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Q05513 (KPCZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 142. 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)
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 interleukines 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 PDK1 (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 PDK1; phosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2. Ref.9 Ref.13 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 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 processanti-apoptosis

Traceable author statement. Source: ProtInc

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

negative regulation of insulin receptor signaling pathway

Inferred from mutant phenotype. Source: BHF-UCL

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype. Source: BHF-UCL

negative regulation of protein complex assembly

Inferred from mutant phenotype. Source: BHF-UCL

peptidyl-serine phosphorylation

Inferred from direct assay. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

   Cellular componentendosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane fraction

Traceable author statement. Source: ProtInc

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor substrate binding

Inferred by curator. Source: BHF-UCL

protein kinase C activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 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.

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 residue2231Phosphoserine Ref.21
Modified residue4101Phosphothreonine; by PDPK1 Ref.9 Ref.23 Ref.25
Modified residue5601Phosphothreonine Ref.24

Natural variations

Alternative sequence1 – 183183Missing in isoform 2.
VSP_041904
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 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

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: 8224878] [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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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: 16710414] [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: 15489334] [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: 8375396] [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: 9447975] [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: 9566925] [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: 9768361] [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: 10356400] [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: 11035106] [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: 11260256] [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: 11781095] [Abstract]
Cited for: INTERACTION WITH PDK1, 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: 12162751] [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: 11755531] [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: 12234671] [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: 12893243] [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: 12887891] [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: 15084291] [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: 15324659] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MARK2.
[21]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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: 18190796] [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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-410, MASS SPECTROMETRY.
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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560, MASS SPECTROMETRY.
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: 20332120] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT, PHOSPHORYLATION AT THR-410.
[26]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Protein kinase Czeta (PKCzeta): activation mechanisms and cellular functions."
Hirai T., Chida K.
J. Biochem. 133:1-7(2003) [PubMed: 12761192] [Abstract]
Cited for: REVIEW ON FUNCTION.
[28]"Protein kinase Czeta and glucose uptake."
Liu L.Z., He A.B., Liu X.J., Li Y., Chang Y.S., Fang F.D.
Biokhimiia 71:701-706(2006) [PubMed: 16903823] [Abstract]
Cited for: REVIEW ON FUNCTION.
[29]"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: 16322752] [Abstract]
Cited for: REVIEW ON FUNCTION.
[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: 16959974] [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: 17344846] [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.
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.
IPIIPI00013749.
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 12-98, 130-587.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05513. 9 interactions.
MINTMINT-5004464.
STRINGQ05513.

PTM databases

PhosphoSiteQ05513.

Polymorphism databases

DMDM68067736.

Proteomic databases

PRIDEQ05513.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378567; ENSP00000367830; ENSG00000067606.
ENST00000400920; ENSP00000383711; ENSG00000067606.
ENST00000400921; ENSP00000383712; ENSG00000067606.
GeneID5590.
KEGGhsa:5590.
UCSCuc001aiq.1. human.

Organism-specific databases

CTD5590.
GeneCardsGC01P001939.
H-InvDBHIX0000046.
HIX0029201.
HGNCHGNC:9412. PRKCZ.
HPACAB004533.
HPA021851.
MIM176982. gene.
neXtProtNX_Q05513.
PharmGKBPA33775.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08632.
GeneTreeENSGT00590000082854.
HOGENOMHBG755340.
HOVERGENHBG108317.
InParanoidQ05513.
OMAAYISSTR.
OrthoDBEOG4T782V.
PhylomeDBQ05513.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
Pathway_Interaction_DBamb2_neutrophils_pathway. amb2 Integrin signaling.
ceramidepathway. Ceramide signaling pathway.
igf1_pathway. IGF1 pathway.
il1pathway. IL1-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
insulin_pathway. Insulin Pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
p75ntrpathway. p75(NTR)-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
txa2pathway. Thromboxane A2 receptor signaling.
tnfpathway. TNF receptor signaling pathway.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ05513.
BgeeQ05513.
CleanExHS_PRKCZ.
GenevestigatorQ05513.
GermOnlineENSG00000067606. Homo sapiens.

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_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
KOK06069.
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. Kinase_like. 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

BindingDBQ05513.
NextBio21684.
PMAP-CutDBQ05513.
SOURCESearch...

Entry information

Entry nameKPCZ_HUMAN
AccessionPrimary (citable) accession number: Q05513
Secondary accession number(s): A8K4N0 expand/collapse secondary AC list , A8MU64, Q15207, Q5SYT5, Q969S4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 142 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families