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Q05513 (KPCZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C zeta type

EC=2.7.11.13
Alternative name(s):
nPKC-zeta
Gene names
Name:PRKCZ
Synonyms:PKC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukins production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In NF-kappa-B-mediated inflammatory response, can relieve the SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Is necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. Ref.7 Ref.11 Ref.14 Ref.19 Ref.20

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-410 (activation loop of the kinase domain) and Thr-560 (turn motif), need to be phosphorylated for its full activation. Phosphatidylinositol 3,4,5-trisphosphate might be a physiological activator By similarity.

Subunit structure

Forms a ternary complex with SQSTM1 and KCNAB2. Forms another ternary complex with SQSTM1 and GABRR3. Forms a complex with SQSTM1 and MAP2K5 By similarity. Interacts with PARD6A, PARD6B, PARD6G and SQSTM1. Part of a complex with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts with ADAP1/CENTA1. Forms a ternary complex composed of SQSTM1 and PAWR. Interacts directly with SQSTM1 Probable. Interacts with IKBKB. Interacts (via the protein kinase domain) with WWC1. Forms a tripartite complex with WWC1 and DDR1, but predominantly in the absence of collagen. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with PDPK1 (via N-terminus region). Ref.8 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ref.25

Subcellular location

Cytoplasm. Endosome. Cell junction. Note: In the retina, localizes in the terminals of the rod bipolar cells By similarity. Associates with endosomes. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. Ref.8 Ref.25

Tissue specificity

Expressed in brain, and to a lesser extent in lung, kidney and testis.

Domain

The OPR domain mediates mutually exclusive interactions with SQSTM1 and PARD6B. Ref.18

The C1 domain does not bind the diacylglycerol (DAG). Ref.18

Post-translational modification

CDH5 is required for its phosphorylation at Thr-410. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2. Phosphorylation at Thr-410 by PI3K activates the kinase. Ref.9 Ref.13 Ref.21 Ref.25

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 OPR domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAA78813.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processInflammatory response
   Cellular componentCell junction
Cytoplasm
Endosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from electronic annotation. Source: Ensembl

activation of phospholipase D activity

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase B activity

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cell migration

Inferred from electronic annotation. Source: Ensembl

establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

long-term memory

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from sequence or structural similarity. Source: UniProtKB

membrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

microtubule cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Traceable author statement PubMed 10770953. Source: ProtInc

negative regulation of hydrolase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 15069075. Source: BHF-UCL

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 15069075. Source: BHF-UCL

negative regulation of protein complex assembly

Inferred from mutant phenotype PubMed 15069075. Source: BHF-UCL

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 15069075. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T-helper 2 cell cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of T-helper 2 cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glucose import

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-10 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-13 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-4 production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interleukin-5 secretion

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein kinase C signaling

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 10770950. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

vesicle transport along microtubule

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical cortex

Inferred from electronic annotation. Source: Ensembl

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell junction

Traceable author statement. Source: Reactome

cell leading edge

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay Ref.25. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 7925449. Source: ProtInc

cytosol

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Traceable author statement PubMed 7925449. Source: ProtInc

membrane raft

Inferred from electronic annotation. Source: Ensembl

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement PubMed 7925449. Source: ProtInc

protein complex

Inferred from electronic annotation. Source: Ensembl

tight junction

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor substrate binding

Inferred by curator PubMed 15069075. Source: BHF-UCL

potassium channel regulator activity

Inferred from electronic annotation. Source: Ensembl

protein kinase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase activity

Inferred from direct assay PubMed 10770950. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 15069075. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05513-1)

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.
Isoform 2 (identifier: Q05513-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: Missing.
Isoform 3 (identifier: Q05513-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: MPSRTGPKME...PGLPCPGEDK → MLTPRTDE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Protein kinase C zeta type
PRO_0000055701

Regions

Domain15 – 9884OPR
Domain252 – 518267Protein kinase
Domain519 – 59072AGC-kinase C-terminal
Zinc finger130 – 18051Phorbol-ester/DAG-type
Nucleotide binding258 – 2669ATP By similarity
Region79 – 14567Interaction with SQSTM1 By similarity

Sites

Active site3761Proton acceptor By similarity
Binding site2811ATP By similarity

Amino acid modifications

Modified residue4101Phosphothreonine; by PDPK1 and PI3K Ref.9 Ref.21 Ref.25
Modified residue5601Phosphothreonine Ref.24

Natural variations

Alternative sequence1 – 183183Missing in isoform 2.
VSP_041904
Alternative sequence1 – 112112MPSRT…PGEDK → MLTPRTDE in isoform 3.
VSP_046347
Natural variant491R → H.
Corresponds to variant rs35271800 [ dbSNP | Ensembl ].
VAR_050560
Natural variant841R → H. Ref.31
Corresponds to variant rs56017162 [ dbSNP | Ensembl ].
VAR_042310
Natural variant5141S → F in a colorectal cancer sample; somatic mutation. Ref.30
VAR_035467
Natural variant5191R → C in a colorectal adenocarcinoma sample; somatic mutation. Ref.31
VAR_042311

Experimental info

Mutagenesis191K → A: No effect on interaction with SQSTM1 and PARD6B. Ref.18
Mutagenesis621D → A: Loss of interaction with SQSTM1 and PARD6B. Ref.18
Mutagenesis661D → A: Loss of interaction with SQSTM1 and PARD6B. Ref.18
Sequence conflict61G → D in AAA36488. Ref.1
Sequence conflict1981K → R in BAF83684. Ref.3
Sequence conflict2621S → T in AAA36488. Ref.1
Sequence conflict2811K → R in BAH11883. Ref.3
Sequence conflict3661F → L in BAF83684. Ref.3
Sequence conflict5001R → G in BAF83684. Ref.3
Sequence conflict5221D → G in BAF83684. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2005. Version 4.
Checksum: 88CCD0577E6A596C

FASTA59267,660
        10         20         30         40         50         60 
MPSRTGPKME GSGGRVRLKA HYGGDIFITS VDAATTFEEL CEEVRDMCRL HQQHPLTLKW 

        70         80         90        100        110        120 
VDSEGDPCTV SSQMELEEAF RLARQCRDEG LIIHVFPSTP EQPGLPCPGE DKSIYRRGAR 

       130        140        150        160        170        180 
RWRKLYRANG HLFQAKRFNR RAYCGQCSER IWGLARQGYR CINCKLLVHK RCHGLVPLTC 

       190        200        210        220        230        240 
RKHMDSVMPS QEPPVDDKNE DADLPSEETD GIAYISSSRK HDSIKDDSED LKPVIDGMDG 

       250        260        270        280        290        300 
IKISQGLGLQ DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE 

       310        320        330        340        350        360 
KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE EHARFYAAEI 

       370        380        390        400        410        420 
CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE GLGPGDTTST FCGTPNYIAP 

       430        440        450        460        470        480 
EILRGEEYGF SVDWWALGVL MFEMMAGRSP FDIITDNPDM NTEDYLFQVI LEKPIRIPRF 

       490        500        510        520        530        540 
LSVKASHVLK GFLNKDPKER LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ ALPPFQPQIT 

       550        560        570        580        590 
DDYGLDNFDT QFTSEPVQLT PDDEDAIKRI DQSEFEGFEY INPLLLSTEE SV 

« Hide

Isoform 2 [UniParc].

Checksum: 21C316A4A2B418BD
Show »

FASTA40946,622
Isoform 3 [UniParc].

Checksum: 219A7C60FCEF0905
Show »

FASTA48856,136

References

« Hide 'large scale' references
[1]"The cDNA sequence encoding human protein kinase C-zeta."
Barbee J.L., Loomis C.R., Deutscher S.L., Burns D.J.
Gene 132:305-306(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Frontal cortex.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain and Teratocarcinoma.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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] (ISOFORM 1).
Tissue: Colon and Ovary.
[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 7-592.
Tissue: Hippocampus.
[7]"Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes."
Schoenwasser D.C., Marais R.M., Marshall C.J., Parker P.J.
Mol. Cell. Biol. 18:790-798(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF MAP2K1/MEK1 AND MAPK1/ERK2.
[8]"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62."
Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.
Mol. Cell. Biol. 18:3069-3080(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
[9]"Regulation of protein kinase C zeta by PI 3-kinase and PDK-1."
Chou M.M., Hou W., Johnson J., Graham L.K., Lee M.H., Chen C.S., Newton A.C., Schaffhausen B.S., Toker A.
Curr. Biol. 8:1069-1077(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-410 BY PDPK1.
[10]"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND IKBKB.
[11]"Protein kinase C zeta plays a central role in activation of the p42/44 mitogen-activated protein kinase by endotoxin in alveolar macrophages."
Monick M.M., Carter A.B., Flaherty D.M., Peterson M.W., Hunninghake G.W.
J. Immunol. 165:4632-4639(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF MAPK1/ERK2.
[12]"Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C."
Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.
Genes Cells 6:107-119(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G.
Tissue: Neuroblastoma.
[13]"Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment."
Hodgkinson C.P., Sale G.J.
Biochemistry 41:561-569(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDPK1, PHOSPHORYLATION.
[14]"Characterization of PDK2 activity against protein kinase B gamma."
Hodgkinson C.P., Sale E.M., Sale G.J.
Biochemistry 41:10351-10359(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF AKT3.
[15]"p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition."
Chang S., Kim J.H., Shin J.
FEBS Lett. 510:57-61(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND PAWR.
[16]"Multiple splice variants of Par3 and of a novel related gene, Par3L, produce proteins with different binding properties."
Gao L., Macara I.G., Joberty G.
Gene 294:99-107(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD3.
[17]"Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C."
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D., Wakefield R.I.D., Johannes F.-J., Aitken A.
Biochem. Biophys. Res. Commun. 307:459-465(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAP1.
[18]"PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62."
Wilson M.I., Gill D.J., Perisic O., Quinn M.T., Williams R.L.
Mol. Cell 12:39-50(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1 AND PARD6B, DOMAIN, MUTAGENESIS OF LYS-19; ASP-62 AND ASP-66.
[19]"Atypical PKC phosphorylates PAR-1 kinases to regulate localization and activity."
Hurov J.B., Watkins J.L., Piwnica-Worms H.
Curr. Biol. 14:736-741(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MARK2 AND MARK3.
[20]"aPKC acts upstream of PAR-1b in both the establishment and maintenance of mammalian epithelial polarity."
Suzuki A., Hirata M., Kamimura K., Maniwa R., Yamanaka T., Mizuno K., Kishikawa M., Hirose H., Amano Y., Izumi N., Miwa Y., Ohno S.
Curr. Biol. 14:1425-1435(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MARK2.
[21]"Role of atypical protein kinase C in estradiol-triggered G1/S progression of MCF-7 cells."
Castoria G., Migliaccio A., Di Domenico M., Lombardi M., de Falco A., Varricchio L., Bilancio A., Barone M.V., Auricchio F.
Mol. Cell. Biol. 24:7643-7653(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-410 BY PI3K.
[22]"KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WWC1 AND DDR1.
[23]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"CCM1 regulates vascular-lumen organization by inducing endothelial polarity."
Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G., Chapon F., Dejana E.
J. Cell Sci. 123:1073-1080(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT, PHOSPHORYLATION AT THR-410.
[26]"Protein kinase Czeta (PKCzeta): activation mechanisms and cellular functions."
Hirai T., Chida K.
J. Biochem. 133:1-7(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[27]"Protein kinase Czeta and glucose uptake."
Liu L.Z., He A.B., Liu X.J., Li Y., Chang Y.S., Fang F.D.
Biochemistry (Mosc.) 71:701-706(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[28]"PKCzeta at the crossroad of NF-kappaB and Jak1/Stat6 signaling pathways."
Moscat J., Rennert P., Diaz-Meco M.T.
Cell Death Differ. 13:702-711(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-514.
[31]"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. expand/collapse author list , 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] HIS-84 AND CYS-519.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14283 mRNA. Translation: AAA36488.1.
BT007082 mRNA. Translation: AAP35745.1.
AK290995 mRNA. Translation: BAF83684.1.
AK294649 mRNA. Translation: BAH11833.1.
AK294782 mRNA. Translation: BAH11883.1.
AL162271 Genomic DNA. No translation available.
AL391845, AL590822, AL645703 Genomic DNA. Translation: CAI15438.1.
AL645703, AL391845, AL590822 Genomic DNA. Translation: CAI21535.1.
BC008058 mRNA. Translation: AAH08058.1.
BC014270 mRNA. Translation: AAH14270.1.
Z15108 mRNA. Translation: CAA78813.1. Different initiation.
PIRJN0877.
RefSeqNP_001028753.1. NM_001033581.1.
NP_001028754.1. NM_001033582.1.
NP_001229803.1. NM_001242874.1.
NP_002735.3. NM_002744.4.
UniGeneHs.496255.

3D structure databases

ProteinModelPortalQ05513.
SMRQ05513. Positions 13-587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111576. 74 interactions.
IntActQ05513. 23 interactions.
MINTMINT-5004464.
STRING9606.ENSP00000367830.

Chemistry

BindingDBQ05513.
ChEMBLCHEMBL3438.
GuidetoPHARMACOLOGY1491.

PTM databases

PhosphoSiteQ05513.

Polymorphism databases

DMDM68067736.

Proteomic databases

PaxDbQ05513.
PRIDEQ05513.

Protocols and materials databases

DNASU5590.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378567; ENSP00000367830; ENSG00000067606. [Q05513-1]
ENST00000400920; ENSP00000383711; ENSG00000067606. [Q05513-2]
ENST00000400921; ENSP00000383712; ENSG00000067606. [Q05513-2]
ENST00000461106; ENSP00000426412; ENSG00000067606. [Q05513-3]
GeneID5590.
KEGGhsa:5590.
UCSCuc001aiq.3. human. [Q05513-1]
uc001ait.3. human. [Q05513-2]

Organism-specific databases

CTD5590.
GeneCardsGC01P001982.
H-InvDBHIX0000049.
HIX0029201.
HGNCHGNC:9412. PRKCZ.
HPACAB004533.
HPA021851.
MIM176982. gene.
neXtProtNX_Q05513.
PharmGKBPA33775.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidQ05513.
KOK06069.
OMARCHVLVP.
OrthoDBEOG7HF1J3.
PhylomeDBQ05513.
TreeFamTF102004.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
SignaLinkQ05513.

Gene expression databases

ArrayExpressQ05513.
BgeeQ05513.
CleanExHS_PRKCZ.
GenevestigatorQ05513.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000554. PKC_zeta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 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. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKCZ. human.
GeneWikiProtein_kinase_M_zeta/Protein_kinase_C_zeta.
GenomeRNAi5590.
NextBio21684.
PMAP-CutDBQ05513.
PROQ05513.
SOURCESearch...

Entry information

Entry nameKPCZ_HUMAN
AccessionPrimary (citable) accession number: Q05513
Secondary accession number(s): A8K4N0 expand/collapse secondary AC list , A8MU64, B7Z2J7, E9PCW2, Q15207, Q5SYT5, Q969S4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 167 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM