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Serine/threonine-protein kinase N1 (EC 2.7.11.13) (Protease-activated kinase 1) (PAK-1) (Protein kinase C-like 1) (Protein kinase C-like PKN) (Protein kinase PKN-alpha) (Protein-kinase C-related kinase 1) (Serine-threonine protein kinase N)

 PKN1_HUMAN              Reviewed;         942 AA.
Q16512; A8K7W5; B2R9R4; B3KVN3; Q15143; Q504U4; Q8IUV5; Q9UD44;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 2.
20-DEC-2017, entry version 204.
RecName: Full=Serine/threonine-protein kinase N1;
EC=2.7.11.13 {ECO:0000269|PubMed:18066052};
AltName: Full=Protease-activated kinase 1;
Short=PAK-1;
AltName: Full=Protein kinase C-like 1;
AltName: Full=Protein kinase C-like PKN;
AltName: Full=Protein kinase PKN-alpha;
AltName: Full=Protein-kinase C-related kinase 1;
AltName: Full=Serine-threonine protein kinase N;
Name=PKN1; Synonyms=PAK1, PKN, PRK1, PRKCL1;
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), AND MUTAGENESIS OF LYS-644.
TISSUE=Hippocampus;
PubMed=8135837; DOI=10.1006/bbrc.1994.1313;
Mukai H., Ono Y.;
"A novel protein kinase with leucine zipper-like sequences: its
catalytic domain is highly homologous to that of protein kinase C.";
Biochem. Biophys. Res. Commun. 199:897-904(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
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 1 AND 2), AND
VARIANTS ILE-555 AND ILE-901.
TISSUE=Kidney, Synovium, and Thymus;
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=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
ILE-901.
TISSUE=Brain, and Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 700-800 (ISOFORMS 1/2), AND VARIANT
VAL-718.
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).
[7]
FUNCTION.
PubMed=8557118; DOI=10.1016/0014-5793(95)01454-3;
Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T.,
Parker P.J.;
"PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156
and serine 163.";
FEBS Lett. 378:281-285(1996).
[8]
FUNCTION.
PubMed=8621664; DOI=10.1074/jbc.271.16.9816;
Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M.,
Miyahara M., Sunakawa H., Ono Y.;
"PKN associates and phosphorylates the head-rod domain of
neurofilament protein.";
J. Biol. Chem. 271:9816-9822(1996).
[9]
ENZYME REGULATION, AND INTERACTION WITH RHOA.
PubMed=8571126; DOI=10.1126/science.271.5249.645;
Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N.,
Mukai H., Ono Y., Kakizuka A., Narumiya S.;
"Protein kinase N (PKN) and PKN-related protein rhophilin as targets
of small GTPase Rho.";
Science 271:645-648(1996).
[10]
FUNCTION.
PubMed=9175763; DOI=10.1006/bbrc.1997.6669;
Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y.,
Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.;
"Domain-specific phosphorylation of vimentin and glial fibrillary
acidic protein by PKN.";
Biochem. Biophys. Res. Commun. 234:621-625(1997).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH RHOB.
PubMed=9478917; DOI=10.1074/jbc.273.9.4811;
Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.;
"PRK1 is targeted to endosomes by the small GTPase, RhoB.";
J. Biol. Chem. 273:4811-4814(1998).
[12]
ENZYME REGULATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ASP-108;
ASP-451; ASP-454; ASP-558 AND ASP-560.
PubMed=9751706; DOI=10.1073/pnas.95.20.11566;
Takahashi M., Mukai H., Toshimori M., Miyamoto M., Ono Y.;
"Proteolytic activation of PKN by caspase-3 or related protease during
apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 95:11566-11571(1998).
[13]
PHOSPHORYLATION AT THR-774 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]
FUNCTION.
PubMed=11104762; DOI=10.1074/jbc.M007427200;
Taniguchi T., Kawamata T., Mukai H., Hasegawa H., Isagawa T.,
Yasuda M., Hashimoto T., Terashima A., Nakai M., Mori H., Ono Y.,
Tanaka C.;
"Phosphorylation of tau is regulated by PKN.";
J. Biol. Chem. 276:10025-10031(2001).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ANDR.
PubMed=12514133; DOI=10.1093/emboj/cdg023;
Metzger E., Muller J.M., Ferrari S., Buettner R., Schule R.;
"A novel inducible transactivation domain in the androgen receptor:
implications for PRK in prostate cancer.";
EMBO J. 22:270-280(2003).
[16]
INTERACTION WITH S.TYPHIMURIUM SSPH1 (MICROBIAL INFECTION).
PubMed=16611232; DOI=10.1111/j.1462-5822.2005.00670.x;
Haraga A., Miller S.I.;
"A Salmonella type III secretion effector interacts with the mammalian
serine/threonine protein kinase PKN1.";
Cell. Microbiol. 8:837-846(2006).
[17]
INTERACTION WITH CCNT2.
PubMed=16331689; DOI=10.1002/jcp.20566;
Cottone G., Baldi A., Palescandolo E., Manente L., Penta R.,
Paggi M.G., De Luca A.;
"Pkn is a novel partner of cyclin T2a in muscle differentiation.";
J. Cell. Physiol. 207:232-237(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-562, 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).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, AND 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-537, 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).
[22]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-644.
PubMed=18066052; DOI=10.1038/ncb1668;
Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
Buettner R., Schule R.;
"Phosphorylation of histone H3 at threonine 11 establishes a novel
chromatin mark for transcriptional regulation.";
Nat. Cell Biol. 10:53-60(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559;
SER-562 AND SER-916, 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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537;
SER-559; SER-562; THR-914 AND SER-916, AND 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).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
FUNCTION, 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).
[28]
INTERACTION WITH PRKCB.
PubMed=20228790; DOI=10.1038/nature08839;
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
at histone H3K4.";
Nature 464:792-796(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537 AND
SER-562, 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).
[30]
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).
[31]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH AKAP13; MAPK14; ZAK AND
MAP2K3.
PubMed=21224381; DOI=10.1074/jbc.M110.185645;
Cariolato L., Cavin S., Diviani D.;
"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
complex involved in alpha1-adrenergic receptor-induced p38
activation.";
J. Biol. Chem. 286:7925-7937(2011).
[32]
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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-533; SER-537;
SER-540; SER-562; SER-608 AND SER-916, 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).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916, 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).
[37]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98 IN COMPLEX WITH RHOA.
PubMed=10619026; DOI=10.1016/S1097-2765(00)80389-5;
Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K.,
Hakoshima T.;
"The structural basis of Rho effector recognition revealed by the
crystal structure of human RhoA complexed with the effector domain of
PKN/PRK1.";
Mol. Cell 4:793-803(1999).
[38]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
PubMed=10388627; DOI=10.1006/jsbi.1999.4114;
Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K.,
Hakoshima T.;
"Biochemical and crystallographic characterization of a Rho effector
domain of the protein serine/threonine kinase N in a complex with
RhoA.";
J. Struct. Biol. 126:166-170(1999).
[39]
STRUCTURE BY NMR OF 116-199 IN COMPLEX WITH RAC1.
PubMed=14514689; DOI=10.1074/jbc.M304313200;
Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y.,
Parker P.J., Blundell T.L., Mott H.R.;
"Molecular dissection of the interaction between the small G proteins
Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1).";
J. Biol. Chem. 278:50578-50587(2003).
[40]
STRUCTURE BY NMR OF 122-199 IN COMPLEX WITH RAC1.
PubMed=18006505; DOI=10.1074/jbc.M706760200;
Modha R., Campbell L.J., Nietlispach D., Buhecha H.R., Owen D.,
Mott H.R.;
"The Rac1 polybasic region is required for interaction with its
effector PRK1.";
J. Biol. Chem. 283:1492-1500(2008).
[41]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 122-199 IN COMPLEX WITH
SALMONELLA SSPH1, UBIQUITINATION (MICROBIAL INFECTION), MUTAGENESIS OF
ARG-181 AND ARG-185, FUNCTION AS ANDROGEN RECEPTOR COACTIVATOR, AND
INTERACTION WITH SALMONELLA SSPH1 (MICROBIAL INFECTION).
PubMed=24248594; DOI=10.1128/MCB.01360-13;
Keszei A.F., Tang X., McCormick C., Zeqiraj E., Rohde J.R., Tyers M.,
Sicheri F.;
"Structure of an SspH1-PKN1 complex reveals the basis for host
substrate recognition and mechanism of activation for a bacterial E3
ubiquitin ligase.";
Mol. Cell. Biol. 34:362-373(2014).
[42]
VARIANTS [LARGE SCALE ANALYSIS] CYS-185; GLU-197; TRP-436; GLN-520;
ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
various processes such as regulation of the intermediate filaments
of the actin cytoskeleton, cell migration, tumor cell invasion and
transcription regulation. Part of a signaling cascade that begins
with the activation of the adrenergic receptor ADRA1B and leads to
the activation of MAPK14. Regulates the cytoskeletal network by
phosphorylating proteins such as VIM and neurofilament proteins
NEFH, NEFL and NEFM, leading to inhibit their polymerization.
Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau,
lowering its ability to bind to microtubules, resulting in
disruption of tubulin assembly. Acts as a key coactivator of
androgen receptor (ANDR)-dependent transcription, by being
recruited to ANDR target genes and specifically mediating
phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific
tag for epigenetic transcriptional activation that promotes
demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C.
Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their
import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-
159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to
phosphorylate RPS6 in vitro. {ECO:0000269|PubMed:11104762,
ECO:0000269|PubMed:12514133, ECO:0000269|PubMed:17332740,
ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:20188095,
ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:21754995,
ECO:0000269|PubMed:24248594, ECO:0000269|PubMed:8557118,
ECO:0000269|PubMed:8621664, ECO:0000269|PubMed:9175763}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:18066052}.
-!- ENZYME REGULATION: Kinase activity is activated upon binding to
Rho proteins (RHOA, RHOB and RAC1). Activated by lipids,
particularly cardiolipin and to a lesser extent by other acidic
phospholipids. Activated by caspase-3 (CASP3) cleavage during
apoptosis. Two specific sites, Thr-774 (activation loop of the
kinase domain) and Ser-916 (turn motif), need to be phosphorylated
for its full activation. {ECO:0000269|PubMed:8571126,
ECO:0000269|PubMed:9751706}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20.6 uM for HDAC5 {ECO:0000269|PubMed:20188095};
-!- SUBUNIT: Interacts with ZFAND6 (By similarity). Interacts with
ANDR (PubMed:12514133). Interacts with PRKCB (PubMed:20228790).
Interacts (via REM 1 and REM 2 repeats) with RAC1
(PubMed:14514689, PubMed:18006505). Interacts (via REM 1 repeat)
with RHOA (PubMed:10619026, PubMed:8571126). Interacts with RHOB
(PubMed:9478917). Interacts (via C-terminus) with PDPK1
(PubMed:10792047). Interacts with CCNT2; enhances MYOD1-dependent
transcription (PubMed:16331689). Component of a signaling complex
containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within
this complex, AKAP13 interacts directly with PKN1, which in turn
recruits MAPK14, MAP2K3 and ZAK (PubMed:21224381).
{ECO:0000250|UniProtKB:P70268, ECO:0000269|PubMed:10619026,
ECO:0000269|PubMed:10792047, ECO:0000269|PubMed:12514133,
ECO:0000269|PubMed:14514689, ECO:0000269|PubMed:16331689,
ECO:0000269|PubMed:18006505, ECO:0000269|PubMed:20228790,
ECO:0000269|PubMed:21224381, ECO:0000269|PubMed:8571126,
ECO:0000269|PubMed:9478917}.
-!- SUBUNIT: (Microbial infection) Interacts (via the second REM
repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via
the leucine-rich repeat region) (PubMed:16611232,
PubMed:24248594). {ECO:0000269|PubMed:16611232,
ECO:0000269|PubMed:24248594}.
-!- INTERACTION:
Q15834:CCDC85B; NbExp=2; IntAct=EBI-602382, EBI-739674;
Q01850:CDR2; NbExp=5; IntAct=EBI-602382, EBI-1181367;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-602382, EBI-10181988;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-602382, EBI-618309;
A6NEM1:GOLGA6L9; NbExp=4; IntAct=EBI-602382, EBI-5916454;
Q9NSC5:HOMER3; NbExp=6; IntAct=EBI-602382, EBI-748420;
P19012:KRT15; NbExp=3; IntAct=EBI-602382, EBI-739566;
Q15323:KRT31; NbExp=5; IntAct=EBI-602382, EBI-948001;
O76014:KRT37; NbExp=4; IntAct=EBI-602382, EBI-1045716;
Q9NYL2-1:MAP3K20; NbExp=2; IntAct=EBI-602382, EBI-687346;
P53778:MAPK12; NbExp=2; IntAct=EBI-602382, EBI-602406;
O15344:MID1; NbExp=3; IntAct=EBI-602382, EBI-2340316;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-602382, EBI-2212028;
Q13077:TRAF1; NbExp=4; IntAct=EBI-602382, EBI-359224;
P08670:VIM; NbExp=3; IntAct=EBI-602382, EBI-353844;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17332740,
ECO:0000269|PubMed:9478917}. Nucleus
{ECO:0000269|PubMed:12514133}. Endosome
{ECO:0000269|PubMed:9478917}. Cell membrane
{ECO:0000250|UniProtKB:Q63433}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q63433}. Cleavage furrow
{ECO:0000269|PubMed:17332740}. Midbody
{ECO:0000269|PubMed:17332740}. Note=Associates with chromatin in a
ligand-dependent manner. Localization to endosomes is mediated via
its interaction with RHOB. Association to the cell membrane is
dependent on Ser-377 phosphorylation. Accumulates during telophase
at the cleavage furrow and finally concentrates around the midbody
in cytokinesis. {ECO:0000250|UniProtKB:Q63433,
ECO:0000269|PubMed:17332740}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16512-1; Sequence=Displayed;
Name=2;
IsoId=Q16512-2; Sequence=VSP_038143;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q16512-3; Sequence=VSP_039213, VSP_039214;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found ubiquitously. Expressed in heart, brain,
placenta, lung, skeletal muscle, kidney and pancreas. Expressed in
numerous tumor cell lines, especially in breast tumor cells.
{ECO:0000269|PubMed:21754995}.
-!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
-!- PTM: Autophosphorylated; preferably on serine. Phosphorylated
during mitosis. {ECO:0000269|PubMed:10792047,
ECO:0000269|PubMed:17332740}.
-!- PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}.
-!- PTM: (Microbial infection) In case of infection, polyubiquitinated
by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its
proteasomal degradation. {ECO:0000269|PubMed:24248594}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D26181; BAA05169.1; -; mRNA.
EMBL; S75546; AAB33345.1; -; mRNA.
EMBL; U33053; AAC50209.1; -; mRNA.
EMBL; AK123007; BAG53845.1; -; mRNA.
EMBL; AK292130; BAF84819.1; -; mRNA.
EMBL; AK313886; BAG36611.1; -; mRNA.
EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040061; AAH40061.1; -; mRNA.
EMBL; BC094766; AAH94766.1; -; mRNA.
CCDS; CCDS42513.1; -. [Q16512-1]
CCDS; CCDS42514.1; -. [Q16512-2]
PIR; JC2129; JC2129.
PIR; S51162; S51162.
RefSeq; NP_002732.3; NM_002741.3. [Q16512-1]
RefSeq; NP_998725.1; NM_213560.1. [Q16512-2]
UniGene; Hs.466044; -.
PDB; 1CXZ; X-ray; 2.20 A; B=13-98.
PDB; 1URF; NMR; -; A=122-199.
PDB; 2RMK; NMR; -; B=122-199.
PDB; 4NKG; X-ray; 2.90 A; B/D=122-199.
PDB; 4OTD; X-ray; 2.00 A; A=605-942.
PDB; 4OTG; X-ray; 2.60 A; A=605-942.
PDB; 4OTH; X-ray; 1.80 A; A=605-942.
PDB; 4OTI; X-ray; 1.93 A; A=605-942.
PDBsum; 1CXZ; -.
PDBsum; 1URF; -.
PDBsum; 2RMK; -.
PDBsum; 4NKG; -.
PDBsum; 4OTD; -.
PDBsum; 4OTG; -.
PDBsum; 4OTH; -.
PDBsum; 4OTI; -.
ProteinModelPortal; Q16512; -.
SMR; Q16512; -.
BioGrid; 111571; 64.
DIP; DIP-34240N; -.
ELM; Q16512; -.
IntAct; Q16512; 70.
MINT; MINT-118694; -.
STRING; 9606.ENSP00000343325; -.
BindingDB; Q16512; -.
ChEMBL; CHEMBL3384; -.
GuidetoPHARMACOLOGY; 1520; -.
iPTMnet; Q16512; -.
PhosphoSitePlus; Q16512; -.
BioMuta; PKN1; -.
DMDM; 259016304; -.
EPD; Q16512; -.
MaxQB; Q16512; -.
PaxDb; Q16512; -.
PeptideAtlas; Q16512; -.
PRIDE; Q16512; -.
DNASU; 5585; -.
Ensembl; ENST00000242783; ENSP00000242783; ENSG00000123143. [Q16512-1]
Ensembl; ENST00000342216; ENSP00000343325; ENSG00000123143. [Q16512-2]
GeneID; 5585; -.
KEGG; hsa:5585; -.
UCSC; uc002myp.4; human. [Q16512-1]
CTD; 5585; -.
DisGeNET; 5585; -.
EuPathDB; HostDB:ENSG00000123143.12; -.
GeneCards; PKN1; -.
H-InvDB; HIX0027472; -.
HGNC; HGNC:9405; PKN1.
HPA; CAB010278; -.
HPA; HPA003982; -.
MIM; 601032; gene.
neXtProt; NX_Q16512; -.
OpenTargets; ENSG00000123143; -.
PharmGKB; PA33769; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOVERGEN; HBG108317; -.
InParanoid; Q16512; -.
KO; K06071; -.
OMA; TMYAIKA; -.
OrthoDB; EOG091G00YT; -.
PhylomeDB; Q16512; -.
TreeFam; TF102005; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
SABIO-RK; Q16512; -.
SignaLink; Q16512; -.
SIGNOR; Q16512; -.
ChiTaRS; PKN1; human.
EvolutionaryTrace; Q16512; -.
GeneWiki; Protein_kinase_N1; -.
GenomeRNAi; 5585; -.
PMAP-CutDB; Q16512; -.
PRO; PR:Q16512; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000123143; -.
CleanEx; HS_PKN1; -.
ExpressionAtlas; Q16512; baseline and differential.
Genevisible; Q16512; HS.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
GO; GO:0035402; F:histone kinase activity (H3-T11 specific); IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0010631; P:epithelial cell migration; IMP:UniProtKB.
GO; GO:0035407; P:histone H3-T11 phosphorylation; IDA:UniProtKB.
GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
GO; GO:0002634; P:regulation of germinal center formation; IEA:Ensembl.
GO; GO:0002637; P:regulation of immunoglobulin production; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0003014; P:renal system process; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd11630; HR1_PKN1_2; 1.
CDD; cd11622; HR1_PKN_1; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
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; IPR037317; PKN1_HR1_2.
InterPro; IPR037313; PKN_HR1_1.
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; SM00742; Hr1; 3.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF46585; SSF46585; 3.
SUPFAM; SSF49562; SSF49562; 2.
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; ATP-binding;
Cell membrane; Chromatin regulator; Complete proteome; Cytoplasm;
Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 942 Serine/threonine-protein kinase N1.
/FTId=PRO_0000055719.
REPEAT 34 110 REM 1.
REPEAT 123 209 REM 2.
REPEAT 210 291 REM 3.
DOMAIN 325 461 C2.
DOMAIN 615 874 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 875 942 AGC-kinase C-terminal.
NP_BIND 621 629 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 181 185 Important for interaction with bacterial
SspH1 and SspH1-mediated
polyubiquitination.
{ECO:0000269|PubMed:24248594}.
ACT_SITE 740 740 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 644 644 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 108 109 Cleavage; by caspase-3.
SITE 454 455 Cleavage; by caspase-3.
SITE 558 559 Cleavage; by caspase-3.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000250|UniProtKB:Q63433}.
MOD_RES 448 448 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 533 533 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 774 774 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:10792047}.
MOD_RES 778 778 Phosphothreonine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 914 914 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 916 916 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 7 MASDAVQ -> MAEANNPSEQELE (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038143.
VAR_SEQ 603 603 S -> R (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039213.
VAR_SEQ 604 942 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039214.
VARIANT 185 185 R -> C (in a metastatic melanoma sample;
somatic mutation; dbSNP:rs267605306).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042337.
VARIANT 197 197 A -> E. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042338.
VARIANT 436 436 R -> W (in dbSNP:rs35132656).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042339.
VARIANT 520 520 R -> Q (in dbSNP:rs56273055).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042340.
VARIANT 555 555 L -> I (in dbSNP:rs34309238).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_042341.
VARIANT 635 635 R -> Q (in dbSNP:rs35416389).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042342.
VARIANT 718 718 I -> V (in dbSNP:rs2230539).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:7988719}.
/FTId=VAR_042343.
VARIANT 873 873 F -> L (in a breast infiltrating ductal
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042344.
VARIANT 901 901 V -> I (in dbSNP:rs10846).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_014937.
VARIANT 921 921 A -> V (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042345.
MUTAGEN 108 108 D->A: Abolishes cleavage by caspase-3 and
formation of AF1 fragment.
{ECO:0000269|PubMed:9751706}.
MUTAGEN 181 181 R->A: Abolishes interaction with
bacterial SspH1.
{ECO:0000269|PubMed:24248594}.
MUTAGEN 181 181 R->K: Decreases interaction with
bacterial SspH1.
{ECO:0000269|PubMed:24248594}.
MUTAGEN 185 185 R->A: Abolishes interaction with
bacterial SspH1.
{ECO:0000269|PubMed:24248594}.
MUTAGEN 451 451 D->A: Abolishes cleavage by caspase-3 and
formation of 70 kDa fragment.
{ECO:0000269|PubMed:9751706}.
MUTAGEN 454 454 D->A: Abolishes cleavage by caspase-3 and
formation of 70 kDa fragment.
{ECO:0000269|PubMed:9751706}.
MUTAGEN 558 558 D->A: Abolishes cleavage by caspase-3 and
formation of AF3 fragment.
{ECO:0000269|PubMed:9751706}.
MUTAGEN 560 560 D->A: Abolishes cleavage by caspase-3 and
formation of AF3 fragment.
{ECO:0000269|PubMed:9751706}.
MUTAGEN 644 644 K->E: Abolishes Serine/threonine-protein
kinase activity.
{ECO:0000269|PubMed:18066052,
ECO:0000269|PubMed:8135837}.
MUTAGEN 644 644 K->R: Substantial reduction of
autophosphorylation.
{ECO:0000269|PubMed:18066052,
ECO:0000269|PubMed:8135837}.
CONFLICT 191 191 G -> D (in Ref. 2; AAB33345/AAC50209).
{ECO:0000305}.
CONFLICT 562 562 S -> P (in Ref. 3; BAG36611).
{ECO:0000305}.
CONFLICT 736 736 I -> T (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
CONFLICT 750 750 T -> A (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
CONFLICT 800 800 G -> A (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
CONFLICT 812 812 E -> G (in Ref. 3; BAG36611).
{ECO:0000305}.
CONFLICT 887 887 L -> P (in Ref. 3; BAG53845).
{ECO:0000305}.
HELIX 15 18 {ECO:0000244|PDB:1CXZ}.
HELIX 29 66 {ECO:0000244|PDB:1CXZ}.
HELIX 71 95 {ECO:0000244|PDB:1CXZ}.
TURN 122 124 {ECO:0000244|PDB:1URF}.
HELIX 126 151 {ECO:0000244|PDB:4NKG}.
TURN 157 159 {ECO:0000244|PDB:4NKG}.
HELIX 160 187 {ECO:0000244|PDB:4NKG}.
STRAND 194 196 {ECO:0000244|PDB:2RMK}.
HELIX 612 614 {ECO:0000244|PDB:4OTH}.
STRAND 615 624 {ECO:0000244|PDB:4OTH}.
STRAND 627 634 {ECO:0000244|PDB:4OTH}.
TURN 635 637 {ECO:0000244|PDB:4OTH}.
STRAND 640 647 {ECO:0000244|PDB:4OTH}.
HELIX 648 653 {ECO:0000244|PDB:4OTH}.
HELIX 657 671 {ECO:0000244|PDB:4OTH}.
TURN 672 674 {ECO:0000244|PDB:4OTG}.
STRAND 681 686 {ECO:0000244|PDB:4OTH}.
STRAND 688 696 {ECO:0000244|PDB:4OTH}.
STRAND 700 702 {ECO:0000244|PDB:4OTH}.
HELIX 703 706 {ECO:0000244|PDB:4OTH}.
TURN 707 709 {ECO:0000244|PDB:4OTH}.
HELIX 714 733 {ECO:0000244|PDB:4OTH}.
HELIX 743 745 {ECO:0000244|PDB:4OTH}.
STRAND 746 748 {ECO:0000244|PDB:4OTH}.
STRAND 750 752 {ECO:0000244|PDB:4OTG}.
STRAND 754 756 {ECO:0000244|PDB:4OTH}.
STRAND 763 765 {ECO:0000244|PDB:4OTD}.
HELIX 779 781 {ECO:0000244|PDB:4OTD}.
HELIX 784 788 {ECO:0000244|PDB:4OTD}.
HELIX 794 810 {ECO:0000244|PDB:4OTH}.
HELIX 820 829 {ECO:0000244|PDB:4OTH}.
HELIX 840 849 {ECO:0000244|PDB:4OTH}.
TURN 854 856 {ECO:0000244|PDB:4OTH}.
TURN 862 864 {ECO:0000244|PDB:4OTH}.
HELIX 865 869 {ECO:0000244|PDB:4OTH}.
HELIX 872 874 {ECO:0000244|PDB:4OTH}.
HELIX 879 883 {ECO:0000244|PDB:4OTH}.
HELIX 906 909 {ECO:0000244|PDB:4OTH}.
HELIX 926 930 {ECO:0000244|PDB:4OTH}.
TURN 931 934 {ECO:0000244|PDB:4OTH}.
SEQUENCE 942 AA; 103932 MW; 61360295EC70BB8E CRC64;
MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR
RATTDLGRSL GPVELLLRGS SRRLDLLHQQ LQELHAHVVL PDPAATHDGP QSPGAGGPTC
SATNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSTKDR KLLLTAQQML QDSKTKIDII
RMQLRRALQA GQLENQAAPD DTQGSPDLGA VELRIEELRH HFRVEHAVAE GAKNVLRLLS
AAKAPDRKAV SEAQEKLTES NQKLGLLREA LERRLGELPA DHPKGRLLRE ELAAASSAAF
STRLAGPFPA THYSTLCKPA PLTGTLEVRV VGCRDLPETI PWNPTPSMGG PGTPDSRPPF
LSRPARGLYS RSGSLSGRSS LKAEAENTSE VSTVLKLDNT VVGQTSWKPC GPNAWDQSFT
LELERARELE LAVFWRDQRG LCALKFLKLE DFLDNERHEV QLDMEPQGCL VAEVTFRNPV
IERIPRLRRQ KKIFSKQQGK AFQRARQMNI DVATWVRLLR RLIPNATGTG TFSPGASPGS
EARTTGDISV EKLNLGTDSD SSPQKSSRDP PSSPSSLSSP IQESTAPELP SETQETPGPA
LCSPLRKSPL TLEDFKFLAV LGRGHFGKVL LSEFRPSGEL FAIKALKKGD IVARDEVESL
MCEKRILAAV TSAGHPFLVN LFGCFQTPEH VCFVMEYSAG GDLMLHIHSD VFSEPRAIFY
SACVVLGLQF LHEHKIVYRD LKLDNLLLDT EGYVKIADFG LCKEGMGYGD RTSTFCGTPE
FLAPEVLTDT SYTRAVDWWG LGVLLYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSA
EAIGIMRRLL RRNPERRLGS SERDAEDVKK QPFFRTLGWE ALLARRLPPP FVPTLSGRTD
VSNFDEEFTG EAPTLSPPRD ARPLTAAEQA AFLDFDFVAG GC


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