PRKCZ
Protein kinase C zeta type
Also known as: KPCZ_HUMAN, PKC2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q05513
- Gene
- PRKCZ
- Ensembl
- ENSG00000067606
- Chromosome
- 1
- Canonical length
- 592 aa
- Protein class
- Enzymes, FDA approved drug targets, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Plasma membrane,Basal body,Cytosol,Flagellar centriole,Mid piece,End piece
OverviewNCBI Gene
Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
592 residues, UniProt reviewed canonical sequence.
>Q05513|PRKCZ
1 MPSRTGPKME GSGGRVRLKA HYGGDIFITS VDAATTFEEL CEEVRDMCRL HQQHPLTLKW
61 VDSEGDPCTV SSQMELEEAF RLARQCRDEG LIIHVFPSTP EQPGLPCPGE DKSIYRRGAR
121 RWRKLYRANG HLFQAKRFNR RAYCGQCSER IWGLARQGYR CINCKLLVHK RCHGLVPLTC
181 RKHMDSVMPS QEPPVDDKNE DADLPSEETD GIAYISSSRK HDSIKDDSED LKPVIDGMDG
241 IKISQGLGLQ DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE
301 KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE EHARFYAAEI
361 CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE GLGPGDTTST FCGTPNYIAP
421 EILRGEEYGF SVDWWALGVL MFEMMAGRSP FDIITDNPDM NTEDYLFQVI LEKPIRIPRF
481 LSVKASHVLK GFLNKDPKER LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ ALPPFQPQIT
541 DDYGLDNFDT QFTSEPVQLT PDDEDAIKRI DQSEFEGFEY INPLLLSTEE SVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRKCZ can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.32
- Highest tissue expression
- 137 nTPM
Expression across tissuesHPA
Tissue
- cerebellum: 137 nTPM
- cerebral cortex: 81 nTPM
- basal ganglia: 58 nTPM
- hippocampal formation: 48 nTPM
- amygdala: 47 nTPM
- spinal cord: 44 nTPM
Single-cell type
- syncytiotrophoblasts: 1,824 nCPM
- late spermatids: 1,337 nCPM
- alveolar cells type 1: 484 nCPM
- transitional alveolar cells: 274 nCPM
- early spermatids: 274 nCPM
- alveolar cells type 2: 209 nCPM
Immune cell
- eosinophil: 16 nTPM
- MAIT T-cell: 2.5 nTPM
- neutrophil: 1.1 nTPM
- memory CD4 T-cell: 0.9 nTPM
- NK-cell: 0.9 nTPM
- T-reg: 0.9 nTPM
Brain region
- cerebellum: 189 nTPM
- cerebral cortex: 153 nTPM
- basal ganglia: 119 nTPM
- white matter: 118 nTPM
- hippocampal formation: 117 nTPM
- pons: 109 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.4
- gnomAD pLI
- 0.54
- gnomAD missense Z
- 2.8
- DepMap mean gene effect
- -0.13
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cellular response to insulin stimulus
- establishment of cell polarity
- establishment or maintenance of epithelial cell apical/basal polarity
- inflammatory response
- intracellular signal transduction
- long-term synaptic potentiation
- microtubule cytoskeleton organization
- negative regulation of apoptotic process
- negative regulation of insulin receptor signaling pathway
- negative regulation of protein-containing complex assembly
- neuron projection extension
- positive regulation of ERK1 and ERK2 cascade
- positive regulation of excitatory postsynaptic potential
- positive regulation of insulin receptor signaling pathway
- positive regulation of interleukin-10 production
- positive regulation of interleukin-13 production
- positive regulation of interleukin-4 production
- positive regulation of interleukin-5 production
- positive regulation of NF-kappaB transcription factor activity
- positive regulation of T-helper 2 cell cytokine production
- positive regulation of T-helper 2 cell differentiation
- protein localization to plasma membrane
- protein phosphorylation
- signal transduction
Molecular functions
- ATP binding
- diacylglycerol-dependent serine/threonine kinase activity
- insulin receptor substrate binding
- protein kinase activity
- protein serine kinase activity
- protein serine/threonine kinase activity
- zinc ion binding
Cellular components
- apical cortex
- apical plasma membrane
- axon hillock
- bicellular tight junction
- cell junction
- cell-cell junction
- centriole
- ciliary basal body
- cytoplasm
- cytosol
- endosome
- extracellular exosome
- membrane
- myelin sheath abaxonal region
- nuclear envelope
- nuclear matrix
- PAR polarity complex
- plasma membrane
- sperm end piece
- sperm midpiece
- tight junction
- vesicle
Protein domainsUniProt · Pfam · InterPro
- PB1 domain
- Protein kinase domain
- AGC-kinase, C-terminal
- Protein kinase C-like, phorbol ester/diacylglycerol-binding domain
- Serine/threonine-protein kinase, active site
- Protein kinase-like domain superfamily
- Protein kinase C
- Protein kinase, ATP binding site
- Protein kinase, C-terminal
- Diacylglycerol/phorbol-ester binding
- Protein kinase C, PB1 domain
- C1-like domain superfamily
- PB1-like domain
- Protein kinase domain
- Phorbol esters/diacylglycerol binding domain (C1 domain)
- Protein kinase C terminal domain
- PB1 domain
- Atypical Protein Kinase C zeta, catalytic domain
- Protein kinase C zeta type, conserved region 1
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PRKCZ in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PRKCZ as an antibody target. Whether an autoantibody or antibody against PRKCZ could matter depends on whether native PRKCZ is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRKCZ is annotated at the cell surface, where native PRKCZ is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label PRKCZ as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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