| IED ID | IndEnz0002013298 |
| Enzyme Type ID | protease013298 |
| Protein Name |
Serine/threonine-protein kinase N2 EC 2.7.11.13 Cardiolipin-activated protein kinase Pak2 PKN gamma Protease-activated kinase 2 PAK-2 Protein kinase C-like 2 Protein-kinase C-related kinase 2 p140 kinase |
| Gene Name | Pkn2 Pak2 Prk2 Prkcl2 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MASNPDRGEILLTELQVDSRPLPFSENVSAVQKLDFSDTIVQQKLDDVKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDYTDCPRTPDTPNSDSRSSTSNNRRLMALQKQLDIELKVKQGAENMIQMYSNGPSKDRKLHGTAQQLLQDNKTKIEVIRMHILQAVLTNELAFDNAKPVISPLELRNGRIIEHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYSTLSKPAALTGTLEVRLWGAKISWENVPGRSKATSVALPGWSPSENRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTIWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMALYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQTPVPATVPVVDARTPELAPPASDSTVTKLDFDLEPEAPPAPPRASSLGEIDDSSELRVLDIPGQGSETVFDIENDRNNMRPKSKSEYELNIPDSSRSCWSVGELEDKRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEASVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLTDWSALLDKKVKPPFVPTIRGREDVSNFDDEFTSEAPILTPPREPRILLEEEQEMFRDFDYVADWC |
| Enzyme Length | 985 |
| Uniprot Accession Number | O08874 |
| Absorption | |
| Active Site | ACT_SITE 783; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027" |
| 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-817 (activation loop of the kinase domain) and Thr-959 (turn motif), need to be phosphorylated for its full activation (By similarity). {ECO:0000250|UniProtKB:Q16513}. |
| Binding Site | BINDING 687; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; |
| DNA Binding | |
| EC Number | 2.7.11.13 |
| Enzyme 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. {ECO:0000250|UniProtKB:Q16513}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 664..672; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| Features | Active site (1); Binding site (1); Chain (1); Compositional bias (2); Domain (6); Modified residue (15); Nucleotide binding (1); Region (6); Site (2) |
| Keywords | ATP-binding;Acetylation;Apoptosis;Cell adhesion;Cell cycle;Cell division;Cell junction;Cell projection;Cilium biogenesis/degradation;Coiled coil;Cytoplasm;Cytoskeleton;Direct protein sequencing;Kinase;Membrane;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16513}. Nucleus {ECO:0000250|UniProtKB:Q16513}. Membrane {ECO:0000250|UniProtKB:Q8BWW9}. 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}. |
| Modified Residue | MOD_RES 77; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q8BWW9; MOD_RES 110; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 121; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 124; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 303; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 307; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 361; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 363; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 536; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 584; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 621; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8BWW9; MOD_RES 632; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 817; /note=Phosphothreonine; by PDPK1; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 953; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q16513; MOD_RES 959; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Binding to Rho and Rac promotes autophosphorylation and phosphorylation on serine and threonine residues. Phosphorylated by CDK10 (By similarity). {ECO:0000250|UniProtKB:Q16513, ECO:0000269|PubMed:9121475}.; PTM: Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death (By similarity). Activated by limited proteolysis with trypsin. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17446865; 8051089; |
| Motif | |
| Gene Encoded By | |
| Mass | 112,069 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17989; RHEA:46608 |
| Cross Reference Brenda |