Pkn2
entrez
109333
canonical
uniprot
Q8BWW9
canonical
ensembl
ENSMUSG00000004591
resolver
ensp
ENSMUSP00000039566
resolver
genesymbol
Pkn2
resolver
genesymbol_syn
Prk2
resolver
genesymbol_syn
Prkcl2
resolver
uniprot
Q3TBR3
resolver
uniprot
Q80WS2
resolver
uniprot
Q8BJL7
resolver
uniprot
Q8BL62
resolver
uniprot_entry
PKN2_MOUSE
resolver
uniprot_sec
Q3TBR3
resolver
uniprot_sec
Q80WS2
resolver
uniprot_sec
Q8BJL7
resolver
uniprot_sec
Q8BL62
resolver
activity_regulation
ACTIVITY REGULATION: Kinase activity is activated upon binding to GTP-bound Rho1/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-815 (activation loop of the kinase domain) and Thr-957 (turn motif), need to be phosphorylated for its full activation (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MASNPDRGEILLTELQGDSRTLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDSTDCPRTPDTPNSDSRSSTSNNRLMALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFKIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPRNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSDNRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQTPVPATVPVVDARIPDLAPPASDSTVTKLDFDLEPEPPPAPPRASSLGETDESSELRVLDIPGQGSETVFNIENDRNNLRPKSKSEYELSIPDSGRSCWGVGELDDKRAQQRFQFSLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLTDWSALMDKKVKPPFVPTIRGREDVSNFDDEFTSEAPILTPPREPRILLEEEQEMFHDFDYVADWC
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 (By similarity). {ECO:0000250|UniProtKB:Q16513, ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519}.
uniprot
proteins
mass_dalton
111607
uniprot
proteins
mutagenesis
MUTAGEN 66; /note="A->K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155."; /evidence="ECO:0000269|PubMed:20974804"; MUTAGEN 155; /note="A->K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60."; /evidence="ECO:0000269|PubMed:20974804"; MUTAGEN 685; /note="K->M: Prevents apical junction formation."; /evidence="ECO:0000269|PubMed:20974804"; MUTAGEN 781; /note="D->A: Prevents apical junction formation."; /evidence="ECO:0000269|PubMed:20974804
uniprot
proteins
post_translational_modification
PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Phosphorylated by CDK10 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16513}.; PTM: Activated by limited proteolysis with trypsin. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death. {ECO:0000250}.
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
10818102
uniprot
proteins
pubmed
11777936
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17403031
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20974804
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
8910519
uniprot
proteins
pubmed
9121475
uniprot
proteins
sequence_length
983
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9121475}. Nucleus {ECO:0000250|UniProtKB:Q16513}. Membrane {ECO:0000269|PubMed:9121475}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q16513}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16513}. Cleavage furrow {ECO:0000250|UniProtKB:Q16513}. Midbody {ECO:0000250|UniProtKB:Q16513}. Cell junction {ECO:0000250|UniProtKB:Q16513}. 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. {ECO:0000250|UniProtKB:Q16513}.
uniprot
proteins