UniProtKB - Q8BWW9 (PKN2_MOUSE)
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Protein
Serine/threonine-protein kinase N2
Gene
Pkn2
Organism
Mus musculus (Mouse)
Status
Functioni
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).By similarity3 Publications
Catalytic activityi
ATP + a protein = ADP + a phosphoprotein.
Enzyme regulationi
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).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 685 | ATPPROSITE-ProRule annotation | 1 | |
Active sitei | 781 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 662 – 670 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cadherin binding Source: MGI
- GTP-Rho binding Source: InterPro
- histone deacetylase binding Source: UniProtKB
- kinase activity Source: MGI
- protein kinase C activity Source: UniProtKB-EC
- protein serine/threonine kinase activity Source: UniProtKB
- RNA polymerase binding Source: MGI
GO - Biological processi
- apical junction assembly Source: UniProtKB
- apoptotic process Source: UniProtKB-KW
- cell adhesion Source: UniProtKB-KW
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- cell projection organization Source: UniProtKB-KW
- epithelial cell migration Source: UniProtKB
- intracellular signal transduction Source: GO_Central
- peptidyl-serine phosphorylation Source: GO_Central
- positive regulation of cytokinesis Source: UniProtKB
- positive regulation of mitotic cell cycle Source: UniProtKB
- positive regulation of viral genome replication Source: MGI
- protein phosphorylation Source: UniProtKB
- regulation of cell motility Source: UniProtKB
- regulation of transcription, DNA-templated Source: UniProtKB-KW
- transcription, DNA-templated Source: UniProtKB-KW
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Apoptosis, Cell adhesion, Cell cycle, Cell division, Cilium biogenesis/degradation, Transcription, Transcription regulation |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-MMU-5625740. RHO GTPases activate PKNs. |
Names & Taxonomyi
Protein namesi | Recommended name: Serine/threonine-protein kinase N2 (EC:2.7.11.13)Alternative name(s): PKN gamma Protein kinase C-like 2 Protein-kinase C-related kinase 2 |
Gene namesi | Name:Pkn2 Synonyms:Prk2, Prkcl2 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:109211. Pkn2. |
Subcellular locationi
Keywords - Cellular componenti
Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 66 | A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155. 1 Publication | 1 | |
Mutagenesisi | 155 | A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60. 1 Publication | 1 | |
Mutagenesisi | 685 | K → M: Prevents apical junction formation. 1 Publication | 1 | |
Mutagenesisi | 781 | D → A: Prevents apical junction formation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000055723 | 1 – 983 | Serine/threonine-protein kinase N2Add BLAST | 983 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 77 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 110 | PhosphoserineBy similarity | 1 | |
Modified residuei | 121 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 124 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 301 | PhosphoserineBy similarity | 1 | |
Modified residuei | 305 | PhosphoserineBy similarity | 1 | |
Modified residuei | 359 | PhosphoserineBy similarity | 1 | |
Modified residuei | 361 | PhosphoserineBy similarity | 1 | |
Modified residuei | 534 | PhosphoserineBy similarity | 1 | |
Modified residuei | 582 | PhosphoserineBy similarity | 1 | |
Modified residuei | 619 | PhosphoserineCombined sources | 1 | |
Modified residuei | 630 | PhosphoserineBy similarity | 1 | |
Modified residuei | 815 | Phosphothreonine; by PDPK1By similarity | 1 | |
Modified residuei | 951 | PhosphoserineBy similarity | 1 | |
Modified residuei | 957 | PhosphothreonineCombined sources | 1 |
Post-translational modificationi
Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Phosphorylated by CDK10 (By similarity).By similarity
Activated by limited proteolysis with trypsin. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 117 – 118 | Cleavage; by caspase-3By similarity | 2 | |
Sitei | 699 – 700 | Cleavage; by caspase-3By similarity | 2 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q8BWW9. |
PaxDbi | Q8BWW9. |
PeptideAtlasi | Q8BWW9. |
PRIDEi | Q8BWW9. |
PTM databases
iPTMneti | Q8BWW9. |
PhosphoSitePlusi | Q8BWW9. |
Expressioni
Tissue specificityi
Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous.4 Publications
Gene expression databases
Bgeei | ENSMUSG00000004591. |
CleanExi | MM_PKN2. |
ExpressionAtlasi | Q8BWW9. baseline and differential. |
Genevisiblei | Q8BWW9. MM. |
Interactioni
Subunit structurei
Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially) and interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation (PubMed:17403031, PubMed:20974804). Interacts with NCK1 (via SH3 domains) (PubMed:8910519). Interacts with RHOC. Interacts with NCK1 and NCK2 (By similarity). Interacts with CD44 (PubMed:17403031). Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity (By similarity). Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity (PubMed:10818102). Interacts (via C-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with CDK10 (By similarity).By similarity4 Publications
GO - Molecular functioni
- cadherin binding Source: MGI
- GTP-Rho binding Source: InterPro
- histone deacetylase binding Source: UniProtKB
- RNA polymerase binding Source: MGI
Protein-protein interaction databases
BioGridi | 224651. 2 interactors. |
STRINGi | 10090.ENSMUSP00000039566. |
Structurei
3D structure databases
ProteinModelPortali | Q8BWW9. |
SMRi | Q8BWW9. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 44 – 119 | REM 1Add BLAST | 76 | |
Repeati | 133 – 213 | REM 2Add BLAST | 81 | |
Repeati | 214 – 295 | REM 3Add BLAST | 82 | |
Domaini | 329 – 462 | C2Add BLAST | 134 | |
Domaini | 656 – 915 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 260 | |
Domaini | 916 – 983 | AGC-kinase C-terminalAdd BLAST | 68 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 381 – 462 | Necessary to rescue apical junction formationAdd BLAST | 82 | |
Regioni | 916 – 976 | Necessary for the catalytic activityBy similarityAdd BLAST | 61 | |
Regioni | 977 – 983 | Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoABy similarity | 7 |
Domaini
The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2.By similarity
The C1 domain does not bind the diacylglycerol (DAG).
The apoptotic C-terminal cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations.By similarity
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG0694. Eukaryota. ENOG410XNPH. LUCA. |
GeneTreei | ENSGT00820000126964. |
HOGENOMi | HOG000233032. |
HOVERGENi | HBG108317. |
InParanoidi | Q8BWW9. |
KOi | K06071. |
OMAi | RSQQMFQ. |
OrthoDBi | EOG091G00YT. |
TreeFami | TF102005. |
Family and domain databases
CDDi | cd08687. C2_PKN-like. 1 hit. cd11622. HR1_PKN_1. 1 hit. |
InterProi | View protein in InterPro IPR000961. AGC-kinase_C. IPR000008. C2_dom. IPR037784. C2_PKN. IPR011072. HR1_rho-bd. IPR036274. HR1_rpt_sf. IPR011009. Kinase-like_dom_sf. IPR017892. Pkinase_C. IPR037313. PKN_HR1_1. IPR000719. Prot_kinase_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. |
Pfami | View protein in Pfam PF02185. HR1. 3 hits. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. |
SMARTi | View protein in SMART SM00239. C2. 1 hit. SM00742. Hr1. 3 hits. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. |
SUPFAMi | SSF46585. SSF46585. 3 hits. SSF56112. SSF56112. 1 hit. |
PROSITEi | View protein in PROSITE PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q8BWW9-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD
60 70 80 90 100
RIKREIRKEL KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL
110 120 130 140 150
QELNAHIVVS DPEDSTDCPR TPDTPNSDSR SSTSNNRLMA LQKQLDIELK
160 170 180 190 200
VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL QDSKTKIEVI RMQILQAVQT
210 220 230 240 250
NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM KLLGSGKVTD
260 270 280 290 300
RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA
310 320 330 340 350
SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA
360 370 380 390 400
TSVALPGWSP SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN
410 420 430 440 450
TVVGQTSWKP ISNQSWDQKF TLELDRSREL EISVYWRDWR SLCAVKFLRL
460 470 480 490 500
EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP VIERRPKLQR QKKIFSKQQG
510 520 530 540 550
KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP ATVPVVDARI
560 570 580 590 600
PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ
610 620 630 640 650
GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ
660 670 680 690 700
FSLQDFRCCA VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS
710 720 730 740 750
LMCEKRIFET VNSVRHPFLV NLFACFQTKE HVCFVMEYAA GGDLMMHIHT
760 770 780 790 800
DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR DLKLDNLLLD TEGFVKIADF
810 820 830 840 850
GLCKEGMGYG DRTSTFCGTP EFLAPEVLTE TSYTRAVDWW GLGVLIYEML
860 870 880 890 900
VGESPFPGDD EEEVFDSIVN DEVRYPRFLS TEAISIMRRL LRRNPERRLG
910 920 930 940 950
AGEKDAEDVK KHPFFRLTDW SALMDKKVKP PFVPTIRGRE DVSNFDDEFT
960 970 980
SEAPILTPPR EPRILLEEEQ EMFHDFDYVA DWC
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 32 | Q → H in BAC32655 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 84 | N → H in BAC33888 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 395 | V → D in BAC38910 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 569 | L → F in BAC32655 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 704 | E → K in BAC33888 (PubMed:16141072).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_012042 | 35 – 45 | Missing in isoform 2. 1 PublicationAdd BLAST | 11 | |
Alternative sequenceiVSP_042185 | 781 – 787 | DLKLDNL → NTIFSSI in isoform 3. 1 Publication | 7 | |
Alternative sequenceiVSP_042186 | 788 – 983 | Missing in isoform 3. 1 PublicationAdd BLAST | 196 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK046248 mRNA. Translation: BAC32655.1. AK133298 mRNA. Translation: BAE21599.1. AK171092 mRNA. Translation: BAE42244.1. AK049713 mRNA. Translation: BAC33888.1. AK083425 mRNA. Translation: BAC38910.1. BC052073 mRNA. Translation: AAH52073.1. |
CCDSi | CCDS51084.1. [Q8BWW9-1] |
RefSeqi | NP_848769.2. NM_178654.4. [Q8BWW9-1] |
UniGenei | Mm.244236. |
Genome annotation databases
Ensembli | ENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591. [Q8BWW9-1] |
GeneIDi | 109333. |
KEGGi | mmu:109333. |
UCSCi | uc008rpe.2. mouse. [Q8BWW9-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | PKN2_MOUSE | |
Accessioni | Q8BWW9Primary (citable) accession number: Q8BWW9 Secondary accession number(s): Q3TBR3 Q8BL62 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 23, 2004 |
Last sequence update: | July 27, 2011 | |
Last modified: | March 28, 2018 | |
This is version 146 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |