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UniProtKB - Q8BWW9 (PKN2_MOUSE)

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Protein

Serine/threonine-protein kinase N2

Gene

Pkn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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).3 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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei685ATPPROSITE-ProRule annotation1
Active sitei781Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi662 – 670ATPPROSITE-ProRule annotation9

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell adhesion, Cell cycle, Cell division, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:109211. Pkn2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus By similarity
  • Membrane 1 Publication
  • Cell projection › lamellipodium By similarity
  • Cytoplasm › cytoskeleton By similarity
  • Cleavage furrow By similarity
  • Midbody By similarity
  • Cell junction By similarity

    • 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.By similarity

GO - Cellular componenti

  • apical junction complex Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: MGI
  • cytoskeleton Source: UniProtKB-SubCell
  • lamellipodium Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
  • midbody Source: UniProtKB
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi66A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155. 1 Publication1
Mutagenesisi155A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60. 1 Publication1
Mutagenesisi685K → M: Prevents apical junction formation. 1 Publication1
Mutagenesisi781D → A: Prevents apical junction formation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000557231 – 983Serine/threonine-protein kinase N2Add BLAST983

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei77N6-acetyllysineCombined sources1
Modified residuei110PhosphoserineBy similarity1
Modified residuei121PhosphothreonineBy similarity1
Modified residuei124PhosphothreonineBy similarity1
Modified residuei301PhosphoserineBy similarity1
Modified residuei305PhosphoserineBy similarity1
Modified residuei359PhosphoserineBy similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei534PhosphoserineBy similarity1
Modified residuei582PhosphoserineBy similarity1
Modified residuei619PhosphoserineCombined sources1
Modified residuei630PhosphoserineBy similarity1
Modified residuei815Phosphothreonine; by PDPK1By similarity1
Modified residuei951PhosphoserineBy similarity1
Modified residuei957PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated.By similarity
Activated by limited proteolysis with trypsin. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei117 – 118Cleavage; by caspase-3By similarity2
Sitei699 – 700Cleavage; by caspase-3By similarity2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BWW9.
PaxDbiQ8BWW9.
PeptideAtlasiQ8BWW9.
PRIDEiQ8BWW9.

PTM databases

iPTMnetiQ8BWW9.
PhosphoSitePlusiQ8BWW9.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous.4 Publications

Gene expression databases

BgeeiENSMUSG00000004591.
CleanExiMM_PKN2.
ExpressionAtlasiQ8BWW9. baseline and differential.
GenevisibleiQ8BWW9. MM.

Interactioni

Subunit structurei

Interacts with RHOA (GTP-bound form preferentially) and RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation. Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity. 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 NCK1, NCK2 and RHOC (By similarity). Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially). Interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially). Interacts with NCK1 (via SH3 domains). Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity. Interacts with CD44.By similarity4 Publications

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi224651. 1 interactor.
STRINGi10090.ENSMUSP00000039566.

Structurei

3D structure databases

ProteinModelPortaliQ8BWW9.
SMRiQ8BWW9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati44 – 119REM 1Add BLAST76
Repeati133 – 213REM 2Add BLAST81
Repeati214 – 295REM 3Add BLAST82
Domaini329 – 462C2Add BLAST134
Domaini656 – 915Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini916 – 983AGC-kinase C-terminalAdd BLAST68

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni381 – 462Necessary to rescue apical junction formationAdd BLAST82
Regioni916 – 976Necessary for the catalytic activityBy similarityAdd BLAST61
Regioni977 – 983Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoABy similarity7

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

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ8BWW9.
KOiK06071.
OMAiRSQQMFQ.
OrthoDBiEOG091G00YT.
TreeFamiTF102005.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiView protein in InterPro
IPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
SMARTiView protein in SMART
SM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView 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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative 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.

« Hide

        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
Length:983
Mass (Da):111,607
Last modified:July 27, 2011 - v3
Checksum:i3961FD79D2718609
GO
Isoform 2 (identifier: Q8BWW9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-45: Missing.

Note: No experimental confirmation available.
Show »
Length:972
Mass (Da):110,313
Checksum:iD2806BCD710C1B29
GO
Isoform 3 (identifier: Q8BWW9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     781-787: DLKLDNL → NTIFSSI
     788-983: Missing.

Show »
Length:787
Mass (Da):88,961
Checksum:i6B762C942B96D5EF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32Q → H in BAC32655 (PubMed:16141072).Curated1
Sequence conflicti84N → H in BAC33888 (PubMed:16141072).Curated1
Sequence conflicti395V → D in BAC38910 (PubMed:16141072).Curated1
Sequence conflicti569L → F in BAC32655 (PubMed:16141072).Curated1
Sequence conflicti704E → K in BAC33888 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01204235 – 45Missing in isoform 2. 1 PublicationAdd BLAST11
Alternative sequenceiVSP_042185781 – 787DLKLDNL → NTIFSSI in isoform 3. 1 Publication7
Alternative sequenceiVSP_042186788 – 983Missing in isoform 3. 1 PublicationAdd BLAST196

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.
CCDSiCCDS51084.1. [Q8BWW9-1]
RefSeqiNP_848769.2. NM_178654.4. [Q8BWW9-1]
UniGeneiMm.244236.

Genome annotation databases

EnsembliENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591. [Q8BWW9-1]
GeneIDi109333.
KEGGimmu:109333.
UCSCiuc008rpe.2. mouse. [Q8BWW9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

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.
CCDSiCCDS51084.1. [Q8BWW9-1]
RefSeqiNP_848769.2. NM_178654.4. [Q8BWW9-1]
UniGeneiMm.244236.

3D structure databases

ProteinModelPortaliQ8BWW9.
SMRiQ8BWW9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224651. 1 interactor.
STRINGi10090.ENSMUSP00000039566.

PTM databases

iPTMnetiQ8BWW9.
PhosphoSitePlusiQ8BWW9.

Proteomic databases

EPDiQ8BWW9.
PaxDbiQ8BWW9.
PeptideAtlasiQ8BWW9.
PRIDEiQ8BWW9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043812; ENSMUSP00000039566; ENSMUSG00000004591. [Q8BWW9-1]
GeneIDi109333.
KEGGimmu:109333.
UCSCiuc008rpe.2. mouse. [Q8BWW9-1]

Organism-specific databases

CTDi5586.
MGIiMGI:109211. Pkn2.

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ8BWW9.
KOiK06071.
OMAiRSQQMFQ.
OrthoDBiEOG091G00YT.
TreeFamiTF102005.

Enzyme and pathway databases

ReactomeiR-MMU-5625740. RHO GTPases activate PKNs.

Miscellaneous databases

ChiTaRSiPkn2. mouse.
PROiPR:Q8BWW9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004591.
CleanExiMM_PKN2.
ExpressionAtlasiQ8BWW9. baseline and differential.
GenevisibleiQ8BWW9. MM.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiView protein in InterPro
IPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
SMARTiView protein in SMART
SM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView 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.
ProtoNetiSearch...

Entry informationi

Entry nameiPKN2_MOUSE
AccessioniPrimary (citable) accession number: Q8BWW9
Secondary accession number(s): Q3TBR3
, Q80WS2, Q8BJL7, Q8BL62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 27, 2011
Last modified: June 7, 2017
This is version 139 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.