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UniProtKB/Swiss-Prot entry P05129


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KPCG_HUMAN
Primary accession number P05129
Secondary accession numbers None
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on February 1, 1994 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 104)
Name and origin of the protein
Protein name Protein kinase C gamma type
Synonyms PKC-gamma
EC 2.7.11.13
Gene name
Name: PRKCG
Synonyms: PKCG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-318.
TISSUE=Brain;
PubMed=3755548 [NCBI, ExPASy, EBI, Israel, Japan]
Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.;
"Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways.";
Science 233:859-866(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 162-697.
TISSUE=Hippocampus;
PubMed=8375396 [NCBI, ExPASy, EBI, Israel, Japan]
Kochs G., Hummel R., Meyer D., Hug H., Marme D., Sarre T.F.;
"Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes.";
Eur. J. Biochem. 216:597-606(1993).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[6]
VARIANTS CYS-141; GLN-415; ASP-523 AND SER-659.
DOI=10.1086/301819; PubMed=9545390 [NCBI, ExPASy, EBI, Israel, Japan]
Al-Maghtheh M., Vithana E.N., Inglehearn C.F., Moore T., Bird A.C., Bhattacharya S.S.;
"Segregation of a PRKCG mutation in two RP11 families.";
Am. J. Hum. Genet. 62:1248-1252(1998).
[7]
SHOWS THAT THE VARIANTS ARE NOT A CAUSE OF RP11.
DOI=10.1086/302554; PubMed=10441600 [NCBI, ExPASy, EBI, Israel, Japan]
Dryja T.P., McEvoy J., McGee T.L., Berson E.L.;
"No mutations in the coding region of the PRKCG gene in three families with retinitis pigmentosa linked to the RP11 locus on chromosome 19q.";
Am. J. Hum. Genet. 65:926-928(1999).
[8]
VARIANTS SCA14 TYR-101; PRO-119 AND ASP-128.
DOI=10.1086/373883; PubMed=12644968 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Missense mutations in the regulatory domain of PKC gamma: a new mechanism for dominant nonepisodic cerebellar ataxia.";
Am. J. Hum. Genet. 72:839-849(2003).
[9]
INTERACTION WITH CDCP1.
DOI=10.1016/j.cell.2005.02.019; PubMed=15851033 [NCBI, ExPASy, EBI, Israel, Japan]
Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.;
"The C2 domain of PKCdelta is a phosphotyrosine binding domain.";
Cell 121:271-280(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF345987; AAK13533.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC047876; AAH47876.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13977; AAA60102.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z15114; CAA78820.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D24664; D24664.
RefSeq NP_002730.1; -.
UniGene Hs.631564
3D structure databases
PDB
2E73; NMR; -; A=36-105.[ExPASy / RCSB / EBI]
2UZP; X-ray; 2.00 A; A/B/C=154-295.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2E73; -.
2UZP; -.
SMR P05129; 93-158, 348-683.
ModBase P05129.
Protein-protein interaction databases
IntAct P05129; -.
PTM databases
PhosphoSite P05129; -.
Organism-specific databases
H-InvDB HIX0027463; -.
HGNC HGNC:9402; PRKCG.
GenAtlas PRKCG.
HPA CAB013051; -.
MIM 176980; gene. [NCBI / EBI]
605361; phenotype. [NCBI / EBI]
Orphanet 99; Cerebellar ataxia, autosomal dominant.
98763; SCA14.
PharmGKB PA33766; -.
GeneCards P05129.
Gene expression databases
ArrayExpress P05129; -.
CleanEx HS_PRKCG; -.
GermOnline ENSG00000126583; Homo sapiens.
Ontologies
GO
GO:0004697; Molecular function: protein kinase C activity (traceable author statement from ProtInc).
GO:0042177; Biological process: negative regulation of protein catabolic process (inferred from direct assay from HGNC).
GO:0031397; Biological process: negative regulation of protein ubiquitination (inferred from direct assay from HGNC).
GO:0032425; Biological process: positive regulation of mismatch repair (inferred from direct assay from HGNC).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR002219; DAG_PE_bd.
IPR015745; PKC.
IPR000961; Pkinase_C.
IPR014375; Prot_kin_PKC_alpha.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22985:SF86; PKC; 1.
Pfam PF00130; C1_1; 2.
PF00168; C2; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000550; PKC_alpha; 1.
PRINTS PR00360; C2DOMAIN.
PR00008; DAGPEDOMAIN.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05129.
ProtoNet P05129.
Proteomic databases
PeptideAtlas P05129; -.
Genome annotation databases
Ensembl ENSG00000126583; Homo sapiens. [Contig view]
GeneID 5582; -.
KEGG hsa:5582; -.
Phylogenomic databases
HOGENOM P05129; -.
HOVERGEN P05129; -.
Other
NextBio 21648; -.
SOURCE PRKCG; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Calcium; Disease mutation; Kinase; Metal-binding; Neurodegeneration; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Polymorphism; Repeat; Serine/threonine-protein kinase; Spinocerebellar ataxia; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   697  697     Protein kinase C gamma type. PRO_0000055689
DOMAIN   170   260  91     C2. 
DOMAIN   351   614  264     Protein kinase. 
DOMAIN   615   685  71     AGC-kinase C-terminal. 
ZN_FING   35    85  51     Phorbol-ester/DAG-type 1. 
ZN_FING   100   150  51     Phorbol-ester/DAG-type 2. 
NP_BIND   357   365  9     ATP (By similarity). 
ACT_SITE   480   480        Proton acceptor (By similarity). 
METAL   186   186        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   187   187        Calcium 1 (By similarity). 
METAL   187   187        Calcium 2 (By similarity). 
METAL   193   193        Calcium 2 (By similarity). 
METAL   246   246        Calcium 1 (By similarity). 
METAL   246   246        Calcium 2 (By similarity). 
METAL   247   247        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   248   248        Calcium 1 (By similarity). 
METAL   248   248        Calcium 2 (By similarity). 
METAL   248   248        Calcium 3 (By similarity). 
METAL   251   251        Calcium 3 (By similarity). 
METAL   252   252        Calcium 3; via carbonyl oxygen (By similarity). 
METAL   254   254        Calcium 1 (By similarity). 
METAL   254   254        Calcium 3 (By similarity). 
BINDING   380   380        ATP (By similarity). 
MOD_RES   195   195        Phosphotyrosine. 
MOD_RES   312   312        Phosphotyrosine (By similarity). 
MOD_RES   322   322        Phosphoserine (By similarity). 
MOD_RES   330   330        Phosphoserine (By similarity). 
MOD_RES   514   514        Phosphothreonine (By similarity). 
MOD_RES   518   518        Phosphothreonine (By similarity). 
MOD_RES   648   648        Phosphothreonine; by autocatalysis (Potential). 
MOD_RES   655   655        Phosphothreonine; by autocatalysis (Potential). 
MOD_RES   687   687        Phosphoserine (By similarity). 
VARIANT   101   101  1     H -> Y (in SCA14). VAR_017060 
VARIANT   119   119  1     S -> P (in SCA14). VAR_017061 
VARIANT   128   128  1     G -> D (in SCA14). VAR_017062 
VARIANT   141   141  1     R -> C. VAR_008755 
VARIANT   415   415  1     H -> Q. VAR_008756 
VARIANT   523   523  1     A -> D. VAR_008757 
VARIANT   659   659  1     R -> S. VAR_008758 
STRAND   160   169  10      
STRAND   172   182  11      
STRAND   194   201  8      
STRAND   222   230  9      
HELIX   233   237  5      
STRAND   239   246  8      
STRAND   249   251  3      
STRAND   254   262  9      
HELIX   263   268  6      
STRAND   271   276  6      
HELIX   280   283  4      
Sequence information
Length: 697 AA [This is the length of the unprocessed precursor] Molecular weight: 78448 Da [This is the MW of the unprocessed precursor] CRC64: 3F911B5BEF713C41 [This is a checksum on the sequence]
        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 

P05129 in FASTA format

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