PKN2
entrez
5586
canonical
uniprot
Q16513
canonical
ensembl
ENSG00000065243
resolver
ensp
ENSP00000359544
resolver
ensp
ENSP00000359552
resolver
ensp
ENSP00000536402
resolver
genesymbol
PKN2
resolver
genesymbol_syn
PRK2
resolver
genesymbol_syn
PRKCL2
resolver
hgnc
HGNC:9406
resolver
uniprot
B4DQ21
resolver
uniprot
B4DTP5
resolver
uniprot
B4DVG1
resolver
uniprot
D3DT24
resolver
uniprot
Q08AF4
resolver
uniprot
Q9H1W4
resolver
uniprot_entry
PKN2_HUMAN
resolver
uniprot_sec
B4DQ21
resolver
uniprot_sec
B4DTP5
resolver
uniprot_sec
B4DVG1
resolver
uniprot_sec
D3DT24
resolver
uniprot_sec
Q08AF4
resolver
uniprot_sec
Q9H1W4
resolver
activity_regulation
ACTIVITY REGULATION: Kinase activity is activated upon binding to GTP-bound Rhoa/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-816 (activation loop of the kinase domain) and Thr-958 (turn motif), need to be phosphorylated for its full activation. {ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:18835241, ECO:0000269|PubMed:9368003}.
uniprot
proteins
amino_acid_sequence
MASNPERGEILLTELQGDSRSLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDITDCPRTPDTPNNDPRCSTSNNRLKALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNEVPKNHPKSRIIIEELSLVAASPTLSPRQSMISTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSETRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQAPVPTTVPVVDVRIPQLAPPASDSTVTKLDFDLEPEPPPAPPRASSLGEIDESSELRVLDIPGQDSETVFDIQNDRNSILPKSQSEYKPDTPQSGLEYSGIQELEDRRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKNTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGASEKDAEDVKKHPFFRLIDWSALMDKKVKPPFIPTIRGREDVSNFDDEFTSEAPILTPPREPRILSEEEQEMFRDFDYIADWC
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (PubMed:27104747). {ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:11781095, ECO:0000269|PubMed:15123640, ECO:0000269|PubMed:15364941, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:27104747, ECO:0000269|PubMed:9121475}.; FUNCTION: (Microbial infection) Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. {ECO:0000269|PubMed:15364941}.
uniprot
proteins
mass_dalton
112035
uniprot
proteins
mutagenesis
MUTAGEN 117; /note="D->A: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700."; /evidence="ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:9368003"; MUTAGEN 121; /note="T->A: Does not suppress ciliogenesis; when associated with A-124."; /evidence="ECO:0000269|PubMed:27104747"; MUTAGEN 124; /note="T->A: Does not suppress ciliogenesis; when associated with A-121."; /evidence="ECO:0000269|PubMed:27104747"; MUTAGEN 686; /note="K->R: Does not inhibit interaction with PTPN13."; /evidence="ECO:0000269|PubMed:11356191"; MUTAGEN 700; /note="D->E: Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117."; /evidence="ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:9368003"; MUTAGEN 816; /note="T->A: Reduces catalytic activity."; /evidence="ECO:0000269|PubMed:18835241"; MUTAGEN 958; /note="T->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:18835241"; MUTAGEN 974; /note="F->A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'."; /evidence="ECO:0000269|PubMed:10226025"; MUTAGEN 977; /note="F->A,L: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 977; /note="F->W,Y: Reduces catalytic activity by 50%."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 978; /note="D->A,S: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 978; /note="D->A: Does not inhibit catalytic activity."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 979; /note="Y->A: Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 979; /note="Y->A: Reduces catalytic activity by 50%."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 979; /note="Y->F,L,W: Reduces catalytic activity by 25%."; /evidence="ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:18835241"; MUTAGEN 984; /note="C->S: Inhibits interaction with PTPN13."; /evidence="ECO:0000269|PubMed:11356191
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. Phosphorylated during mitosis. Phosphorylated by CDK10 (PubMed:27104747). {ECO:0000269|PubMed:10792047, ECO:0000269|PubMed:17332740, ECO:0000269|PubMed:27104747}.; PTM: Activated by limited proteolysis with trypsin (By similarity). Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death. {ECO:0000250, ECO:0000269|PubMed:9368003}.
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
10026169
uniprot
proteins
pubmed
10226025
uniprot
proteins
pubmed
10792047
uniprot
proteins
pubmed
10818102
uniprot
proteins
pubmed
10926925
uniprot
proteins
pubmed
11356191
uniprot
proteins
pubmed
11777936
uniprot
proteins
pubmed
11781095
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15123640
uniprot
proteins
pubmed
15364941
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17332740
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18835241
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20188095
uniprot
proteins
pubmed
20974804
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21754995
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27104747
uniprot
proteins
pubmed
7851406
uniprot
proteins
pubmed
7988719
uniprot
proteins
pubmed
9121475
uniprot
proteins
pubmed
9368003
uniprot
proteins
sequence_length
984
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11356191, ECO:0000269|PubMed:17332740}. Nucleus {ECO:0000269|PubMed:11356191}. Membrane {ECO:0000250|UniProtKB:Q8BWW9}. Cell projection, lamellipodium {ECO:0000269|PubMed:11356191}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11356191}. Cleavage furrow {ECO:0000269|PubMed:17332740}. Midbody {ECO:0000269|PubMed:17332740}. Cell junction {ECO:0000269|PubMed:20974804}. Note=Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells. In the course of viral infection, colocalizes with HCV NS5B at perinuclear region in the cytoplasm. {ECO:0000269|PubMed:11356191, ECO:0000269|PubMed:17332740}.
uniprot
proteins