Protein kinase C gamma type - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P05129 (KPCG_HUMAN)

Last modified July 7, 2009. Version 115. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Protein kinase C gamma type
      Short name=PKC-gamma
    EC=2.7.11.13

Gene names

Name:	PRKCG
Synonyms:	PKCG

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	697 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.
Subunit structure	Interacts with CDCP1. Ref.5
Involvement in disease	Defects in PRKCG are the cause of spinocerebellar ataxia type 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). Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

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Ontologies

Keywords
Coding sequence diversity	Polymorphism
Disease	Disease mutation Neurodegeneration Spinocerebellar ataxia
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell death Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro negative regulation of protein catabolic process Inferred from direct assay. Source: HGNC negative regulation of protein ubiquitination Inferred from direct assay. Source: HGNC positive regulation of mismatch repair Inferred from direct assay. Source: HGNC protein amino acid phosphorylation Ref.3 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase C activity Ref.3 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 697

697

Protein kinase C gamma type

PRO_0000055689

Regions

Domain

170 – 260

Domain

351 – 614

264

Protein kinase

Domain

615 – 685

AGC-kinase C-terminal

Zinc finger

35 – 85

Phorbol-ester/DAG-type 1

Zinc finger

100 – 150

Phorbol-ester/DAG-type 2

Nucleotide binding

357 – 365

ATP By similarity

Sites

Active site

480

Proton acceptor By similarity

Metal binding

186

Calcium 1; via carbonyl oxygen By similarity

Metal binding

187

Calcium 1 By similarity

Metal binding

187

Calcium 2 By similarity

Metal binding

193

Calcium 2 By similarity

Metal binding

246

Calcium 1 By similarity

Metal binding

246

Calcium 2 By similarity

Metal binding

247

Calcium 2; via carbonyl oxygen By similarity

Metal binding

248

Calcium 1 By similarity

Metal binding

248

Calcium 2 By similarity

Metal binding

248

Calcium 3 By similarity

Metal binding

251

Calcium 3 By similarity

Metal binding

252

Calcium 3; via carbonyl oxygen By similarity

Metal binding

254

Calcium 1 By similarity

Metal binding

254

Calcium 3 By similarity

Binding site

380

ATP By similarity

Amino acid modifications

Modified residue

195

Phosphotyrosine Ref.6

Modified residue

312

Phosphotyrosine By similarity

Modified residue

322

Phosphoserine By similarity

Modified residue

330

Phosphoserine By similarity

Modified residue

514

Phosphothreonine Ref.8

Modified residue

518

Phosphothreonine By similarity

Modified residue

648

Phosphothreonine; by autocatalysis Potential

Modified residue

655

Phosphothreonine; by autocatalysis Potential

Modified residue

687

Phosphoserine By similarity

Natural variations

Natural variant

101

H → Y in SCA14. Ref.12

VAR_017060

Natural variant

119

S → P in SCA14. Ref.12

VAR_017061

Natural variant

128

G → D in SCA14. Ref.12

VAR_017062

Natural variant

141

R → C Ref.10

VAR_008755

Natural variant

415

H → Q Ref.10

VAR_008756

Natural variant

523

A → D Ref.10

VAR_008757

Natural variant

659

R → S Ref.10

VAR_008758

Secondary structure

697

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P05129-1 [UniParc].

Last modified February 1, 1994. Version 3.
Checksum: 3F911B5BEF713C41
Show »

FASTA

697

78,448

        10         20         30         40         50         60 
MAGLGPGVGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG 

        70         80         90        100        110        120 
KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL 

       130        140        150        160        170        180 
LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTA DEIHVTVGEA 

       190        200        210        220        230        240 
RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTRTVKATLN PVWNETFVFN LKPGDVERRL 

       250        260        270        280        290        300 
SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ 

       310        320        330        340        350        360 
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDPKRCFFG ASPGRLHISD FSFLMVLGKG 

       370        380        390        400        410        420 
SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL 

       430        440        450        460        470        480 
HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD 

       490        500        510        520        530        540 
LKLDNVMLDA EGHIKITDFG MCKENVFPGT TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS 

       550        560        570        580        590        600 
FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS 

       610        620        630        640        650        660 
GPDGEPTIRA HGFFRWIDWE RLERLEIPPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL 

       670        680        690 
VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"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: 3755548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-318. Tissue: Brain.
[4]	"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: 8375396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-697. Tissue: Hippocampus.
[5]	"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: 15851033] [Abstract] Cited for: INTERACTION WITH CDCP1.
[6]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, MASS SPECTROMETRY.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-655, MASS SPECTROMETRY.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, MASS SPECTROMETRY.
[9]	"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.
[10]	"Segregation of a PRKCG mutation in two RP11 families." Al-Maghtheh M., Vithana E.N., Inglehearn C.F., Moore T., Bird A.C., Bhattacharya S.S. Am. J. Hum. Genet. 62:1248-1252(1998) [PubMed: 9545390] [Abstract] Cited for: VARIANTS CYS-141; GLN-415; ASP-523 AND SER-659.
[11]	"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: 10441600] [Abstract] Cited for: SHOWS THAT THE VARIANTS ARE NOT A CAUSE OF RP11.
[12]	"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: 12644968] [Abstract] Cited for: VARIANTS SCA14 TYR-101; PRO-119 AND ASP-128.
+	Additional computationally mapped references.

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Web resources

Mutations of the PRKCG gene

Retina International's Scientific Newsletter

GeneReviews

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Cross-references

Sequence databases

AF345987 mRNA. Translation: AAK13533.1.
BC047876 mRNA. Translation: AAH47876.1.
M13977 mRNA. Translation: AAA60102.1. Different termination.
Z15114 mRNA. Translation: CAA78820.1.

IPI

IPI00007128.

PIR

D24664.

RefSeq

NP_002730.1.

UniGene

Hs.631564

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E73	NMR	-	A	36-105	[»]
2UZP	X-ray	2.00	A/B/C	154-295	[»]

SMR

P05129. Positions 93-158, 348-683.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05129. 5 interactions.

PTM databases

PhosphoSite

P05129.

Proteomic databases

PeptideAtlas

P05129.

PRIDE

P05129.

Genome annotation databases

Ensembl

ENSG00000126583. Homo sapiens. [Contig view]

GeneID

5582.

KEGG

hsa:5582.

UCSC

uc002qcq.1. human.

Organism-specific databases

GeneCards

GC19P059077.

H-InvDB

HIX0027463.

HGNC

HGNC:9402. PRKCG.

HPA

CAB013051.

MIM

176980. gene.
605361. phenotype.

Orphanet

98763. Ataxia, spinocerebellar, type 14.
99. Autosomal dominant cerebellar ataxia.

PharmGKB

PA33766.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P05129.

HOVERGEN

P05129.

OMA

P05129. ICKGFLT.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

endothelinpathway. Endothelins.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
txa2pathway. Thromboxane A2 receptor signaling.

Gene expression databases

ArrayExpress

P05129.

Bgee

P05129.

CleanEx

HS_PRKCG.

GermOnline

ENSG00000126583. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR002219. DAG_PE_bd.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

PANTHER

PTHR22985:SF86. PKC. 1 hit.

Pfam

PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000550. PKC_alpha. 1 hit.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

NextBio

21648.

PMAP-CutDB

P05129.

SOURCE

Search...

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Entry information

Entry name

KPCG_HUMAN

Accession

Primary (citable) accession number: P05129

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	February 1, 1994
Last modified:	July 7, 2009
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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