Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase N2

Gene

Pkn2

Organism
Rattus norvegicus (Rat)
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) (By similarity).By similarity

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-817 (activation loop of the kinase domain) and Thr-959 (turn motif), need to be phosphorylated for its full activation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei687 – 6871ATPPROSITE-ProRule annotation
Active sitei783 – 7831Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi664 – 6729ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell adhesion, Cell cycle, Cell division, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase N2 (EC:2.7.11.13)
Alternative name(s):
Cardiolipin-activated protein kinase Pak2
PKN gamma
Protease-activated kinase 2
Short name:
PAK-2
Protein kinase C-like 2
Protein-kinase C-related kinase 2
p140 kinase
Gene namesi
Name:Pkn2
Synonyms:Pak2, Prk2, Prkcl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620146. Pkn2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Membrane By similarity
  • Cell projectionlamellipodium By similarity
  • Cytoplasmcytoskeleton 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

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 985985Serine/threonine-protein kinase N2PRO_0000055724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei121 – 1211PhosphothreonineBy similarity
Modified residuei124 – 1241PhosphothreonineBy similarity
Modified residuei303 – 3031PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei361 – 3611PhosphoserineBy similarity
Modified residuei363 – 3631PhosphoserineBy similarity
Modified residuei536 – 5361PhosphoserineBy similarity
Modified residuei584 – 5841PhosphoserineCombined sources
Modified residuei621 – 6211PhosphoserineBy similarity
Modified residuei632 – 6321PhosphoserineBy similarity
Modified residuei817 – 8171Phosphothreonine; by PDPK1By similarity
Modified residuei953 – 9531PhosphoserineBy similarity
Modified residuei959 – 9591PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Binding to Rho and Rac promotes autophosphorylation and phosphorylation on serine and threonine residues.By similarity1 Publication
Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death (By similarity). Activated by limited proteolysis with trypsin.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei117 – 1182Cleavage; by caspase-3By similarity
Sitei701 – 7022Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO08874.
PRIDEiO08874.

PTM databases

iPTMnetiO08874.
PhosphoSiteiO08874.

Expressioni

Tissue specificityi

Expressed in liver (at protein level).2 Publications

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 similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiO08874. 1 interaction.
MINTiMINT-4781977.
STRINGi10116.ENSRNOP00000034133.

Structurei

3D structure databases

ProteinModelPortaliO08874.
SMRiO08874. Positions 130-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati47 – 11973REM 1Add
BLAST
Repeati137 – 21478REM 2Add
BLAST
Repeati219 – 29678REM 3Add
BLAST
Domaini373 – 46492C2Add
BLAST
Domaini658 – 917260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini918 – 98568AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 46482Necessary to rescue apical junction formationBy similarityAdd
BLAST
Regioni918 – 97861Necessary for the catalytic activityBy similarityAdd
BLAST
Regioni979 – 9857Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoABy similarity

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

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 3 REM (Hr1) repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiO08874.
PhylomeDBiO08874.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 1 hit.
InterProiIPR000961. 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.
[Graphical view]
PfamiPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNPDRGEI LLTELQVDSR PLPFSENVSA VQKLDFSDTI VQQKLDDVKD
60 70 80 90 100
RIKREIRKEL KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL
110 120 130 140 150
QELNAHIVVS DPEDYTDCPR TPDTPNSDSR SSTSNNRRLM ALQKQLDIEL
160 170 180 190 200
KVKQGAENMI QMYSNGPSKD RKLHGTAQQL LQDNKTKIEV IRMHILQAVL
210 220 230 240 250
TNELAFDNAK PVISPLELRN GRIIEHHFRI EFAVAEGAKN VMKLLGSGKV
260 270 280 290 300
TDRKALSEAQ ARFNESSQKL DLLKYSLEQR LNELPKNHPK SSVVIEELSL
310 320 330 340 350
VASPTLSPRQ SMLSTQNQYS TLSKPAALTG TLEVRLWGAK ISWENVPGRS
360 370 380 390 400
KATSVALPGW SPSENRSSFM SRTSKSKSGS SRNLLKTDDL SNDVCAVLKL
410 420 430 440 450
DNTVVGQTIW KPISNQSWDQ KFTLELDRSR ELEISVYWRD WRSLCAVKFL
460 470 480 490 500
RLEDFLDNQR HGMALYLEPQ GTLFAEVTFF NPVIERRPKL QRQKKIFSKQ
510 520 530 540 550
QGKTFLRAPQ MNINIATWGR LVRRAIPTVN HSGTFSPQTP VPATVPVVDA
560 570 580 590 600
RTPELAPPAS DSTVTKLDFD LEPEAPPAPP RASSLGEIDD SSELRVLDIP
610 620 630 640 650
GQGSETVFDI ENDRNNMRPK SKSEYELNIP DSSRSCWSVG ELEDKRSQQR
660 670 680 690 700
FQFNLQDFRC CAVLGRGHFG KVLLAEYKHT NEMFAIKALK KGDIVARDEV
710 720 730 740 750
DSLMCEKRIF ETVNSVRHPF LVNLFACFQT KEHVCFVMEY AAGGDLMMHI
760 770 780 790 800
HTDVFSEPRA VFYAACVVLG LQYLHEHKIV YRDLKLDNLL LDTEASVKIA
810 820 830 840 850
DFGLCKEGMG YGDRTSTFCG TPEFLAPEVL TETSYTRAVD WWGLGVLIYE
860 870 880 890 900
MLVGESPFPG DDEEEVFDSI VNDEVRYPRF LSTEAISIMR RLLRRNPERR
910 920 930 940 950
LGAGEKDAED VKKHPFFRLT DWSALLDKKV KPPFVPTIRG REDVSNFDDE
960 970 980
FTSEAPILTP PREPRILLEE EQEMFRDFDY VADWC
Length:985
Mass (Da):112,069
Last modified:January 9, 2007 - v2
Checksum:iAE71D30379715C3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012350 Genomic DNA. No translation available.
AABR03012657 Genomic DNA. No translation available.
U75358 mRNA. Translation: AAB53364.1.
UniGeneiRn.30325.

Genome annotation databases

UCSCiRGD:620146. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012350 Genomic DNA. No translation available.
AABR03012657 Genomic DNA. No translation available.
U75358 mRNA. Translation: AAB53364.1.
UniGeneiRn.30325.

3D structure databases

ProteinModelPortaliO08874.
SMRiO08874. Positions 130-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08874. 1 interaction.
MINTiMINT-4781977.
STRINGi10116.ENSRNOP00000034133.

PTM databases

iPTMnetiO08874.
PhosphoSiteiO08874.

Proteomic databases

PaxDbiO08874.
PRIDEiO08874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620146. rat.

Organism-specific databases

RGDi620146. Pkn2.

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiO08874.
PhylomeDBiO08874.

Miscellaneous databases

PROiO08874.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 1 hit.
InterProiIPR000961. 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.
[Graphical view]
PfamiPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF46585. SSF46585. 3 hits.
SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPKN2_RAT
AccessioniPrimary (citable) accession number: O08874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.