PRKCZ
entrez
5590
canonical
uniprot
Q05513
canonical
ensembl
ENSG00000067606
resolver
ensp
ENSP00000367830
resolver
ensp
ENSP00000383712
resolver
ensp
ENSP00000424398
resolver
ensp
ENSP00000426412
resolver
ensp
ENSP00000547922
resolver
ensp
ENSP00000681855
resolver
genesymbol
PRKCZ
resolver
genesymbol_syn
PKC2
resolver
hgnc
HGNC:9412
resolver
uniprot
A8K4N0
resolver
uniprot
A8MU64
resolver
uniprot
B7Z2J7
resolver
uniprot
E9PCW2
resolver
uniprot
Q15207
resolver
uniprot
Q5SYT5
resolver
uniprot
Q969S4
resolver
uniprot_entry
KPCZ_HUMAN
resolver
uniprot_sec
A8K4N0
resolver
uniprot_sec
A8MU64
resolver
uniprot_sec
B7Z2J7
resolver
uniprot_sec
E9PCW2
resolver
uniprot_sec
Q15207
resolver
uniprot_sec
Q5SYT5
resolver
uniprot_sec
Q969S4
resolver
activity_regulation
ACTIVITY 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). Isoform 2: Constitutively active (By similarity). {ECO:0000250|UniProtKB:Q02956}.
uniprot
proteins
amino_acid_sequence
MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
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 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'. Phosphorylates VAMP2 in vitro (PubMed:17313651). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231). {ECO:0000269|PubMed:11035106, ECO:0000269|PubMed:12162751, ECO:0000269|PubMed:15084291, ECO:0000269|PubMed:15324659, ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:36040231, ECO:0000269|PubMed:9447975}.; FUNCTION: [Isoform 2]: Involved in late synaptic long term potention phase in CA1 hippocampal cells and long term memory maintenance. {ECO:0000250|UniProtKB:Q02956}.
uniprot
proteins
mass_dalton
67660
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="K->A: No effect on interaction with SQSTM1 and PARD6B."; /evidence="ECO:0000269|PubMed:12887891"; MUTAGEN 62; /note="D->A: Loss of interaction with SQSTM1 and PARD6B."; /evidence="ECO:0000269|PubMed:12887891"; MUTAGEN 66; /note="D->A: Loss of interaction with SQSTM1 and PARD6B."; /evidence="ECO:0000269|PubMed:12887891
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:11781095, ECO:0000269|PubMed:15314172, ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:9768361}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
PKC subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10356400
uniprot
proteins
pubmed
11035106
uniprot
proteins
pubmed
11260256
uniprot
proteins
pubmed
11755531
uniprot
proteins
pubmed
11781095
uniprot
proteins
pubmed
12162751
uniprot
proteins
pubmed
12234671
uniprot
proteins
pubmed
12761192
uniprot
proteins
pubmed
12887891
uniprot
proteins
pubmed
12893243
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15084291
uniprot
proteins
pubmed
15314172
uniprot
proteins
pubmed
15324659
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16322752
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16792529
uniprot
proteins
pubmed
16903823
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17313651
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18190796
uniprot
proteins
pubmed
18321849
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20332120
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24682284
uniprot
proteins
pubmed
26583432
uniprot
proteins
pubmed
31519760
uniprot
proteins
pubmed
36040231
uniprot
proteins
pubmed
7597083
uniprot
proteins
pubmed
8224878
uniprot
proteins
pubmed
8375396
uniprot
proteins
pubmed
9447975
uniprot
proteins
pubmed
9566925
uniprot
proteins
pubmed
9768361
uniprot
proteins
sequence_length
592
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:9566925}. Endosome {ECO:0000269|PubMed:9566925}. Cell junction {ECO:0000269|PubMed:7597083}. Membrane {ECO:0000250|UniProtKB:P09217}; Peripheral membrane protein {ECO:0000305}. Note=In the retina, localizes in the terminals of the rod bipolar cells (By similarity). Associates with endosomes (PubMed:9566925). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (PubMed:7597083). Colocalizes with VAMP2 and WDFY2 in intracellular vesicles (PubMed:17313651). Transiently translocates to the membrane of CA1 hippocampal cells in response to the induction of long term potentiation (By similarity). {ECO:0000250|UniProtKB:P09217, ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:7597083, ECO:0000269|PubMed:9566925}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:P09217}.
uniprot
proteins