
    CCDSiCCDS12867.1.
    PIRiD24664.
    RefSeqiNP_002730.1. NM_002739.3.
    UniGeneiHs.631564.

    Genome annotation databases

    EnsembliENST00000263431; ENSP00000263431; ENSG00000126583.
    ENST00000542049; ENSP00000438090; ENSG00000126583.
    GeneIDi5582.
    KEGGihsa:5582.
    UCSCiuc002qcq.1. human.

    Polymorphism databases

    DMDMi462455.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Mutations of the PRKCG gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF345987 mRNA. Translation: AAK13533.1 .
    AK303741 mRNA. Translation: BAH14036.1 .
    AC008440 Genomic DNA. No translation available.
    BC047876 mRNA. Translation: AAH47876.1 .
    M13977 mRNA. Translation: AAA60102.1 .
    Z15114 mRNA. Translation: CAA78820.1 .
    CCDSi CCDS12867.1.
    PIRi D24664.
    RefSeqi NP_002730.1. NM_002739.3.
    UniGenei Hs.631564.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E73 NMR - A 36-105 [» ]
    2UZP X-ray 2.00 A/B/C 154-295 [» ]
    ProteinModelPortali P05129.
    SMRi P05129. Positions 36-683.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111568. 24 interactions.
    DIPi DIP-39795N.
    IntActi P05129. 7 interactions.
    MINTi MINT-222801.
    STRINGi 9606.ENSP00000263431.

    Chemistry

    BindingDBi P05129.
    ChEMBLi CHEMBL2093867.
    GuidetoPHARMACOLOGYi 1484.

    PTM databases

    PhosphoSitei P05129.

    Polymorphism databases

    DMDMi 462455.

    Proteomic databases

    PaxDbi P05129.
    PeptideAtlasi P05129.
    PRIDEi P05129.

    Protocols and materials databases

    DNASUi 5582.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263431 ; ENSP00000263431 ; ENSG00000126583 .
    ENST00000542049 ; ENSP00000438090 ; ENSG00000126583 .
    GeneIDi 5582.
    KEGGi hsa:5582.
    UCSCi uc002qcq.1. human.

    Organism-specific databases

    CTDi 5582.
    GeneCardsi GC19P054382.
    GeneReviewsi PRKCG.
    HGNCi HGNC:9402. PRKCG.
    HPAi CAB013051.
    MIMi 176980. gene.
    605361. phenotype.
    neXtProti NX_P05129.
    Orphaneti 98763. Spinocerebellar ataxia type 14.
    PharmGKBi PA33766.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108317.
    InParanoidi P05129.
    KOi K02677.
    OrthoDBi EOG77M8QM.
    PhylomeDBi P05129.
    TreeFami TF351133.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    Reactomei REACT_1178. Disinhibition of SNARE formation.
    REACT_1280. Response to elevated platelet cytosolic Ca2+.
    REACT_172599. WNT5A-dependent internalization of FZD4.
    REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    REACT_19333. G alpha (z) signalling events.
    REACT_9000. Calmodulin induced events.
    SignaLinki P05129.

    Miscellaneous databases

    EvolutionaryTracei P05129.
    GeneWikii PRKCG.
    GenomeRNAii 5582.
    NextBioi 21648.
    PMAP-CutDB P05129.
    PROi P05129.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05129.
    Bgeei P05129.
    CleanExi HS_PRKCG.
    Genevestigatori P05129.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR000008. C2_dom.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00130. C1_1. 2 hits.
    PF00168. C2. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000550. PKC_alpha. 1 hit.
    PRINTSi PR00360. C2DOMAIN.
    PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS50004. C2. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cui W.C., Yu L., Chu Y.Y., Wang J., Zheng L.H., Zhou G.J., Zhao S.Y.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Kidney.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Brain.
    5. "Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways."
      Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.
      Science 233:859-866(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-317 (ISOFORM 1).
      Tissue: Brain.
    6. "Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes."
      Kochs G., Hummel R., Meyer D., Hug H., Marme D., Sarre T.F.
      Eur. J. Biochem. 216:597-606(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-697 (ISOFORM 1).
      Tissue: Hippocampus.
    7. "The C2 domain of PKCdelta is a phosphotyrosine binding domain."
      Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.
      Cell 121:271-280(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDCP1.
    8. "Protein kinase C delta regulates Ser46 phosphorylation of p53 tumor suppressor in the apoptotic response to DNA damage."
      Yoshida K., Liu H., Miki Y.
      J. Biol. Chem. 281:5734-5740(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53INP1 AND P53/TP53.
    9. "Protein kinase C gamma (PKC gamma): function of neuron specific isotype."
      Saito N., Shirai Y.
      J. Biochem. 132:683-687(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    10. Cited for: REVIEW ON FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
      Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
      PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    13. "Solution structure of the phorbol esters/diacylglycerol binding domain of protein kinase C gamma."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 36-105.
    14. "Crystal structure of C2 domain of protein kinase C gamma."
      Pike A.C.W., Amos A., Johansson C., Sobott F., Savitsky P., Berridge G., Fedorov O., Umeano C., Gorrec F., Bunkoczi G., Debreczeni J., Von Delft F., Arrowsmith C.H., Edwards A., Weigelt J., Sundstrom M., Knapp S.
      Submitted (APR-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 154-295 IN COMPLEX WITH CALCIUM IONS.
    15. Cited for: VARIANTS CYS-141; GLN-415; ASP-523 AND SER-659.
    16. "No mutations in the coding region of the PRKCG gene in three families with retinitis pigmentosa linked to the RP11 locus on chromosome 19q."
      Dryja T.P., McEvoy J., McGee T.L., Berson E.L.
      Am. J. Hum. Genet. 65:926-928(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SHOWS THAT THE VARIANTS ARE NOT A CAUSE OF RP11.
    17. "Missense mutations in the regulatory domain of PKC gamma: a new mechanism for dominant nonepisodic cerebellar ataxia."
      Chen D.-H., Brkanac Z., Verlinde C.L.M.J., Tan X.-J., Bylenok L., Nochlin D., Matsushita M., Lipe H., Wolff J., Fernandez M., Cimino P.J., Bird T.D., Raskind W.H.
      Am. J. Hum. Genet. 72:839-849(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, VARIANTS SCA14 TYR-101; PRO-119 AND ASP-128.

    Entry informationi

    Entry nameiKPCG_HUMAN
    AccessioniPrimary (citable) accession number: P05129
    Secondary accession number(s): B7Z8Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 174 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3