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O08874 (PKN2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Pkn2
Synonyms:Pak2, Prk2, Prkcl2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length985 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 associates 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.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme 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. Ref.2

Subcellular location

Cytoplasm. Nucleus By similarity. Membrane By similarity. 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.

Tissue specificity

Expressed in liver (at protein level). Ref.2 Ref.3

Domain

The N-terminus region interferes with the interaction between AKT1 and the C-terminus region of PKN2 By similarity.

The C1 domain does not bind the diacylglycerol (DAG).

The apoptotic C-terminus cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, pyruvate dehydrogenase kinase PDK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations By similarity.

Post-translational modification

Phosphorylated during mitosis By similarity. Autophosphorylated. Phosphorylated. Binding to Rho and Rac promotes autophosphorylation and phosphorylation on serine and threonine residues. Ref.3

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

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 1 protein kinase domain.

Contains 3 REM (Hr1) repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 985984Serine/threonine-protein kinase N2
PRO_0000055724

Regions

Repeat47 – 11973REM 1
Repeat137 – 21478REM 2
Repeat219 – 29678REM 3
Domain373 – 46492C2
Domain658 – 917260Protein kinase
Domain918 – 98568AGC-kinase C-terminal
Nucleotide binding664 – 6729ATP By similarity
Region383 – 46482Necessary to rescue apical junction formation By similarity
Region918 – 97861Necessary for the catalytic activity By similarity
Region979 – 9857Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA By similarity

Sites

Active site7831Proton acceptor By similarity
Binding site6871ATP By similarity
Site1171Cleavage; by caspase-3 By similarity
Site7011Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1101Phosphoserine By similarity
Modified residue1211Phosphothreonine By similarity
Modified residue1241Phosphothreonine By similarity
Modified residue2911Phosphoserine By similarity
Modified residue3031Phosphoserine By similarity
Modified residue3071Phosphoserine By similarity
Modified residue3611Phosphoserine By similarity
Modified residue3631Phosphoserine By similarity
Modified residue3681Phosphoserine By similarity
Modified residue5321Phosphoserine By similarity
Modified residue5361Phosphoserine By similarity
Modified residue5601Phosphoserine By similarity
Modified residue5621Phosphoserine By similarity
Modified residue5831Phosphoserine By similarity
Modified residue5841Phosphoserine By similarity
Modified residue6321Phosphoserine By similarity
Modified residue8151Phosphothreonine By similarity
Modified residue8171Phosphothreonine; by PDPK1 By similarity
Modified residue9591Phosphothreonine Probable

Sequences

Sequence LengthMass (Da)Tools
O08874 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: AE71D30379715C3D

FASTA985112,069
        10         20         30         40         50         60 
MASNPDRGEI LLTELQVDSR PLPFSENVSA VQKLDFSDTI VQQKLDDVKD RIKREIRKEL 

        70         80         90        100        110        120 
KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDYTDCPR 

       130        140        150        160        170        180 
TPDTPNSDSR SSTSNNRRLM ALQKQLDIEL KVKQGAENMI QMYSNGPSKD RKLHGTAQQL 

       190        200        210        220        230        240 
LQDNKTKIEV IRMHILQAVL TNELAFDNAK PVISPLELRN GRIIEHHFRI EFAVAEGAKN 

       250        260        270        280        290        300 
VMKLLGSGKV TDRKALSEAQ ARFNESSQKL DLLKYSLEQR LNELPKNHPK SSVVIEELSL 

       310        320        330        340        350        360 
VASPTLSPRQ SMLSTQNQYS TLSKPAALTG TLEVRLWGAK ISWENVPGRS KATSVALPGW 

       370        380        390        400        410        420 
SPSENRSSFM SRTSKSKSGS SRNLLKTDDL SNDVCAVLKL DNTVVGQTIW KPISNQSWDQ 

       430        440        450        460        470        480 
KFTLELDRSR ELEISVYWRD WRSLCAVKFL RLEDFLDNQR HGMALYLEPQ GTLFAEVTFF 

       490        500        510        520        530        540 
NPVIERRPKL QRQKKIFSKQ QGKTFLRAPQ MNINIATWGR LVRRAIPTVN HSGTFSPQTP 

       550        560        570        580        590        600 
VPATVPVVDA RTPELAPPAS DSTVTKLDFD LEPEAPPAPP RASSLGEIDD SSELRVLDIP 

       610        620        630        640        650        660 
GQGSETVFDI ENDRNNMRPK SKSEYELNIP DSSRSCWSVG ELEDKRSQQR FQFNLQDFRC 

       670        680        690        700        710        720 
CAVLGRGHFG KVLLAEYKHT NEMFAIKALK KGDIVARDEV DSLMCEKRIF ETVNSVRHPF 

       730        740        750        760        770        780 
LVNLFACFQT KEHVCFVMEY AAGGDLMMHI HTDVFSEPRA VFYAACVVLG LQYLHEHKIV 

       790        800        810        820        830        840 
YRDLKLDNLL LDTEASVKIA DFGLCKEGMG YGDRTSTFCG TPEFLAPEVL TETSYTRAVD 

       850        860        870        880        890        900 
WWGLGVLIYE MLVGESPFPG DDEEEVFDSI VNDEVRYPRF LSTEAISIMR RLLRRNPERR 

       910        920        930        940        950        960 
LGAGEKDAED VKKHPFFRLT DWSALLDKKV KPPFVPTIRG REDVSNFDDE FTSEAPILTP 

       970        980 
PREPRILLEE EQEMFRDFDY VADWC

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed: 15057822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Isolation and characterization of a structural homologue of human PRK2 from rat liver: distinguishing substrate and lipid activator specificities."
Yu W., Liu J., Morrice N.A., Wettenhall R.E.H.
J. Biol. Chem. 272:10030-10034(1997) [PubMed: 9092545] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 138-979, PARTIAL PROTEIN SEQUENCE, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Liver and Myeloma.
[3]"The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
Vincent S., Settleman J.
Mol. Cell. Biol. 17:2247-2256(1997) [PubMed: 9121475] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-44 AND 255-266, AUTOPHOSPHORYLATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AABR03012350 Genomic DNA. No translation available.
AABR03012657 Genomic DNA. No translation available.
U75358 mRNA. Translation: AAB53364.1.
IPIIPI00214079.
UniGeneRn.30325.

3D structure databases

ProteinModelPortalO08874.
SMRO08874. Positions 130-207.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4781977.
STRINGO08874.

PTM databases

PhosphoSiteO08874.

Proteomic databases

PRIDEO08874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD620146. Pkn2.

Phylogenomic databases

eggNOGmaNOG08893.
GeneTreeENSGT00560000076750.
HOVERGENHBG108317.
InParanoidO08874.
OrthoDBEOG40ZQWW.

Gene expression databases

ArrayExpressO08874.
GenevestigatorO08874.
GermOnlineENSRNOG00000011317. Rattus norvegicus.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]
Gene3DG3DSA:1.10.287.160. HR1_rho-bd. 3 hits.
PfamPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00742. Hr1. 3 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF46585. PKN_effector. 3 hits.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePKN2_RAT
AccessionPrimary (citable) accession number: O08874
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 9, 2007
Last modified: January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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