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Protein

Protein kinase C gamma type

Gene

PRKCG

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

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. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Ca2+Note: Binds 3 Ca2+ 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

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein kinase C activity Source: Ensembl
  • protein kinase activity Source: HGNC
  • protein kinase C activity Source: ProtInc
  • protein serine/threonine/tyrosine kinase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms

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_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_19333. G alpha (z) signalling events.
REACT_263890. WNT5A-dependent internalization of FZD4.
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 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 14 (SCA14)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionSpinocerebellar 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).

See also OMIM:605361
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.

Chemistry

DrugBankiDB00675. Tamoxifen.

Polymorphism and mutation databases

BioMutaiPRKCG.
DMDMi462455.

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 PDPK1By similarity
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

BgeeiP05129.
CleanExiHS_PRKCG.
ExpressionAtlasiP05129. baseline and differential.
GenevisibleiP05129. HS.

Organism-specific databases

HPAiCAB013051.
HPA047870.
HPA054560.

Interactioni

Subunit structurei

Interacts with GRIA4 (By similarity). Interacts with CDCP1. Interacts with TP53INP1 and p53/TP53. Interacts with ARNTL/BMAL1 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi111568. 33 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 – 523Combined sources
Beta strandi57 – 593Combined sources
Turni67 – 693Combined sources
Helixi75 – 806Combined sources
Turni86 – 894Combined sources
Beta strandi160 – 16910Combined sources
Beta strandi172 – 18211Combined sources
Beta strandi194 – 2018Combined sources
Beta strandi222 – 2309Combined sources
Helixi233 – 2375Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi254 – 2629Combined sources
Helixi263 – 2686Combined sources
Beta strandi271 – 2766Combined sources
Helixi280 – 2834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120449.
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.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase.
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. AlignAdd to basket

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

        10         20         30         40         50
MAGLGPGVGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS
60 70 80 90 100
HCTDFIWGIG KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK
110 120 130 140 150
HKFRLHSYSS PTFCDHCGSL LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC
160 170 180 190 200
GVDHTERRGR LQLEIRAPTA DEIHVTVGEA RNLIPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPRNLTKQ KTRTVKATLN PVWNETFVFN LKPGDVERRL SVEVWDWDRT
260 270 280 290 300
SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ
310 320 330 340 350
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDPKRCFFG ASPGRLHISD
360 370 380 390 400
FSFLMVLGKG SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK
410 420 430 440 450
RVLALGGRGP GGRPHFLTQL HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG
460 470 480 490 500
KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD LKLDNVMLDA EGHIKITDFG
510 520 530 540 550
MCKENVFPGT TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS FGVLLYEMLA
560 570 580 590 600
GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS
610 620 630 640 650
GPDGEPTIRA HGFFRWIDWE RLERLEIPPP FRPRPCGRSG ENFDKFFTRA
660 670 680 690
APALTPPDRL VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM
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:
EMBLi
GenBanki
DDBJi
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. [P05129-1]
PIRiD24664.
RefSeqiNP_002730.1. NM_002739.3. [P05129-1]
UniGeneiHs.631564.

Genome annotation databases

EnsembliENST00000263431; ENSP00000263431; ENSG00000126583. [P05129-1]
GeneIDi5582.
KEGGihsa:5582.
UCSCiuc002qcq.1. human. [P05129-1]

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:
EMBLi
GenBanki
DDBJi
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. [P05129-1]
PIRiD24664.
RefSeqiNP_002730.1. NM_002739.3. [P05129-1]
UniGeneiHs.631564.

3D structure databases

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

Protein-protein interaction databases

BioGridi111568. 33 interactions.
DIPiDIP-39795N.
IntActiP05129. 7 interactions.
MINTiMINT-222801.
STRINGi9606.ENSP00000263431.

Chemistry

BindingDBiP05129.
ChEMBLiCHEMBL2093867.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1484.

PTM databases

PhosphoSiteiP05129.

Polymorphism and mutation databases

BioMutaiPRKCG.
DMDMi462455.

Proteomic databases

PaxDbiP05129.
PeptideAtlasiP05129.
PRIDEiP05129.

Protocols and materials databases

DNASUi5582.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263431; ENSP00000263431; ENSG00000126583. [P05129-1]
GeneIDi5582.
KEGGihsa:5582.
UCSCiuc002qcq.1. human. [P05129-1]

Organism-specific databases

CTDi5582.
GeneCardsiGC19P054382.
GeneReviewsiPRKCG.
HGNCiHGNC:9402. PRKCG.
HPAiCAB013051.
HPA047870.
HPA054560.
MIMi176980. gene.
605361. phenotype.
neXtProtiNX_P05129.
Orphaneti98763. Spinocerebellar ataxia type 14.
PharmGKBiPA33766.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOVERGENiHBG108317.
InParanoidiP05129.
KOiK02677.
OrthoDBiEOG77M8QM.
PhylomeDBiP05129.
TreeFamiTF351133.

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_1178. Disinhibition of SNARE formation.
REACT_1280. Response to elevated platelet cytosolic Ca2+.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_19333. G alpha (z) signalling events.
REACT_263890. WNT5A-dependent internalization of FZD4.
REACT_9000. Calmodulin induced events.
SignaLinkiP05129.

Miscellaneous databases

EvolutionaryTraceiP05129.
GeneWikiiPRKCG.
GenomeRNAii5582.
NextBioi21648.
PMAP-CutDBP05129.
PROiP05129.
SOURCEiSearch...

Gene expression databases

BgeeiP05129.
CleanExiHS_PRKCG.
ExpressionAtlasiP05129. baseline and differential.
GenevisibleiP05129. HS.

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.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 182 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.