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Q8BWW9

- PKN2_MOUSE

UniProt

Q8BWW9 - PKN2_MOUSE

Protein

Serine/threonine-protein kinase N2

Gene

Pkn2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    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

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:109211. Pkn2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus By similarity. Membrane 1 Publication. 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.By similarity

    GO - Cellular componenti

    1. apical junction complex Source: UniProtKB
    2. cleavage furrow Source: UniProtKB
    3. cytoplasm Source: MGI
    4. cytoskeleton Source: UniProtKB-SubCell
    5. lamellipodium Source: UniProtKB
    6. membrane Source: UniProtKB-SubCell
    7. midbody Source: UniProtKB
    8. nucleus Source: MGI

    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.
    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

    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.
    GeneTreeiENSGT00750000117322.
    HOGENOMiHOG000233032.
    HOVERGENiHBG108317.
    InParanoidiQ3TBR3.
    KOiK06071.
    OMAiRSQQMFQ.
    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_dom.
    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

    MASNPDRGEI LLTELQGDSR TLPFSENVSA VQKLDFSDTM VQQKLDDIKD    50
    RIKREIRKEL KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL 100
    QELNAHIVVS DPEDSTDCPR TPDTPNSDSR SSTSNNRLMA LQKQLDIELK 150
    VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL QDSKTKIEVI RMQILQAVQT 200
    NELAFDNAKP VISPLELRME ELRHHFKIEF AVAEGAKNVM KLLGSGKVTD 250
    RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPRNHPKSS VVIEELSLVA 300
    SPTLSPRQSM LSTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA 350
    TSVALPGWSP SDNRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN 400
    TVVGQTSWKP ISNQSWDQKF TLELDRSREL EISVYWRDWR SLCAVKFLRL 450
    EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP VIERRPKLQR QKKIFSKQQG 500
    KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQTPVP ATVPVVDARI 550
    PDLAPPASDS TVTKLDFDLE PEPPPAPPRA SSLGETDESS ELRVLDIPGQ 600
    GSETVFNIEN DRNNLRPKSK SEYELSIPDS GRSCWGVGEL DDKRAQQRFQ 650
    FSLQDFRCCA VLGRGHFGKV LLAEYKHTNE MFAIKALKKG DIVARDEVDS 700
    LMCEKRIFET VNSVRHPFLV NLFACFQTKE HVCFVMEYAA GGDLMMHIHT 750
    DVFSEPRAVF YAACVVLGLQ YLHEHKIVYR DLKLDNLLLD TEGFVKIADF 800
    GLCKEGMGYG DRTSTFCGTP EFLAPEVLTE TSYTRAVDWW GLGVLIYEML 850
    VGESPFPGDD EEEVFDSIVN DEVRYPRFLS TEAISIMRRL LRRNPERRLG 900
    AGEKDAEDVK KHPFFRLTDW SALMDKKVKP PFVPTIRGRE DVSNFDDEFT 950
    SEAPILTPPR EPRILLEEEQ EMFHDFDYVA DWC 983
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.

    3D structure databases

    ProteinModelPortali Q8BWW9.
    SMRi Q8BWW9. Positions 56-107, 136-199, 613-983.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8BWW9.

    Proteomic databases

    MaxQBi Q8BWW9.
    PaxDbi Q8BWW9.
    PRIDEi Q8BWW9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000043812 ; ENSMUSP00000039566 ; ENSMUSG00000004591 . [Q8BWW9-1 ]
    GeneIDi 109333.
    KEGGi mmu:109333.
    UCSCi uc008rpe.2. mouse. [Q8BWW9-1 ]

    Organism-specific databases

    CTDi 5586.
    MGIi MGI:109211. Pkn2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117322.
    HOGENOMi HOG000233032.
    HOVERGENi HBG108317.
    InParanoidi Q3TBR3.
    KOi K06071.
    OMAi RSQQMFQ.
    OrthoDBi EOG7X9G6Q.
    TreeFami TF102005.

    Miscellaneous databases

    ChiTaRSi PKN2. mouse.
    NextBioi 361929.
    PROi Q8BWW9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BWW9.
    CleanExi MM_PKN2.
    Genevestigatori Q8BWW9.

    Family and domain databases

    Gene3Di 1.10.287.160. 3 hits.
    2.60.40.150. 2 hits.
    InterProi 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.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF02185. HR1. 3 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00742. Hr1. 3 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46585. SSF46585. 3 hits.
    SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 113 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