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Protein

Protein kinase C zeta type

Gene

Prkcz

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin 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 the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis. Phosphorylates VAMP2 in vitro (By similarity).By similarity9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei281 – 2811ATPPROSITE-ProRule annotation
Active sitei376 – 3761Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 18051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi258 – 2669ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • 14-3-3 protein binding Source: RGD
  • ATP binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • phospholipase binding Source: RGD
  • potassium channel regulator activity Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase activity Source: RGD
  • protein kinase binding Source: RGD
  • protein kinase C activity Source: RGD
  • protein serine/threonine kinase activity Source: RGD

GO - Biological processi

  • actin cytoskeleton reorganization Source: RGD
  • activation of phospholipase D activity Source: RGD
  • activation of protein kinase B activity Source: RGD
  • cell migration Source: RGD
  • cell surface receptor signaling pathway Source: RGD
  • cellular protein localization Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • establishment of cell polarity Source: UniProtKB
  • inflammatory response Source: UniProtKB-KW
  • insulin receptor signaling pathway Source: RGD
  • intracellular signal transduction Source: RGD
  • long-term memory Source: RGD
  • long-term synaptic potentiation Source: UniProtKB
  • membrane depolarization Source: RGD
  • membrane hyperpolarization Source: RGD
  • microtubule cytoskeleton organization Source: Ensembl
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of hydrolase activity Source: RGD
  • negative regulation of insulin receptor signaling pathway Source: Ensembl
  • negative regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  • negative regulation of protein complex assembly Source: Ensembl
  • neuron projection extension Source: Ensembl
  • peptidyl-serine phosphorylation Source: RGD
  • positive regulation of cell-matrix adhesion Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of excitatory postsynaptic potential Source: UniProtKB
  • positive regulation of glucose import Source: RGD
  • positive regulation of insulin receptor signaling pathway Source: UniProtKB
  • positive regulation of interleukin-10 secretion Source: UniProtKB
  • positive regulation of interleukin-13 secretion Source: UniProtKB
  • positive regulation of interleukin-4 production Source: UniProtKB
  • positive regulation of interleukin-5 secretion Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of protein transport Source: RGD
  • positive regulation of synaptic transmission Source: RGD
  • positive regulation of T-helper 2 cell cytokine production Source: UniProtKB
  • positive regulation of T-helper 2 cell differentiation Source: UniProtKB
  • protein heterooligomerization Source: RGD
  • protein kinase C signaling Source: RGD
  • protein localization to plasma membrane Source: Ensembl
  • protein phosphorylation Source: RGD
  • signal transduction Source: RGD
  • vesicle transport along microtubule Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Inflammatory response

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.13. 5301.
ReactomeiR-RNO-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-RNO-5218921. VEGFR2 mediated cell proliferation.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C zeta type (EC:2.7.11.13)
Alternative name(s):
nPKC-zeta
Gene namesi
Name:Prkcz
Synonyms:Pkcz
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi3399. Prkcz.

Subcellular locationi

  • Cytoplasm 2 Publications
  • Endosome By similarity
  • Cell junction By similarity

  • Note: In the retina, localizes in the terminals of the rod bipolar cells. Associated with endosomes. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. Colocalizes with VAMP2 and WDFY2 in intracellular vesicles.By similarity

GO - Cellular componenti

  • apical cortex Source: Ensembl
  • apical plasma membrane Source: Ensembl
  • axon hillock Source: Ensembl
  • bicellular tight junction Source: Ensembl
  • cell-cell junction Source: UniProtKB
  • cell leading edge Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: Ensembl
  • intracellular membrane-bounded organelle Source: RGD
  • membrane raft Source: RGD
  • microtubule organizing center Source: Ensembl
  • myelin sheath abaxonal region Source: Ensembl
  • nuclear envelope Source: Ensembl
  • nuclear matrix Source: Ensembl
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: UniProtKB
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621D → A: Loss of interaction with SQSTM1. 1 Publication

Chemistry

ChEMBLiCHEMBL2094266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Protein kinase C zeta typePRO_0000055704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei410 – 4101Phosphothreonine; by PDPK1 and PI3KBy similarity
Modified residuei560 – 5601PhosphothreonineCombined sources1 Publication
Modified residuei591 – 5911PhosphoserineCombined sources

Post-translational modificationi

CDH5 is required for its phosphorylation at Thr-410. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-410 by PI3K activates the kinase (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP09217.
PRIDEiP09217.

PTM databases

iPTMnetiP09217.
PhosphoSiteiP09217.

Expressioni

Gene expression databases

GenevisibleiP09217. RN.

Interactioni

Subunit structurei

Interacts with PARD6A, PARD6B and PARD6G. Part of a complex with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts with ADAP1/CENTA1 (By similarity). Forms a ternary complex with SQSTM1 and KCNAB2. Forms another ternary complex with SQSTM1 and GABRR3. Forms a complex with SQSTM1 and MAP2K5. 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-terminal region). Interacts with WDFY2 (via WD repeats 1-3) (By similarity). Interacts with VAMP2 (By similarity). Forms a complex with WDFY2 and VAMP2 (By similarity).By similarity3 Publications

GO - Molecular functioni

  • 14-3-3 protein binding Source: RGD
  • phospholipase binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi247554. 15 interactions.
DIPiDIP-40867N.
IntActiP09217. 2 interactions.
MINTiMINT-125335.
STRINGi10116.ENSRNOP00000021285.

Structurei

Secondary structure

1
592
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228Combined sources
Beta strandi25 – 317Combined sources
Helixi37 – 4711Combined sources
Beta strandi56 – 616Combined sources
Beta strandi67 – 704Combined sources
Helixi73 – 8513Combined sources
Beta strandi89 – 979Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MJSX-ray2.50A/C/E/G/I/K/M/O/Q/S/U/W15-101[»]
ProteinModelPortaliP09217.
SMRiP09217. Positions 12-98, 247-584.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9884PB1PROSITE-ProRule annotationAdd
BLAST
Domaini252 – 518267Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini519 – 59072AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 14567Interaction with SQSTM1Add
BLAST

Domaini

The PB1 domain mediate mutually exclusive interactions with SQSTM1 and PARD6B.By similarity
The C1 domain does not bind the diacylglycerol (DAG).1 Publication

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 18051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP09217.
KOiK18952.
OMAiRCHVLVP.
OrthoDBiEOG7HF1J3.
PhylomeDBiP09217.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS51745. PB1. 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]

Sequencei

Sequence statusi: Complete.

P09217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSRTDPKMD RSGGRVRLKA HYGGDILITS VDPTTTFQDL CEEVRDMCGL
60 70 80 90 100
HQQHPLTLKW VDSEGDPCTV SSQMELEEAF RLACQGRDEV LIIHVFPSIP
110 120 130 140 150
EQPGMPCPGE DKSIYRRGAR RWRKLYRANG HLFQAKRFNR RAYCGQCSER
160 170 180 190 200
IWGLARQGYR CINCKLLVHK RCHVLVPLTC RRHMDSVMPS QEPPVDDKND
210 220 230 240 250
GVDLPSEETD GIAYISSSRK HDNIKDDSED LKPVIDGVDG IKISQGLGLQ
260 270 280 290 300
DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE
310 320 330 340 350
KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE
360 370 380 390 400
EHARFYAAEI CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE
410 420 430 440 450
GLGPGDTTST FCGTPNYIAP EILRGEEYGF SVDWWALGVL MFEMMAGRSP
460 470 480 490 500
FDIITDNPDM NTEDYLFQVI LEKPIRIPRF LSVKASHVLK GFLNKDPKER
510 520 530 540 550
LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ TLPPFQPQIT DDYGLDNFDT
560 570 580 590
QFTSEPVQLT PDDEDVIKRI DQSEFEGFEY INPLLLSAEE SV
Length:592
Mass (Da):67,733
Last modified:February 1, 1991 - v2
Checksum:i5A3021171C2FD7C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 11211QPGMPCPGEDK → FRAEEAAEKAE in AAA41878 (PubMed:2834397).CuratedAdd
BLAST
Sequence conflicti102 – 11211QPGMPCPGEDK → FRAEEAAEKAE no nucleotide entry (PubMed:3691811).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04532 mRNA. Translation: AAA41934.1.
M18332 mRNA. Translation: AAA41878.1.
PIRiA30314.
RefSeqiNP_071952.1. NM_022507.1.
UniGeneiRn.1109.

Genome annotation databases

EnsembliENSRNOT00000021285; ENSRNOP00000021285; ENSRNOG00000015480.
GeneIDi25522.
KEGGirno:25522.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04532 mRNA. Translation: AAA41934.1.
M18332 mRNA. Translation: AAA41878.1.
PIRiA30314.
RefSeqiNP_071952.1. NM_022507.1.
UniGeneiRn.1109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MJSX-ray2.50A/C/E/G/I/K/M/O/Q/S/U/W15-101[»]
ProteinModelPortaliP09217.
SMRiP09217. Positions 12-98, 247-584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247554. 15 interactions.
DIPiDIP-40867N.
IntActiP09217. 2 interactions.
MINTiMINT-125335.
STRINGi10116.ENSRNOP00000021285.

Chemistry

ChEMBLiCHEMBL2094266.

PTM databases

iPTMnetiP09217.
PhosphoSiteiP09217.

Proteomic databases

PaxDbiP09217.
PRIDEiP09217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021285; ENSRNOP00000021285; ENSRNOG00000015480.
GeneIDi25522.
KEGGirno:25522.

Organism-specific databases

CTDi5590.
RGDi3399. Prkcz.

Phylogenomic databases

eggNOGiKOG0695. Eukaryota.
ENOG410ZMG2. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP09217.
KOiK18952.
OMAiRCHVLVP.
OrthoDBiEOG7HF1J3.
PhylomeDBiP09217.

Enzyme and pathway databases

BRENDAi2.7.11.13. 5301.
ReactomeiR-RNO-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-RNO-5218921. VEGFR2 mediated cell proliferation.

Miscellaneous databases

NextBioi606991.
PROiP09217.

Gene expression databases

GenevisibleiP09217. RN.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. PB1_dom.
IPR002219. PE/DAG-bd.
IPR012233. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS51745. PB1. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protein kinase C zeta subspecies from rat brain: its structure, expression, and properties."
    Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
    Proc. Natl. Acad. Sci. U.S.A. 86:3099-3103(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The structure, expression, and properties of additional members of the protein kinase C family."
    Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
    J. Biol. Chem. 263:6927-6932(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-592.
    Tissue: Brain.
  3. "Identification of three additional members of rat protein kinase C family: delta-, epsilon- and zeta-subspecies."
    Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.
    FEBS Lett. 226:125-128(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-180.
  4. "Persistent activation of the zeta isoform of protein kinase C in the maintenance of long-term potentiation."
    Sacktor T.C., Osten P., Valsamis H., Jiang X., Naik M.U., Sublette E.
    Proc. Natl. Acad. Sci. U.S.A. 90:8342-8346(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LONG-TERM POTENTIATION.
  5. "Evidence for a role of MEK and MAPK during signal transduction by protein kinase C zeta."
    Berra E., Diaz-Meco M.T., Lozano J., Frutos S., Municio M.M., Sanchez P., Sanz L., Moscat J.
    EMBO J. 14:6157-6163(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF MAP2K1/MEK1 AND MAPK3/ERK1.
  6. "Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport."
    Standaert M.L., Galloway L., Karnam P., Bandyopadhyay G., Moscat J., Farese R.V.
    J. Biol. Chem. 272:30075-30082(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein."
    Puls A., Schmidt S., Grawe F., Stabel S.
    Proc. Natl. Acad. Sci. U.S.A. 94:6191-6196(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, DOMAIN.
  8. "Activation of IkappaB kinase beta by protein kinase C isoforms."
    Lallena M.J., Diaz-Meco M.T., Bren G., Paya C.V., Moscat J.
    Mol. Cell. Biol. 19:2180-2188(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION.
  9. "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway."
    Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.
    EMBO J. 19:1576-1586(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION.
  10. "Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta."
    Etienne-Manneville S., Hall A.
    Cell 106:489-498(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL POLARITY.
  11. "MEK5, a new target of the atypical protein kinase C isoforms in mitogenic signaling."
    Diaz-Meco M.T., Moscat J.
    Mol. Cell. Biol. 21:1218-1227(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF MAP2K5/MEK5 AND MAPK7/ERK5.
  12. "Protein kinase Mzeta is necessary and sufficient for LTP maintenance."
    Ling D.S., Benardo L.S., Serrano P.A., Blace N., Kelly M.T., Crary J.F., Sacktor T.C.
    Nat. Neurosci. 5:295-296(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LONG-TERM POTENTIATION.
  13. "ZIP3, a new splice variant of the PKC-zeta-interacting protein family, binds to GABAC receptors, PKC-zeta, and Kv beta 2."
    Croci C., Brandstaetter J.H., Enz R.
    J. Biol. Chem. 278:6128-6135(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND GABRR3, SUBCELLULAR LOCATION.
  14. "Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins."
    Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., Michaelsen E., Bjoerkoey G., Johansen T.
    J. Biol. Chem. 278:34568-34581(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND MAP2K5, MUTAGENESIS OF ASP-62.
  15. "Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation."
    Le Good J.A., Brindley D.N.
    Biochem. J. 378:83-92(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-410 AND THR-560.
  16. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560 AND SER-591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKPCZ_RAT
AccessioniPrimary (citable) accession number: P09217
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.