Skip Header

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

Q8BWW9 - PKN2_MOUSE

UniProt

Q8BWW9 - PKN2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei117 – 1182Cleavage; by caspase-3By similarity
Binding sitei685 – 6851ATPPROSITE-ProRule annotation
Sitei699 – 7002Cleavage; by caspase-3By similarity
Active sitei781 – 7811Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi662 – 6709ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone deacetylase binding Source: UniProtKB
  3. poly(A) RNA binding Source: MGI
  4. protein kinase C activity Source: UniProtKB-EC
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. apical junction assembly Source: UniProtKB
  2. apoptotic process Source: UniProtKB-KW
  3. cell adhesion Source: UniProtKB-KW
  4. cell cycle Source: UniProtKB-KW
  5. cell division Source: UniProtKB-KW
  6. epithelial cell migration Source: UniProtKB
  7. positive regulation of cytokinesis Source: UniProtKB
  8. positive regulation of mitotic cell cycle Source: UniProtKB
  9. protein phosphorylation Source: UniProtKB
  10. regulation of cell motility Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB-KW
  12. signal transduction Source: InterPro
  13. transcription, DNA-templated Source: UniProtKB-KW
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):
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 › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: 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).By similarity

GO - Cellular componenti

  1. apical junction complex Source: UniProtKB
  2. centrosome Source: MGI
  3. cleavage furrow Source: UniProtKB
  4. cytoplasm Source: MGI
  5. intermediate filament cytoskeleton Source: MGI
  6. lamellipodium Source: UniProtKB
  7. membrane Source: UniProtKB-SubCell
  8. midbody Source: UniProtKB
  9. nucleus Source: MGI
  10. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-155. 1 Publication
Mutagenesisi155 – 1551A → K: Inhibits interaction with RHOA, reduces localization at junctions and prevents apical junction formation; when associated with K-60. 1 Publication
Mutagenesisi685 – 6851K → M: Prevents apical junction formation. 1 Publication
Mutagenesisi781 – 7811D → A: Prevents apical junction formation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 983983Serine/threonine-protein kinase N2PRO_0000055723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771N6-acetyllysine1 Publication
Modified residuei110 – 1101PhosphoserineBy similarity
Modified residuei121 – 1211PhosphothreonineBy similarity
Modified residuei124 – 1241PhosphothreonineBy similarity
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei305 – 3051PhosphoserineBy similarity
Modified residuei359 – 3591PhosphoserineBy similarity
Modified residuei361 – 3611PhosphoserineBy similarity
Modified residuei534 – 5341PhosphoserineBy similarity
Modified residuei582 – 5821PhosphoserineBy similarity
Modified residuei630 – 6301PhosphoserineBy similarity
Modified residuei815 – 8151Phosphothreonine; by PDPK1By similarity
Modified residuei957 – 9571PhosphothreonineCurated

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BWW9.
PaxDbiQ8BWW9.
PRIDEiQ8BWW9.

PTM databases

PhosphoSiteiQ8BWW9.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8BWW9.
CleanExiMM_PKN2.
ExpressionAtlasiQ8BWW9. baseline and differential.
GenevestigatoriQ8BWW9.

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

Structurei

3D structure databases

ProteinModelPortaliQ8BWW9.
SMRiQ8BWW9. Positions 56-107, 136-199, 613-983.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 11976REM 1Add
BLAST
Repeati133 – 21381REM 2Add
BLAST
Repeati214 – 29582REM 3Add
BLAST
Domaini329 – 462134C2Add
BLAST
Domaini656 – 915260Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini916 – 98368AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni381 – 46282Necessary to rescue apical junction formationAdd
BLAST
Regioni916 – 97661Necessary for the catalytic activityBy similarityAdd
BLAST
Regioni977 – 9837Negatively 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

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

eggNOGiCOG0515.
GeneTreeiENSGT00770000120523.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ8BWW9.
KOiK06071.
OMAiHELEDRR.
OrthoDBiEOG7X9G6Q.
TreeFamiTF102005.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
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.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00742. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321Q → H in BAC32655. (PubMed:16141072)Curated
Sequence conflicti84 – 841N → H in BAC33888. (PubMed:16141072)Curated
Sequence conflicti395 – 3951V → D in BAC38910. (PubMed:16141072)Curated
Sequence conflicti569 – 5691L → F in BAC32655. (PubMed:16141072)Curated
Sequence conflicti704 – 7041E → K in BAC33888. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 4511Missing in isoform 2. 1 PublicationVSP_012042Add
BLAST
Alternative sequencei781 – 7877DLKLDNL → NTIFSSI in isoform 3. 1 PublicationVSP_042185
Alternative sequencei788 – 983196Missing in isoform 3. 1 PublicationVSP_042186Add
BLAST

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. Positions 56-107, 136-199, 613-983.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8BWW9.

Proteomic databases

MaxQBiQ8BWW9.
PaxDbiQ8BWW9.
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

eggNOGiCOG0515.
GeneTreeiENSGT00770000120523.
HOGENOMiHOG000233032.
HOVERGENiHBG108317.
InParanoidiQ8BWW9.
KOiK06071.
OMAiHELEDRR.
OrthoDBiEOG7X9G6Q.
TreeFamiTF102005.

Miscellaneous databases

ChiTaRSiPkn2. mouse.
NextBioi361929.
PROiQ8BWW9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BWW9.
CleanExiMM_PKN2.
ExpressionAtlasiQ8BWW9. baseline and differential.
GenevestigatoriQ8BWW9.

Family and domain databases

Gene3Di1.10.287.160. 3 hits.
2.60.40.150. 2 hits.
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.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF02185. HR1. 3 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00742. 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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J and NOD.
    Tissue: Corpora quadrigemina, Spinal cord and Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling."
    Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.
    J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCK1, TISSUE SPECIFICITY.
  4. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase."
    Sun W., Vincent S., Settleman J., Johnson G.L.
    J. Biol. Chem. 275:24421-24428(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K2.
  6. "Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion."
    Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y., Li J., Dotto G.P.
    J. Cell Biol. 156:137-148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
    Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
    J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN PHOSPHORYLATION OF CTTN, ENZYME REGULATION, INTERACTION WITH CD44 AND RAC1, TISSUE SPECIFICITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
    Wallace S.W., Magalhaes A., Hall A.
    Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAC1 AND RHOA, MUTAGENESIS OF ALA-66; ALA-155; LYS-685 AND ASP-781.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Entry informationi

Entry nameiPKN2_MOUSE
AccessioniPrimary (citable) accession number: Q8BWW9
Secondary accession number(s): Q3TBR3
, Q80WS2, Q8BJL7, Q8BL62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 117 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

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 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.