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Serine/threonine-protein kinase N2 (EC 2.7.11.13) (PKN gamma) (Protein kinase C-like 2) (Protein-kinase C-related kinase 2)

 PKN2_HUMAN              Reviewed;         984 AA.
Q16513; B4DQ21; B4DTP5; B4DVG1; D3DT24; Q08AF4; Q9H1W4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 181.
RecName: Full=Serine/threonine-protein kinase N2;
EC=2.7.11.13;
AltName: Full=PKN gamma;
AltName: Full=Protein kinase C-like 2;
AltName: Full=Protein-kinase C-related kinase 2;
Name=PKN2; Synonyms=PRK2, PRKCL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7988719; DOI=10.1016/0014-5793(94)01202-4;
Palmer R.H., Ridden J., Parker P.J.;
"Identification of multiple, novel, protein kinase C-related gene
products.";
FEBS Lett. 356:5-8(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=B-cell, and Spleen;
PubMed=7851406; DOI=10.1111/j.1432-1033.1995.tb20395.x;
Palmer R.H., Ridden J., Parker P.J.;
"Cloning and expression patterns of two members of a novel protein-
kinase-C-related kinase family.";
Eur. J. Biochem. 227:344-351(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
TISSUE=Placenta, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
ENZYME REGULATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ASP-117
AND ASP-700.
PubMed=9368003; DOI=10.1074/jbc.272.47.29449;
Cryns V.L., Byun Y., Rana A., Mellor H., Lustig K.D., Ghanem L.,
Parker P.J., Kirschner M.W., Yuan J.;
"Specific proteolysis of the kinase protein kinase C-related kinase 2
by caspase-3 during apoptosis. Identification by a novel, small pool
expression cloning strategy.";
J. Biol. Chem. 272:29449-29453(1997).
[8]
FUNCTION, INTERACTION WITH RAC1 AND RHOA, AND AUTOPHOSPHORYLATION.
PubMed=9121475; DOI=10.1128/MCB.17.4.2247;
Vincent S., Settleman J.;
"The PRK2 kinase is a potential effector target of both Rho and Rac
GTPases and regulates actin cytoskeletal organization.";
Mol. Cell. Biol. 17:2247-2256(1997).
[9]
FUNCTION, INTERACTION WITH PDPK1, AND MUTAGENESIS OF PHE-974; PHE-977;
ASP-978 AND TYR-979.
PubMed=10226025; DOI=10.1016/S0960-9822(99)80186-9;
Balendran A., Casamayor A., Deak M., Paterson A., Gaffney P.,
Currie R., Downes C.P., Alessi D.R.;
"PDK1 acquires PDK2 activity in the presence of a synthetic peptide
derived from the carboxyl terminus of PRK2.";
Curr. Biol. 9:393-404(1999).
[10]
INTERACTION WITH NCK1 AND NCK2, AND TISSUE SPECIFICITY.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[11]
INTERACTION WITH MAP3K2.
PubMed=10818102; DOI=10.1074/jbc.M003148200;
Sun W., Vincent S., Settleman J., Johnson G.L.;
"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.";
J. Biol. Chem. 275:24421-24428(2000).
[12]
FUNCTION IN APOPTOSIS, FUNCTION IN AKT1 ACTIVITY INHIBITION, ENZYME
REGULATION, INTERACTION WITH AKT1, AND MUTAGENESIS OF ASP-117 AND
ASP-700.
PubMed=10926925; DOI=10.1074/jbc.M001753200;
Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.;
"Inhibition of Akt and its anti-apoptotic activities by tumor necrosis
factor-induced protein kinase C-related kinase 2 (PRK2) cleavage.";
J. Biol. Chem. 275:34451-34458(2000).
[13]
PHOSPHORYLATION AT THR-816 BY PDPK1, AND INTERACTION WITH PDPK1.
PubMed=10792047; DOI=10.1073/pnas.090491897;
Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.;
"Phosphorylation of protein kinase N by phosphoinositide-dependent
protein kinase-1 mediates insulin signals to the actin cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000).
[14]
INTERACTION WITH PTPN13, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-686 AND CYS-984.
PubMed=11356191; DOI=10.1016/S0014-5793(01)02401-2;
Gross C., Heumann R., Erdmann K.S.;
"The protein kinase C-related kinase PRK2 interacts with the protein
tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif.";
FEBS Lett. 496:101-104(2001).
[15]
FUNCTION IN KINASE ACTIVITY INHIBITION, AND INTERACTION WITH PDPK1.
PubMed=11781095; DOI=10.1021/bi010719z;
Hodgkinson C.P., Sale G.J.;
"Regulation of both PDK1 and the phosphorylation of PKC-zeta and
-delta by a C-terminal PRK2 fragment.";
Biochemistry 41:561-569(2002).
[16]
FUNCTION IN CELL ADHESION, AND INDUCTION.
PubMed=11777936; DOI=10.1083/jcb.200105140;
Calautti E., Grossi M., Mammucari C., Aoyama Y., Pirro M., Ono Y.,
Li J., Dotto G.P.;
"Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in
keratinocyte cell-cell adhesion.";
J. Cell Biol. 156:137-148(2002).
[17]
FUNCTION IN HCV REPLICATION, FUNCTION IN PHOSPHORYLATION OF NS5B, AND
INTERACTION WITH HCV NS5B.
PubMed=15364941; DOI=10.1074/jbc.M408617200;
Kim S.J., Kim J.H., Kim Y.G., Lim H.S., Oh J.W.;
"Protein kinase C-related kinase 2 regulates hepatitis C virus RNA
polymerase function by phosphorylation.";
J. Biol. Chem. 279:50031-50041(2004).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-958, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306 AND
SER-360, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[20]
FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=17332740; DOI=10.1038/sj.emboj.7601637;
Schmidt A., Durgan J., Magalhaes A., Hall A.;
"Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit
from cytokinesis.";
EMBO J. 26:1624-1636(2007).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[22]
ENZYME REGULATION, INTERACTION WITH PDPK1, AND MUTAGENESIS OF THR-816;
THR-958; PHE-977; ASP-978 AND TYR-979.
PubMed=18835241; DOI=10.1016/j.abb.2008.09.008;
Lim W.G., Chen X., Liu J.P., Tan B.J., Zhou S., Smith A., Lees N.,
Hou L., Gu F., Yu X.Y., Du Y., Smith D., Verma C., Liu K., Duan W.;
"The C-terminus of PRK2/PKNgamma is required for optimal activation by
RhoA in a GTP-dependent manner.";
Arch. Biochem. Biophys. 479:170-178(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-958, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-121; THR-124;
SER-302; SER-306; SER-360; SER-362; SER-535; THR-628; SER-631 AND
THR-958, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
FUNCTION IN PHOSPHORYLATION OF HDAC5, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
McKinsey T.A.;
"Protein kinase C-related kinase targets nuclear localization signals
in a subset of class IIa histone deacetylases.";
FEBS Lett. 584:1103-1110(2010).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-306; SER-360;
SER-583 AND THR-958, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
FUNCTION, INTERACTION WITH RAC1; RHOA AND RHOC, AND SUBCELLULAR
LOCATION.
PubMed=20974804; DOI=10.1128/MCB.01001-10;
Wallace S.W., Magalhaes A., Hall A.;
"The Rho target PRK2 regulates apical junction formation in human
bronchial epithelial cells.";
Mol. Cell. Biol. 31:81-91(2011).
[33]
FUNCTION IN CELL MIGRATION, AND TISSUE SPECIFICITY.
PubMed=21754995; DOI=10.1371/journal.pone.0021732;
Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S.,
Collazos A., Parker P.J.;
"Regulatory domain selectivity in the cell-type specific PKN-
dependence of cell migration.";
PLoS ONE 6:E21732-E21732(2011).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-360; SER-583;
THR-628 AND THR-958, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952 AND THR-958, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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 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). Phosphorylates HCV NS5B leading
to stimulation of HCV RNA replication.
{ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10926925,
ECO:0000269|PubMed:11777936, ECO:0000269|PubMed:11781095,
ECO:0000269|PubMed:15364941, ECO:0000269|PubMed:17332740,
ECO:0000269|PubMed:20188095, ECO:0000269|PubMed:20974804,
ECO:0000269|PubMed:21754995, ECO:0000269|PubMed:9121475}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Kinase activity is activated upon binding to
GTP-bound Rhoa/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-816
(activation loop of the kinase domain) and Thr-958 (turn motif),
need to be phosphorylated for its full activation.
{ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:18835241,
ECO:0000269|PubMed:9368003}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15.83 uM for HDAC5 {ECO:0000269|PubMed:20188095};
-!- SUBUNIT: 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 CD44 (By similarity). 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 with
MAP3K2; the interaction activates PRK2 kinase activity in a
MAP3K2-independent 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 HCV NS5B
(via N-terminal finger domain). Interacts with NCK1, NCK2 and
RHOC. {ECO:0000250, ECO:0000269|PubMed:10026169,
ECO:0000269|PubMed:10226025, ECO:0000269|PubMed:10792047,
ECO:0000269|PubMed:10818102, ECO:0000269|PubMed:10926925,
ECO:0000269|PubMed:11356191, ECO:0000269|PubMed:11781095,
ECO:0000269|PubMed:15364941, ECO:0000269|PubMed:18835241,
ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:9121475}.
-!- INTERACTION:
O92972:- (xeno); NbExp=7; IntAct=EBI-2511350, EBI-10006231;
Q15118:PDK1; NbExp=6; IntAct=EBI-2511350, EBI-7016221;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11356191,
ECO:0000269|PubMed:17332740}. Nucleus
{ECO:0000269|PubMed:11356191}. Membrane
{ECO:0000250|UniProtKB:Q8BWW9}. Cell projection, lamellipodium
{ECO:0000269|PubMed:11356191}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11356191}. Cleavage furrow
{ECO:0000269|PubMed:17332740}. Midbody
{ECO:0000269|PubMed:17332740}. Cell junction
{ECO:0000269|PubMed:20974804}. 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. In
the course of viral infection, colocalizes with HCV NS5B at
perinuclear region in the cytoplasm. {ECO:0000269|PubMed:11356191,
ECO:0000269|PubMed:17332740}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q16513-1; Sequence=Displayed;
Name=2;
IsoId=Q16513-2; Sequence=VSP_042183;
Name=3;
IsoId=Q16513-3; Sequence=VSP_042184;
Name=4;
IsoId=Q16513-4; Sequence=VSP_042181;
Name=5;
IsoId=Q16513-5; Sequence=VSP_042180, VSP_042182;
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in numerous tumor cell
lines, especially in bladder tumor cells.
{ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:21754995}.
-!- INDUCTION: Up-regulated during keratinocyte differentiation.
{ECO:0000269|PubMed:11777936}.
-!- DOMAIN: The N-terminal regioninterferes with the interaction
between AKT1 and the C-terminal regionof PKN2.
-!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
-!- DOMAIN: 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.
-!- PTM: Autophosphorylated. Phosphorylated during mitosis.
{ECO:0000269|PubMed:10792047, ECO:0000269|PubMed:17332740}.
-!- PTM: Activated by limited proteolysis with trypsin (By
similarity). Proteolytically cleaved by caspase-3 during the
induction of apoptotic cell death. {ECO:0000250,
ECO:0000269|PubMed:9368003}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U33052; AAC50208.1; -; mRNA.
EMBL; S75548; AAB33346.1; -; mRNA.
EMBL; AK298595; BAG60783.1; -; mRNA.
EMBL; AK300304; BAG62057.1; -; mRNA.
EMBL; AK301066; BAG62673.1; -; mRNA.
EMBL; AL136381; CAI23271.1; -; Genomic_DNA.
EMBL; AC119426; CAI23271.1; JOINED; Genomic_DNA.
EMBL; CH471097; EAW73161.1; -; Genomic_DNA.
EMBL; CH471097; EAW73164.1; -; Genomic_DNA.
EMBL; BC125199; AAI25200.1; -; mRNA.
CCDS; CCDS714.1; -. [Q16513-1]
CCDS; CCDS81350.1; -. [Q16513-3]
PIR; S67527; S67527.
RefSeq; NP_001307636.1; NM_001320707.1. [Q16513-3]
RefSeq; NP_001307637.1; NM_001320708.1. [Q16513-4]
RefSeq; NP_001307638.1; NM_001320709.1. [Q16513-2]
RefSeq; NP_006247.1; NM_006256.3. [Q16513-1]
RefSeq; XP_011540074.1; XM_011541772.2. [Q16513-5]
UniGene; Hs.440833; -.
PDB; 4CRS; X-ray; 2.75 A; A=646-984.
PDB; 4RRV; X-ray; 1.41 A; B=969-983.
PDBsum; 4CRS; -.
PDBsum; 4RRV; -.
ProteinModelPortal; Q16513; -.
SMR; Q16513; -.
BioGrid; 111572; 90.
ELM; Q16513; -.
IntAct; Q16513; 51.
MINT; MINT-198348; -.
STRING; 9606.ENSP00000359552; -.
BindingDB; Q16513; -.
ChEMBL; CHEMBL3032; -.
GuidetoPHARMACOLOGY; 1521; -.
iPTMnet; Q16513; -.
PhosphoSitePlus; Q16513; -.
BioMuta; PKN2; -.
DMDM; 6225859; -.
EPD; Q16513; -.
MaxQB; Q16513; -.
PaxDb; Q16513; -.
PeptideAtlas; Q16513; -.
PRIDE; Q16513; -.
DNASU; 5586; -.
Ensembl; ENST00000370513; ENSP00000359544; ENSG00000065243. [Q16513-3]
Ensembl; ENST00000370521; ENSP00000359552; ENSG00000065243. [Q16513-1]
GeneID; 5586; -.
KEGG; hsa:5586; -.
UCSC; uc001dmn.4; human. [Q16513-1]
CTD; 5586; -.
DisGeNET; 5586; -.
EuPathDB; HostDB:ENSG00000065243.18; -.
GeneCards; PKN2; -.
HGNC; HGNC:9406; PKN2.
HPA; HPA034861; -.
MIM; 602549; gene.
neXtProt; NX_Q16513; -.
OpenTargets; ENSG00000065243; -.
PharmGKB; PA33770; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233032; -.
HOVERGEN; HBG108317; -.
InParanoid; Q16513; -.
KO; K06071; -.
OMA; RSQQMFQ; -.
OrthoDB; EOG091G00YT; -.
PhylomeDB; Q16513; -.
TreeFam; TF102005; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
SABIO-RK; Q16513; -.
SignaLink; Q16513; -.
SIGNOR; Q16513; -.
ChiTaRS; PKN2; human.
GeneWiki; PKN2; -.
GenomeRNAi; 5586; -.
PMAP-CutDB; Q16513; -.
PRO; PR:Q16513; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000065243; -.
CleanEx; HS_PKN2; -.
ExpressionAtlas; Q16513; baseline and differential.
Genevisible; Q16513; HS.
GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; IDA:AgBase.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0070063; F:RNA polymerase binding; IPI:AgBase.
GO; GO:0043297; P:apical junction assembly; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0010631; P:epithelial cell migration; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011072; HR1_rho-bd.
InterPro; IPR036274; HR1_rpt_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF02185; HR1; 3.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00239; C2; 1.
SMART; SM00742; Hr1; 3.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF46585; SSF46585; 3.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Cell adhesion; Cell cycle; Cell division; Cell junction;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase.
CHAIN 1 984 Serine/threonine-protein kinase N2.
/FTId=PRO_0000055722.
REPEAT 44 119 REM 1.
REPEAT 133 213 REM 2.
REPEAT 214 295 REM 3.
DOMAIN 330 463 C2.
DOMAIN 657 916 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 917 984 AGC-kinase C-terminal.
NP_BIND 663 671 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 382 463 Necessary to rescue apical junction
formation. {ECO:0000250}.
REGION 917 977 Necessary for the catalytic activity.
REGION 978 984 Negatively regulates the responsiveness
of the catalytic activity by cardiolipin
and is required for optimal activation by
the GTP-bound RhoA.
ACT_SITE 782 782 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 686 686 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 117 118 Cleavage; by caspase-3.
SITE 700 701 Cleavage; by caspase-3.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 77 77 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BWW9}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 121 121 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 124 124 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BWW9}.
MOD_RES 628 628 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 816 816 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:10792047}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 958 958 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 326 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042180.
VAR_SEQ 1 157 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042181.
VAR_SEQ 327 329 LTG -> MNS (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042182.
VAR_SEQ 375 390 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042183.
VAR_SEQ 428 475 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042184.
VARIANT 94 94 E -> D (in dbSNP:rs12039846).
/FTId=VAR_050562.
VARIANT 197 197 A -> E (in dbSNP:rs35207128).
/FTId=VAR_050563.
VARIANT 655 655 Q -> R (in dbSNP:rs12085658).
/FTId=VAR_050564.
MUTAGEN 117 117 D->A: Prevents proteolytic processing by
caspase-3 during apoptosis. Diminishes
pro-apoptotic function; when associated
with E-700. {ECO:0000269|PubMed:10926925,
ECO:0000269|PubMed:9368003}.
MUTAGEN 686 686 K->R: Does not inhibit interaction with
PTPN13. {ECO:0000269|PubMed:11356191}.
MUTAGEN 700 700 D->E: Prevents proteolytic processing by
caspase-3 during apoptosis. Diminishes
pro-apoptotic function; when associated
with A-117. {ECO:0000269|PubMed:10926925,
ECO:0000269|PubMed:9368003}.
MUTAGEN 816 816 T->A: Reduces catalytic activity.
{ECO:0000269|PubMed:18835241}.
MUTAGEN 958 958 T->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:18835241}.
MUTAGEN 974 974 F->A: Abolishes interaction with PDPK1
and prevents the phosphorylation of AKT1
at 'Ser-473'.
{ECO:0000269|PubMed:10226025}.
MUTAGEN 977 977 F->A,L: Abolishes interaction with PDPK1
and prevents the phosphorylation of AKT1
at 'Ser-473'. Reduces catalytic activity
by 90%. {ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 977 977 F->W,Y: Reduces catalytic activity by
50%. {ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 978 978 D->A,S: Abolishes interaction with PDPK1
and prevents the phosphorylation of AKT1
at 'Ser-473'.
{ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 978 978 D->A: Does not inhibit catalytic
activity. {ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 979 979 Y->A: Abolishes interaction with PDPK1
and prevents the phosphorylation of AKT1
at 'Ser-473'.
{ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 979 979 Y->A: Reduces catalytic activity by 50%.
{ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 979 979 Y->F,L,W: Reduces catalytic activity by
25%. {ECO:0000269|PubMed:10226025,
ECO:0000269|PubMed:18835241}.
MUTAGEN 984 984 C->S: Inhibits interaction with PTPN13.
{ECO:0000269|PubMed:11356191}.
CONFLICT 483 483 I -> V (in Ref. 3; BAG62673).
{ECO:0000305}.
CONFLICT 565 565 K -> R (in Ref. 3; BAG60783).
{ECO:0000305}.
CONFLICT 625 625 K -> R (in Ref. 3; BAG62673).
{ECO:0000305}.
CONFLICT 795 795 F -> L (in Ref. 6; AAI25200).
{ECO:0000305}.
HELIX 647 649 {ECO:0000244|PDB:4CRS}.
STRAND 652 654 {ECO:0000244|PDB:4CRS}.
STRAND 657 665 {ECO:0000244|PDB:4CRS}.
STRAND 670 676 {ECO:0000244|PDB:4CRS}.
STRAND 682 689 {ECO:0000244|PDB:4CRS}.
HELIX 690 695 {ECO:0000244|PDB:4CRS}.
HELIX 699 714 {ECO:0000244|PDB:4CRS}.
STRAND 723 729 {ECO:0000244|PDB:4CRS}.
STRAND 732 738 {ECO:0000244|PDB:4CRS}.
HELIX 745 749 {ECO:0000244|PDB:4CRS}.
HELIX 756 774 {ECO:0000244|PDB:4CRS}.
TURN 775 777 {ECO:0000244|PDB:4CRS}.
HELIX 785 787 {ECO:0000244|PDB:4CRS}.
STRAND 788 790 {ECO:0000244|PDB:4CRS}.
STRAND 796 798 {ECO:0000244|PDB:4CRS}.
STRAND 805 807 {ECO:0000244|PDB:4CRS}.
HELIX 821 823 {ECO:0000244|PDB:4CRS}.
HELIX 826 830 {ECO:0000244|PDB:4CRS}.
HELIX 838 852 {ECO:0000244|PDB:4CRS}.
HELIX 862 871 {ECO:0000244|PDB:4CRS}.
HELIX 882 891 {ECO:0000244|PDB:4CRS}.
HELIX 896 898 {ECO:0000244|PDB:4CRS}.
STRAND 903 905 {ECO:0000244|PDB:4CRS}.
HELIX 907 911 {ECO:0000244|PDB:4CRS}.
HELIX 914 916 {ECO:0000244|PDB:4CRS}.
HELIX 921 925 {ECO:0000244|PDB:4CRS}.
STRAND 944 946 {ECO:0000244|PDB:4CRS}.
HELIX 948 951 {ECO:0000244|PDB:4CRS}.
SEQUENCE 984 AA; 112035 MW; 687EC417A0F51C1D CRC64;
MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL
KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDITDCPR
TPDTPNNDPR CSTSNNRLKA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL
QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM
KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA
ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK ATSVALPGWS
PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD NTVVGQTSWK PISNQSWDQK
FTLELDRSRE LEISVYWRDW RSLCAVKFLR LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN
PVIERRPKLQ RQKKIFSKQQ GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV
PTTVPVVDVR IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG
QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF QFNLQDFRCC
AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD SLMCEKRIFE TVNSVRHPFL
VNLFACFQTK EHVCFVMEYA AGGDLMMHIH TDVFSEPRAV FYAACVVLGL QYLHEHKIVY
RDLKLDNLLL DTEGFVKIAD FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW
WGLGVLIYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL
GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF TSEAPILTPP
REPRILSEEE QEMFRDFDYI ADWC


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EIAAB31335 PAK-2,Pkn2,Prk2,Prkcl2,Protease-activated kinase 2,Protein kinase C-like 2,Protein-kinase C-related kinase 2,Rat,Rattus norvegicus,Serine_threonine-protein kinase N2
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB32397 cAMP-dependent protein kinase catalytic subunit PRKX,Mouse,Mus musculus,Pkare,PKA-related protein kinase,PrKX,Prkx,Protein kinase X,Protein kinase X-linked,Serine_threonine-protein kinase PRKX
EIAAB31338 Homo sapiens,Human,PKN3,PKNBETA,Protein kinase PKN-beta,Protein-kinase C-related kinase 3,Serine_threonine-protein kinase N3
EIAAB31337 Homo sapiens,Human,PKN2,PRK2,PRKCL2,Protein kinase C-like 2,Protein-kinase C-related kinase 2,Serine_threonine-protein kinase N2
EIAAB40326 Pancreatic serine_threonine-protein kinase,Pask,PS_TK,PSTK1,Rat,Rattus norvegicus,Serine_threonine-protein kinase 39,Spak,STE20_SPS1-related proline-alanine-rich protein kinase,Ste-20-related kinase,S
EIAAB31339 Mouse,Mus musculus,Pkn3,Pknbeta,Protein kinase PKN-beta,Protein-kinase C-related kinase 3,Serine_threonine-protein kinase N3
E1358m ELISA kit Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
U1358m CLIA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
E1358h ELISA kit Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T


 

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