Full text data of PKN1
PKN1
(PAK1, PKN, PRK1, PRKCL1)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein kinase N1; 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)
Serine/threonine-protein kinase N1; 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)
UniProt
Q16512
ID PKN1_HUMAN Reviewed; 942 AA.
AC Q16512; A8K7W5; B2R9R4; B3KVN3; Q15143; Q504U4; Q8IUV5; Q9UD44;
read moreDT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase N1;
DE EC=2.7.11.13;
DE AltName: Full=Protease-activated kinase 1;
DE Short=PAK-1;
DE AltName: Full=Protein kinase C-like 1;
DE AltName: Full=Protein kinase C-like PKN;
DE AltName: Full=Protein kinase PKN-alpha;
DE AltName: Full=Protein-kinase C-related kinase 1;
DE AltName: Full=Serine-threonine protein kinase N;
GN Name=PKN1; Synonyms=PAK1, PKN, PRK1, PRKCL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF LYS-644.
RC TISSUE=Hippocampus;
RX PubMed=8135837; DOI=10.1006/bbrc.1994.1313;
RA Mukai H., Ono Y.;
RT "A novel protein kinase with leucine zipper-like sequences: its
RT catalytic domain is highly homologous to that of protein kinase C.";
RL Biochem. Biophys. Res. Commun. 199:897-904(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=7851406; DOI=10.1111/j.1432-1033.1995.tb20395.x;
RA Palmer R.H., Ridden J., Parker P.J.;
RT "Cloning and expression patterns of two members of a novel protein-
RT kinase-C-related kinase family.";
RL Eur. J. Biochem. 227:344-351(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS ILE-555 AND ILE-901.
RC TISSUE=Kidney, Synovium, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ILE-901.
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 700-800 (ISOFORMS 1/2), AND VARIANT
RP VAL-718.
RX PubMed=7988719; DOI=10.1016/0014-5793(94)01202-4;
RA Palmer R.H., Ridden J., Parker P.J.;
RT "Identification of multiple, novel, protein kinase C-related gene
RT products.";
RL FEBS Lett. 356:5-8(1994).
RN [7]
RP FUNCTION, AND INTERACTION WITH MARCKS.
RX PubMed=8557118; DOI=10.1016/0014-5793(95)01454-3;
RA Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T.,
RA Parker P.J.;
RT "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156
RT and serine 163.";
RL FEBS Lett. 378:281-285(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH NEFH; NEFL AND NEFM.
RX PubMed=8621664; DOI=10.1074/jbc.271.16.9816;
RA Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M.,
RA Miyahara M., Sunakawa H., Ono Y.;
RT "PKN associates and phosphorylates the head-rod domain of
RT neurofilament protein.";
RL J. Biol. Chem. 271:9816-9822(1996).
RN [9]
RP ENZYME REGULATION, AND INTERACTION WITH RHOA.
RX PubMed=8571126; DOI=10.1126/science.271.5249.645;
RA Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N.,
RA Mukai H., Ono Y., Kakizuka A., Narumiya S.;
RT "Protein kinase N (PKN) and PKN-related protein rhophilin as targets
RT of small GTPase Rho.";
RL Science 271:645-648(1996).
RN [10]
RP FUNCTION, AND INTERACTION WITH GFAP AND VIM.
RX PubMed=9175763; DOI=10.1006/bbrc.1997.6669;
RA Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y.,
RA Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.;
RT "Domain-specific phosphorylation of vimentin and glial fibrillary
RT acidic protein by PKN.";
RL Biochem. Biophys. Res. Commun. 234:621-625(1997).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RHOB.
RX PubMed=9478917; DOI=10.1074/jbc.273.9.4811;
RA Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.;
RT "PRK1 is targeted to endosomes by the small GTPase, RhoB.";
RL J. Biol. Chem. 273:4811-4814(1998).
RN [12]
RP ENZYME REGULATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ASP-108;
RP ASP-451; ASP-454; ASP-558 AND ASP-560.
RX PubMed=9751706; DOI=10.1073/pnas.95.20.11566;
RA Takahashi M., Mukai H., Toshimori M., Miyamoto M., Ono Y.;
RT "Proteolytic activation of PKN by caspase-3 or related protease during
RT apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11566-11571(1998).
RN [13]
RP PHOSPHORYLATION AT THR-774 BY PDPK1, AND INTERACTION WITH PDPK1.
RX PubMed=10792047; DOI=10.1073/pnas.090491897;
RA Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.;
RT "Phosphorylation of protein kinase N by phosphoinositide-dependent
RT protein kinase-1 mediates insulin signals to the actin cytoskeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000).
RN [14]
RP FUNCTION, AND INTERACTION WITH MAPT.
RX PubMed=11104762; DOI=10.1074/jbc.M007427200;
RA Taniguchi T., Kawamata T., Mukai H., Hasegawa H., Isagawa T.,
RA Yasuda M., Hashimoto T., Terashima A., Nakai M., Mori H., Ono Y.,
RA Tanaka C.;
RT "Phosphorylation of tau is regulated by PKN.";
RL J. Biol. Chem. 276:10025-10031(2001).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ANDR.
RX PubMed=12514133; DOI=10.1093/emboj/cdg023;
RA Metzger E., Muller J.M., Ferrari S., Buettner R., Schule R.;
RT "A novel inducible transactivation domain in the androgen receptor:
RT implications for PRK in prostate cancer.";
RL EMBO J. 22:270-280(2003).
RN [16]
RP INTERACTION WITH S.TYPHIMURIUM SSPH1.
RX PubMed=16611232; DOI=10.1111/j.1462-5822.2005.00670.x;
RA Haraga A., Miller S.I.;
RT "A Salmonella type III secretion effector interacts with the mammalian
RT serine/threonine protein kinase PKN1.";
RL Cell. Microbiol. 8:837-846(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-562, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17332740; DOI=10.1038/sj.emboj.7601637;
RA Schmidt A., Durgan J., Magalhaes A., Hall A.;
RT "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit
RT from cytokinesis.";
RL EMBO J. 26:1624-1636(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-537, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-644.
RX PubMed=18066052; DOI=10.1038/ncb1668;
RA Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
RA Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
RA Buettner R., Schule R.;
RT "Phosphorylation of histone H3 at threonine 11 establishes a novel
RT chromatin mark for transcriptional regulation.";
RL Nat. Cell Biol. 10:53-60(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559;
RP SER-562 AND SER-916, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537;
RP SER-559; SER-562; THR-914 AND SER-916, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION WITH HDAC5;
RP HDAC7 AND HDAC9.
RX PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
RA Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
RA McKinsey T.A.;
RT "Protein kinase C-related kinase targets nuclear localization signals
RT in a subset of class IIa histone deacetylases.";
RL FEBS Lett. 584:1103-1110(2010).
RN [27]
RP INTERACTION WITH PRKCB.
RX PubMed=20228790; DOI=10.1038/nature08839;
RA Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
RT at histone H3K4.";
RL Nature 464:792-796(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537 AND
RP SER-562, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP FUNCTION IN CELL MIGRATION, AND TISSUE SPECIFICITY.
RX PubMed=21754995; DOI=10.1371/journal.pone.0021732;
RA Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S.,
RA Collazos A., Parker P.J.;
RT "Regulatory domain selectivity in the cell-type specific PKN-
RT dependence of cell migration.";
RL PLoS ONE 6:E21732-E21732(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98 IN COMPLEX WITH RHOA.
RX PubMed=10619026; DOI=10.1016/S1097-2765(00)80389-5;
RA Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K.,
RA Hakoshima T.;
RT "The structural basis of Rho effector recognition revealed by the
RT crystal structure of human RhoA complexed with the effector domain of
RT PKN/PRK1.";
RL Mol. Cell 4:793-803(1999).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
RX PubMed=10388627; DOI=10.1006/jsbi.1999.4114;
RA Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K.,
RA Hakoshima T.;
RT "Biochemical and crystallographic characterization of a Rho effector
RT domain of the protein serine/threonine kinase N in a complex with
RT RhoA.";
RL J. Struct. Biol. 126:166-170(1999).
RN [35]
RP STRUCTURE BY NMR OF 116-199 IN COMPLEX WITH RAC1.
RX PubMed=14514689; DOI=10.1074/jbc.M304313200;
RA Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y.,
RA Parker P.J., Blundell T.L., Mott H.R.;
RT "Molecular dissection of the interaction between the small G proteins
RT Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1).";
RL J. Biol. Chem. 278:50578-50587(2003).
RN [36]
RP STRUCTURE BY NMR OF 122-199 IN COMPLEX WITH RAC1.
RX PubMed=18006505; DOI=10.1074/jbc.M706760200;
RA Modha R., Campbell L.J., Nietlispach D., Buhecha H.R., Owen D.,
RA Mott H.R.;
RT "The Rac1 polybasic region is required for interaction with its
RT effector PRK1.";
RL J. Biol. Chem. 283:1492-1500(2008).
RN [37]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-185; GLU-197; TRP-436; GLN-520;
RP ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
CC various processes such as regulation of the intermediate filaments
CC of the actin cytoskeleton, cell migration, tumor cell invasion and
CC transcription regulation. Regulates the cytoskeletal network by
CC phosphorylating proteins such as VIM and neurofilament proteins
CC NEFH, NEFL and NEFM, leading to inhibit their polymerization.
CC Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau,
CC lowering its ability to bind to microtubules, resulting in
CC disruption of tubulin assembly. Acts as a key coactivator of
CC androgen receptor (ANDR)-dependent transcription, by being
CC recruited to ANDR target genes and specifically mediating
CC phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific
CC tag for epigenetic transcriptional activation that promotes
CC demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C.
CC Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their
CC import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-
CC 159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to
CC phosphorylate RPS6 in vitro.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Kinase activity is activated upon binding to
CC Rho proteins (RHOA, RHOB and RAC1). Activated by lipids,
CC particularly cardiolipin and to a lesser extent by other acidic
CC phospholipids. Activated by caspase-3 (CASP3) cleavage during
CC apoptosis. Two specific sites, Thr-774 (activation loop of the
CC kinase domain) and Ser-916 (turn motif), need to be phosphorylated
CC for its full activation.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.6 uM for HDAC5;
CC -!- SUBUNIT: Interacts with ZA20D3 (By similarity). Interacts with
CC ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2
CC repeats) with RAC1. Interacts (via REM 1 repeat) with RHOA.
CC Interacts with RHOB. In case of infection, interacts with
CC S.typhimurium protein sspH1. Interacts (via C-terminus) with
CC PDPK1.
CC -!- INTERACTION:
CC Q15834:CCDC85B; NbExp=2; IntAct=EBI-602382, EBI-739674;
CC P53778:MAPK12; NbExp=2; IntAct=EBI-602382, EBI-602406;
CC Q9NYL2-1:MLTK; NbExp=2; IntAct=EBI-602382, EBI-687346;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endosome. Cell membrane;
CC Peripheral membrane protein. Cleavage furrow. Midbody.
CC Note=Associates with chromatin in a ligand-dependent manner.
CC Localization to endosomes is mediated via its interaction with
CC RHOB. Association to the cell membrane is dependent on Ser-374
CC phosphorylation. Accumulates during telophase at the cleavage
CC furrow and finally concentrates around the midbody in cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16512-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16512-2; Sequence=VSP_038143;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q16512-3; Sequence=VSP_039213, VSP_039214;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Found ubiquitously. Expressed in heart, brain,
CC placenta, lung, skeletal muscle, kidney and pancreas. Expressed in
CC numerous tumor cell lines, especially in breast tumor cells.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC -!- PTM: Autophosphorylated; preferably on serine. Phosphorylated
CC during mitosis.
CC -!- PTM: Activated by limited proteolysis with trypsin (By
CC similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily.
CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 3 REM (Hr1) repeats.
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DR EMBL; D26181; BAA05169.1; -; mRNA.
DR EMBL; S75546; AAB33345.1; -; mRNA.
DR EMBL; U33053; AAC50209.1; -; mRNA.
DR EMBL; AK123007; BAG53845.1; -; mRNA.
DR EMBL; AK292130; BAF84819.1; -; mRNA.
DR EMBL; AK313886; BAG36611.1; -; mRNA.
DR EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040061; AAH40061.1; -; mRNA.
DR EMBL; BC094766; AAH94766.1; -; mRNA.
DR PIR; JC2129; JC2129.
DR PIR; S51162; S51162.
DR RefSeq; NP_002732.3; NM_002741.3.
DR RefSeq; NP_998725.1; NM_213560.1.
DR UniGene; Hs.466044; -.
DR PDB; 1CXZ; X-ray; 2.20 A; B=13-98.
DR PDB; 1URF; NMR; -; A=122-199.
DR PDB; 2RMK; NMR; -; B=122-199.
DR PDBsum; 1CXZ; -.
DR PDBsum; 1URF; -.
DR PDBsum; 2RMK; -.
DR ProteinModelPortal; Q16512; -.
DR SMR; Q16512; 13-98, 122-199, 577-941.
DR DIP; DIP-34240N; -.
DR IntAct; Q16512; 14.
DR MINT; MINT-118694; -.
DR STRING; 9606.ENSP00000343325; -.
DR BindingDB; Q16512; -.
DR ChEMBL; CHEMBL3384; -.
DR GuidetoPHARMACOLOGY; 1520; -.
DR PhosphoSite; Q16512; -.
DR DMDM; 259016304; -.
DR PaxDb; Q16512; -.
DR PRIDE; Q16512; -.
DR DNASU; 5585; -.
DR Ensembl; ENST00000242783; ENSP00000242783; ENSG00000123143.
DR Ensembl; ENST00000342216; ENSP00000343325; ENSG00000123143.
DR GeneID; 5585; -.
DR KEGG; hsa:5585; -.
DR UCSC; uc002myp.3; human.
DR CTD; 5585; -.
DR GeneCards; GC19P014544; -.
DR H-InvDB; HIX0027472; -.
DR HGNC; HGNC:9405; PKN1.
DR HPA; CAB010278; -.
DR HPA; HPA003982; -.
DR MIM; 601032; gene.
DR neXtProt; NX_Q16512; -.
DR PharmGKB; PA33769; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG108317; -.
DR KO; K06071; -.
DR OMA; EFRSSGE; -.
DR OrthoDB; EOG7X9G6Q; -.
DR BRENDA; 2.7.11.13; 2681.
DR SignaLink; Q16512; -.
DR ChiTaRS; PKN1; human.
DR EvolutionaryTrace; Q16512; -.
DR GeneWiki; Protein_kinase_N1; -.
DR GenomeRNAi; 5585; -.
DR NextBio; 21660; -.
DR PMAP-CutDB; Q16512; -.
DR PRO; PR:Q16512; -.
DR ArrayExpress; Q16512; -.
DR Bgee; Q16512; -.
DR CleanEx; HS_PKN1; -.
DR Genevestigator; Q16512; -.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR GO; GO:0035402; F:histone kinase activity (H3-T11 specific); IDA:UniProtKB.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR GO; GO:0010631; P:epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
DR GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.160; -; 3.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; FALSE_NEG.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell membrane; Chromatin regulator; Complete proteome; Cytoplasm;
KW Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 942 Serine/threonine-protein kinase N1.
FT /FTId=PRO_0000055719.
FT REPEAT 34 110 REM 1.
FT REPEAT 123 209 REM 2.
FT REPEAT 210 291 REM 3.
FT DOMAIN 325 461 C2.
FT DOMAIN 615 874 Protein kinase.
FT DOMAIN 875 942 AGC-kinase C-terminal.
FT NP_BIND 621 629 ATP (By similarity).
FT ACT_SITE 740 740 Proton acceptor (By similarity).
FT BINDING 644 644 ATP (By similarity).
FT SITE 108 109 Cleavage; by caspase-3.
FT SITE 454 455 Cleavage; by caspase-3.
FT SITE 558 559 Cleavage; by caspase-3.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 205 205 Phosphoserine.
FT MOD_RES 374 374 Phosphoserine (By similarity).
FT MOD_RES 448 448 N6-acetyllysine.
FT MOD_RES 533 533 Phosphoserine.
FT MOD_RES 537 537 Phosphoserine.
FT MOD_RES 559 559 Phosphoserine.
FT MOD_RES 562 562 Phosphoserine.
FT MOD_RES 774 774 Phosphothreonine; by PDPK1.
FT MOD_RES 778 778 Phosphothreonine.
FT MOD_RES 914 914 Phosphothreonine.
FT MOD_RES 916 916 Phosphoserine.
FT VAR_SEQ 1 7 MASDAVQ -> MAEANNPSEQELE (in isoform 2).
FT /FTId=VSP_038143.
FT VAR_SEQ 603 603 S -> R (in isoform 3).
FT /FTId=VSP_039213.
FT VAR_SEQ 604 942 Missing (in isoform 3).
FT /FTId=VSP_039214.
FT VARIANT 185 185 R -> C (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_042337.
FT VARIANT 197 197 A -> E.
FT /FTId=VAR_042338.
FT VARIANT 436 436 R -> W (in dbSNP:rs35132656).
FT /FTId=VAR_042339.
FT VARIANT 520 520 R -> Q (in dbSNP:rs56273055).
FT /FTId=VAR_042340.
FT VARIANT 555 555 L -> I (in dbSNP:rs34309238).
FT /FTId=VAR_042341.
FT VARIANT 635 635 R -> Q (in dbSNP:rs35416389).
FT /FTId=VAR_042342.
FT VARIANT 718 718 I -> V (in dbSNP:rs2230539).
FT /FTId=VAR_042343.
FT VARIANT 873 873 F -> L (in a breast infiltrating ductal
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_042344.
FT VARIANT 901 901 V -> I (in dbSNP:rs10846).
FT /FTId=VAR_014937.
FT VARIANT 921 921 A -> V (in a colorectal adenocarcinoma
FT sample; somatic mutation).
FT /FTId=VAR_042345.
FT MUTAGEN 108 108 D->A: Abolishes cleavage by caspase-3 and
FT formation of AF1 fragment.
FT MUTAGEN 451 451 D->A: Abolishes cleavage by caspase-3 and
FT formation of 70 kDa fragment.
FT MUTAGEN 454 454 D->A: Abolishes cleavage by caspase-3 and
FT formation of 70 kDa fragment.
FT MUTAGEN 558 558 D->A: Abolishes cleavage by caspase-3 and
FT formation of AF3 fragment.
FT MUTAGEN 560 560 D->A: Abolishes cleavage by caspase-3 and
FT formation of AF3 fragment.
FT MUTAGEN 644 644 K->E: Abolishes Serine/threonine-protein
FT kinase activity.
FT MUTAGEN 644 644 K->R: Substantial reduction of
FT autophosphorylation.
FT CONFLICT 191 191 G -> D (in Ref. 2; AAB33345/AAC50209).
FT CONFLICT 562 562 S -> P (in Ref. 3; BAG36611).
FT CONFLICT 736 736 I -> T (in Ref. 6; no nucleotide entry).
FT CONFLICT 750 750 T -> A (in Ref. 6; no nucleotide entry).
FT CONFLICT 800 800 G -> A (in Ref. 6; no nucleotide entry).
FT CONFLICT 812 812 E -> G (in Ref. 3; BAG36611).
FT CONFLICT 887 887 L -> P (in Ref. 3; BAG53845).
FT HELIX 15 18
FT HELIX 29 66
FT HELIX 71 95
FT TURN 122 124
FT HELIX 126 154
FT STRAND 155 157
FT HELIX 160 192
FT STRAND 194 196
SQ 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
//
ID PKN1_HUMAN Reviewed; 942 AA.
AC Q16512; A8K7W5; B2R9R4; B3KVN3; Q15143; Q504U4; Q8IUV5; Q9UD44;
read moreDT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase N1;
DE EC=2.7.11.13;
DE AltName: Full=Protease-activated kinase 1;
DE Short=PAK-1;
DE AltName: Full=Protein kinase C-like 1;
DE AltName: Full=Protein kinase C-like PKN;
DE AltName: Full=Protein kinase PKN-alpha;
DE AltName: Full=Protein-kinase C-related kinase 1;
DE AltName: Full=Serine-threonine protein kinase N;
GN Name=PKN1; Synonyms=PAK1, PKN, PRK1, PRKCL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF LYS-644.
RC TISSUE=Hippocampus;
RX PubMed=8135837; DOI=10.1006/bbrc.1994.1313;
RA Mukai H., Ono Y.;
RT "A novel protein kinase with leucine zipper-like sequences: its
RT catalytic domain is highly homologous to that of protein kinase C.";
RL Biochem. Biophys. Res. Commun. 199:897-904(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=7851406; DOI=10.1111/j.1432-1033.1995.tb20395.x;
RA Palmer R.H., Ridden J., Parker P.J.;
RT "Cloning and expression patterns of two members of a novel protein-
RT kinase-C-related kinase family.";
RL Eur. J. Biochem. 227:344-351(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS ILE-555 AND ILE-901.
RC TISSUE=Kidney, Synovium, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ILE-901.
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 700-800 (ISOFORMS 1/2), AND VARIANT
RP VAL-718.
RX PubMed=7988719; DOI=10.1016/0014-5793(94)01202-4;
RA Palmer R.H., Ridden J., Parker P.J.;
RT "Identification of multiple, novel, protein kinase C-related gene
RT products.";
RL FEBS Lett. 356:5-8(1994).
RN [7]
RP FUNCTION, AND INTERACTION WITH MARCKS.
RX PubMed=8557118; DOI=10.1016/0014-5793(95)01454-3;
RA Palmer R.H., Schonwasser D.C., Rahman D., Pappin D.J., Herget T.,
RA Parker P.J.;
RT "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156
RT and serine 163.";
RL FEBS Lett. 378:281-285(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH NEFH; NEFL AND NEFM.
RX PubMed=8621664; DOI=10.1074/jbc.271.16.9816;
RA Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M.,
RA Miyahara M., Sunakawa H., Ono Y.;
RT "PKN associates and phosphorylates the head-rod domain of
RT neurofilament protein.";
RL J. Biol. Chem. 271:9816-9822(1996).
RN [9]
RP ENZYME REGULATION, AND INTERACTION WITH RHOA.
RX PubMed=8571126; DOI=10.1126/science.271.5249.645;
RA Watanabe G., Saito Y., Madaule P., Ishizaki T., Fujisawa K., Morii N.,
RA Mukai H., Ono Y., Kakizuka A., Narumiya S.;
RT "Protein kinase N (PKN) and PKN-related protein rhophilin as targets
RT of small GTPase Rho.";
RL Science 271:645-648(1996).
RN [10]
RP FUNCTION, AND INTERACTION WITH GFAP AND VIM.
RX PubMed=9175763; DOI=10.1006/bbrc.1997.6669;
RA Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y.,
RA Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.;
RT "Domain-specific phosphorylation of vimentin and glial fibrillary
RT acidic protein by PKN.";
RL Biochem. Biophys. Res. Commun. 234:621-625(1997).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RHOB.
RX PubMed=9478917; DOI=10.1074/jbc.273.9.4811;
RA Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.;
RT "PRK1 is targeted to endosomes by the small GTPase, RhoB.";
RL J. Biol. Chem. 273:4811-4814(1998).
RN [12]
RP ENZYME REGULATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ASP-108;
RP ASP-451; ASP-454; ASP-558 AND ASP-560.
RX PubMed=9751706; DOI=10.1073/pnas.95.20.11566;
RA Takahashi M., Mukai H., Toshimori M., Miyamoto M., Ono Y.;
RT "Proteolytic activation of PKN by caspase-3 or related protease during
RT apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11566-11571(1998).
RN [13]
RP PHOSPHORYLATION AT THR-774 BY PDPK1, AND INTERACTION WITH PDPK1.
RX PubMed=10792047; DOI=10.1073/pnas.090491897;
RA Dong L.Q., Landa L.R., Wick M.J., Zhu L., Mukai H., Ono Y., Liu F.;
RT "Phosphorylation of protein kinase N by phosphoinositide-dependent
RT protein kinase-1 mediates insulin signals to the actin cytoskeleton.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5089-5094(2000).
RN [14]
RP FUNCTION, AND INTERACTION WITH MAPT.
RX PubMed=11104762; DOI=10.1074/jbc.M007427200;
RA Taniguchi T., Kawamata T., Mukai H., Hasegawa H., Isagawa T.,
RA Yasuda M., Hashimoto T., Terashima A., Nakai M., Mori H., Ono Y.,
RA Tanaka C.;
RT "Phosphorylation of tau is regulated by PKN.";
RL J. Biol. Chem. 276:10025-10031(2001).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ANDR.
RX PubMed=12514133; DOI=10.1093/emboj/cdg023;
RA Metzger E., Muller J.M., Ferrari S., Buettner R., Schule R.;
RT "A novel inducible transactivation domain in the androgen receptor:
RT implications for PRK in prostate cancer.";
RL EMBO J. 22:270-280(2003).
RN [16]
RP INTERACTION WITH S.TYPHIMURIUM SSPH1.
RX PubMed=16611232; DOI=10.1111/j.1462-5822.2005.00670.x;
RA Haraga A., Miller S.I.;
RT "A Salmonella type III secretion effector interacts with the mammalian
RT serine/threonine protein kinase PKN1.";
RL Cell. Microbiol. 8:837-846(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-562, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=17332740; DOI=10.1038/sj.emboj.7601637;
RA Schmidt A., Durgan J., Magalhaes A., Hall A.;
RT "Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit
RT from cytokinesis.";
RL EMBO J. 26:1624-1636(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-537, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-644.
RX PubMed=18066052; DOI=10.1038/ncb1668;
RA Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
RA Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
RA Buettner R., Schule R.;
RT "Phosphorylation of histone H3 at threonine 11 establishes a novel
RT chromatin mark for transcriptional regulation.";
RL Nat. Cell Biol. 10:53-60(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537; SER-559;
RP SER-562 AND SER-916, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-533; SER-537;
RP SER-559; SER-562; THR-914 AND SER-916, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-448, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION WITH HDAC5;
RP HDAC7 AND HDAC9.
RX PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
RA Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
RA McKinsey T.A.;
RT "Protein kinase C-related kinase targets nuclear localization signals
RT in a subset of class IIa histone deacetylases.";
RL FEBS Lett. 584:1103-1110(2010).
RN [27]
RP INTERACTION WITH PRKCB.
RX PubMed=20228790; DOI=10.1038/nature08839;
RA Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
RT at histone H3K4.";
RL Nature 464:792-796(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-537 AND
RP SER-562, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP FUNCTION IN CELL MIGRATION, AND TISSUE SPECIFICITY.
RX PubMed=21754995; DOI=10.1371/journal.pone.0021732;
RA Lachmann S., Jevons A., De Rycker M., Casamassima A., Radtke S.,
RA Collazos A., Parker P.J.;
RT "Regulatory domain selectivity in the cell-type specific PKN-
RT dependence of cell migration.";
RL PLoS ONE 6:E21732-E21732(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98 IN COMPLEX WITH RHOA.
RX PubMed=10619026; DOI=10.1016/S1097-2765(00)80389-5;
RA Maesaki R., Ihara K., Shimizu T., Kuroda S., Kaibuchi K.,
RA Hakoshima T.;
RT "The structural basis of Rho effector recognition revealed by the
RT crystal structure of human RhoA complexed with the effector domain of
RT PKN/PRK1.";
RL Mol. Cell 4:793-803(1999).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-98.
RX PubMed=10388627; DOI=10.1006/jsbi.1999.4114;
RA Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K.,
RA Hakoshima T.;
RT "Biochemical and crystallographic characterization of a Rho effector
RT domain of the protein serine/threonine kinase N in a complex with
RT RhoA.";
RL J. Struct. Biol. 126:166-170(1999).
RN [35]
RP STRUCTURE BY NMR OF 116-199 IN COMPLEX WITH RAC1.
RX PubMed=14514689; DOI=10.1074/jbc.M304313200;
RA Owen D., Lowe P.N., Nietlispach D., Brosnan C.E., Chirgadze D.Y.,
RA Parker P.J., Blundell T.L., Mott H.R.;
RT "Molecular dissection of the interaction between the small G proteins
RT Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1).";
RL J. Biol. Chem. 278:50578-50587(2003).
RN [36]
RP STRUCTURE BY NMR OF 122-199 IN COMPLEX WITH RAC1.
RX PubMed=18006505; DOI=10.1074/jbc.M706760200;
RA Modha R., Campbell L.J., Nietlispach D., Buhecha H.R., Owen D.,
RA Mott H.R.;
RT "The Rac1 polybasic region is required for interaction with its
RT effector PRK1.";
RL J. Biol. Chem. 283:1492-1500(2008).
RN [37]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-185; GLU-197; TRP-436; GLN-520;
RP ILE-555; GLN-635; VAL-718; LEU-873; ILE-901 AND VAL-921.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
CC various processes such as regulation of the intermediate filaments
CC of the actin cytoskeleton, cell migration, tumor cell invasion and
CC transcription regulation. Regulates the cytoskeletal network by
CC phosphorylating proteins such as VIM and neurofilament proteins
CC NEFH, NEFL and NEFM, leading to inhibit their polymerization.
CC Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau,
CC lowering its ability to bind to microtubules, resulting in
CC disruption of tubulin assembly. Acts as a key coactivator of
CC androgen receptor (ANDR)-dependent transcription, by being
CC recruited to ANDR target genes and specifically mediating
CC phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific
CC tag for epigenetic transcriptional activation that promotes
CC demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C.
CC Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their
CC import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-
CC 159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to
CC phosphorylate RPS6 in vitro.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Kinase activity is activated upon binding to
CC Rho proteins (RHOA, RHOB and RAC1). Activated by lipids,
CC particularly cardiolipin and to a lesser extent by other acidic
CC phospholipids. Activated by caspase-3 (CASP3) cleavage during
CC apoptosis. Two specific sites, Thr-774 (activation loop of the
CC kinase domain) and Ser-916 (turn motif), need to be phosphorylated
CC for its full activation.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.6 uM for HDAC5;
CC -!- SUBUNIT: Interacts with ZA20D3 (By similarity). Interacts with
CC ANDR. Interacts with PRKCB. Interacts (via REM 1 and REM 2
CC repeats) with RAC1. Interacts (via REM 1 repeat) with RHOA.
CC Interacts with RHOB. In case of infection, interacts with
CC S.typhimurium protein sspH1. Interacts (via C-terminus) with
CC PDPK1.
CC -!- INTERACTION:
CC Q15834:CCDC85B; NbExp=2; IntAct=EBI-602382, EBI-739674;
CC P53778:MAPK12; NbExp=2; IntAct=EBI-602382, EBI-602406;
CC Q9NYL2-1:MLTK; NbExp=2; IntAct=EBI-602382, EBI-687346;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endosome. Cell membrane;
CC Peripheral membrane protein. Cleavage furrow. Midbody.
CC Note=Associates with chromatin in a ligand-dependent manner.
CC Localization to endosomes is mediated via its interaction with
CC RHOB. Association to the cell membrane is dependent on Ser-374
CC phosphorylation. Accumulates during telophase at the cleavage
CC furrow and finally concentrates around the midbody in cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16512-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16512-2; Sequence=VSP_038143;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q16512-3; Sequence=VSP_039213, VSP_039214;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Found ubiquitously. Expressed in heart, brain,
CC placenta, lung, skeletal muscle, kidney and pancreas. Expressed in
CC numerous tumor cell lines, especially in breast tumor cells.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC -!- PTM: Autophosphorylated; preferably on serine. Phosphorylated
CC during mitosis.
CC -!- PTM: Activated by limited proteolysis with trypsin (By
CC similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily.
CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 3 REM (Hr1) repeats.
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DR EMBL; D26181; BAA05169.1; -; mRNA.
DR EMBL; S75546; AAB33345.1; -; mRNA.
DR EMBL; U33053; AAC50209.1; -; mRNA.
DR EMBL; AK123007; BAG53845.1; -; mRNA.
DR EMBL; AK292130; BAF84819.1; -; mRNA.
DR EMBL; AK313886; BAG36611.1; -; mRNA.
DR EMBL; AC008569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040061; AAH40061.1; -; mRNA.
DR EMBL; BC094766; AAH94766.1; -; mRNA.
DR PIR; JC2129; JC2129.
DR PIR; S51162; S51162.
DR RefSeq; NP_002732.3; NM_002741.3.
DR RefSeq; NP_998725.1; NM_213560.1.
DR UniGene; Hs.466044; -.
DR PDB; 1CXZ; X-ray; 2.20 A; B=13-98.
DR PDB; 1URF; NMR; -; A=122-199.
DR PDB; 2RMK; NMR; -; B=122-199.
DR PDBsum; 1CXZ; -.
DR PDBsum; 1URF; -.
DR PDBsum; 2RMK; -.
DR ProteinModelPortal; Q16512; -.
DR SMR; Q16512; 13-98, 122-199, 577-941.
DR DIP; DIP-34240N; -.
DR IntAct; Q16512; 14.
DR MINT; MINT-118694; -.
DR STRING; 9606.ENSP00000343325; -.
DR BindingDB; Q16512; -.
DR ChEMBL; CHEMBL3384; -.
DR GuidetoPHARMACOLOGY; 1520; -.
DR PhosphoSite; Q16512; -.
DR DMDM; 259016304; -.
DR PaxDb; Q16512; -.
DR PRIDE; Q16512; -.
DR DNASU; 5585; -.
DR Ensembl; ENST00000242783; ENSP00000242783; ENSG00000123143.
DR Ensembl; ENST00000342216; ENSP00000343325; ENSG00000123143.
DR GeneID; 5585; -.
DR KEGG; hsa:5585; -.
DR UCSC; uc002myp.3; human.
DR CTD; 5585; -.
DR GeneCards; GC19P014544; -.
DR H-InvDB; HIX0027472; -.
DR HGNC; HGNC:9405; PKN1.
DR HPA; CAB010278; -.
DR HPA; HPA003982; -.
DR MIM; 601032; gene.
DR neXtProt; NX_Q16512; -.
DR PharmGKB; PA33769; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG108317; -.
DR KO; K06071; -.
DR OMA; EFRSSGE; -.
DR OrthoDB; EOG7X9G6Q; -.
DR BRENDA; 2.7.11.13; 2681.
DR SignaLink; Q16512; -.
DR ChiTaRS; PKN1; human.
DR EvolutionaryTrace; Q16512; -.
DR GeneWiki; Protein_kinase_N1; -.
DR GenomeRNAi; 5585; -.
DR NextBio; 21660; -.
DR PMAP-CutDB; Q16512; -.
DR PRO; PR:Q16512; -.
DR ArrayExpress; Q16512; -.
DR Bgee; Q16512; -.
DR CleanEx; HS_PKN1; -.
DR Genevestigator; Q16512; -.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR GO; GO:0035402; F:histone kinase activity (H3-T11 specific); IDA:UniProtKB.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR GO; GO:0010631; P:epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
DR GO; GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.160; -; 3.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; FALSE_NEG.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell membrane; Chromatin regulator; Complete proteome; Cytoplasm;
KW Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 942 Serine/threonine-protein kinase N1.
FT /FTId=PRO_0000055719.
FT REPEAT 34 110 REM 1.
FT REPEAT 123 209 REM 2.
FT REPEAT 210 291 REM 3.
FT DOMAIN 325 461 C2.
FT DOMAIN 615 874 Protein kinase.
FT DOMAIN 875 942 AGC-kinase C-terminal.
FT NP_BIND 621 629 ATP (By similarity).
FT ACT_SITE 740 740 Proton acceptor (By similarity).
FT BINDING 644 644 ATP (By similarity).
FT SITE 108 109 Cleavage; by caspase-3.
FT SITE 454 455 Cleavage; by caspase-3.
FT SITE 558 559 Cleavage; by caspase-3.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 205 205 Phosphoserine.
FT MOD_RES 374 374 Phosphoserine (By similarity).
FT MOD_RES 448 448 N6-acetyllysine.
FT MOD_RES 533 533 Phosphoserine.
FT MOD_RES 537 537 Phosphoserine.
FT MOD_RES 559 559 Phosphoserine.
FT MOD_RES 562 562 Phosphoserine.
FT MOD_RES 774 774 Phosphothreonine; by PDPK1.
FT MOD_RES 778 778 Phosphothreonine.
FT MOD_RES 914 914 Phosphothreonine.
FT MOD_RES 916 916 Phosphoserine.
FT VAR_SEQ 1 7 MASDAVQ -> MAEANNPSEQELE (in isoform 2).
FT /FTId=VSP_038143.
FT VAR_SEQ 603 603 S -> R (in isoform 3).
FT /FTId=VSP_039213.
FT VAR_SEQ 604 942 Missing (in isoform 3).
FT /FTId=VSP_039214.
FT VARIANT 185 185 R -> C (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_042337.
FT VARIANT 197 197 A -> E.
FT /FTId=VAR_042338.
FT VARIANT 436 436 R -> W (in dbSNP:rs35132656).
FT /FTId=VAR_042339.
FT VARIANT 520 520 R -> Q (in dbSNP:rs56273055).
FT /FTId=VAR_042340.
FT VARIANT 555 555 L -> I (in dbSNP:rs34309238).
FT /FTId=VAR_042341.
FT VARIANT 635 635 R -> Q (in dbSNP:rs35416389).
FT /FTId=VAR_042342.
FT VARIANT 718 718 I -> V (in dbSNP:rs2230539).
FT /FTId=VAR_042343.
FT VARIANT 873 873 F -> L (in a breast infiltrating ductal
FT carcinoma sample; somatic mutation).
FT /FTId=VAR_042344.
FT VARIANT 901 901 V -> I (in dbSNP:rs10846).
FT /FTId=VAR_014937.
FT VARIANT 921 921 A -> V (in a colorectal adenocarcinoma
FT sample; somatic mutation).
FT /FTId=VAR_042345.
FT MUTAGEN 108 108 D->A: Abolishes cleavage by caspase-3 and
FT formation of AF1 fragment.
FT MUTAGEN 451 451 D->A: Abolishes cleavage by caspase-3 and
FT formation of 70 kDa fragment.
FT MUTAGEN 454 454 D->A: Abolishes cleavage by caspase-3 and
FT formation of 70 kDa fragment.
FT MUTAGEN 558 558 D->A: Abolishes cleavage by caspase-3 and
FT formation of AF3 fragment.
FT MUTAGEN 560 560 D->A: Abolishes cleavage by caspase-3 and
FT formation of AF3 fragment.
FT MUTAGEN 644 644 K->E: Abolishes Serine/threonine-protein
FT kinase activity.
FT MUTAGEN 644 644 K->R: Substantial reduction of
FT autophosphorylation.
FT CONFLICT 191 191 G -> D (in Ref. 2; AAB33345/AAC50209).
FT CONFLICT 562 562 S -> P (in Ref. 3; BAG36611).
FT CONFLICT 736 736 I -> T (in Ref. 6; no nucleotide entry).
FT CONFLICT 750 750 T -> A (in Ref. 6; no nucleotide entry).
FT CONFLICT 800 800 G -> A (in Ref. 6; no nucleotide entry).
FT CONFLICT 812 812 E -> G (in Ref. 3; BAG36611).
FT CONFLICT 887 887 L -> P (in Ref. 3; BAG53845).
FT HELIX 15 18
FT HELIX 29 66
FT HELIX 71 95
FT TURN 122 124
FT HELIX 126 154
FT STRAND 155 157
FT HELIX 160 192
FT STRAND 194 196
SQ 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
//
MIM
601032
*RECORD*
*FIELD* NO
601032
*FIELD* TI
*601032 PROTEIN KINASE N1; PKN1
;;PROTEIN KINASE C-RELATED KINASE 1; PRK1;;
SERINE/THREONINE PROTEIN KINASE N; PKN;;
read morePKN-ALPHA;;
PROTEIN KINASE C-LIKE 1; PRKCL1;;
PAK1, RAT, HOMOLOG OF
*FIELD* TX
CLONING
Mukai and Ono (1994) isolated a cDNA for the protein kinase PRK1, which
they designated PKN, from a human hippocampus cDNA library. The putative
942-amino acid protein has leucine zipper-like sequences at its N
terminus and contains a domain with strong similarity to that of the
protein kinase C (PKC) family. Ubiquitous expression in human tissues
was shown. Antisera detected a 120-kD recombinantly expressed protein on
Western blots. The protein showed intrinsic protein kinase activity that
was abolished by a mutation in the predicted ATP binding site.
Palmer et al. (1994) used degenerate PCR to isolate 3 novel members of
the closely related PKC family, termed PRK1, PRK2 (602549), and PRK3
(610714). Palmer et al. (1995) cloned a full-length cDNA of PRK1 from a
human fetal brain library. Using Northern blot and RT-PCR analyses,
Palmer et al. (1995) detected expression of PRK1 in all tissues and cell
lines tested.
GENE FUNCTION
In a study of proteins that bind to the rho GTPase (see Ridley and Hall,
1992), Amano et al. (1996) discovered a protein that had partial amino
acid sequences identical to PKN. They found that rho binds directly to a
polybasic region of the N-terminal regulatory domain that precedes the
leucine zipper-like motif. The authors speculated that through this
activity, PKN may mediate the rho-dependent signaling pathway.
Metzger et al. (2003) found that androgen receptor (AR; 313700) and PRK1
interact in vitro and in vivo. Stimulation of the PRK1 signaling cascade
resulted in ligand-dependent superactivation of AR in human prostate
carcinoma cells, and PRK1 promoted a functional complex of AR with the
coactivator TIF2 (NCOA2; 601993). PRK1 signaling stimulated AR activity
in the presence of adrenal androgens and in the presence of an AR
antagonist. Metzger et al. (2003) concluded that AR is controlled by
PRK1 signaling as well as by ligand binding.
MAPPING
Bartsch et al. (1998) used fluorescence in situ hybridization to map the
PRKCL1 gene to 19p13.1-p12 and radiation hybrid mapping to localize the
gene in subband 19p12. By segregation analysis, they mapped the
corresponding mouse gene (Prkcl1) to chromosome 8.
*FIELD* RF
1. Amano, M.; Mukai, H.; Ono, Y.; Chihara, K.; Matsui, T.; Hamajima,
Y.; Okawa, K.; Iwamatsu, A.; Kaibuchi, K.: Identification of a putative
target for rho as the serine-threonine kinase protein kinase N. Science 271:
648-651, 1996.
2. Bartsch, J. W.; Mukai, H.; Takahashi, N.; Ronsiek, M.; Fuchs, S.;
Jockusch, H.; Ono, Y.: The protein kinase N (PKN) gene PRKCL1/Prkcl1
maps to human chromosome 19p12-p13.1 and mouse chromosome 8 with close
linkage to the myodystrophy (myd) mutation. Genomics 49: 129-132,
1998.
3. 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.
4. 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.
5. Palmer, R. H.; Ridden, J.; Parker, P. J.: Identification of multiple,
novel, protein kinase C-related gene products. FEBS Lett. 356: 5-8,
1994.
6. Palmer, R. H.; Ridden, J.; Parker, P. J.: Cloning and expressions
patterns of two members of a novel protein-kinase-C-related kinase
family. Europ. J. Biochem. 227: 344-351, 1995.
7. Ridley, A. J.; Hall, A.: The small GTP-binding protein rho regulates
the assembly of focal adhesions and actin stress fibers in response
to growth factors. Cell 70: 389-399, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 11/29/2005
Carol A. Bocchini - updated: 6/18/1998
Jennifer P. Macke - updated: 6/1/1998
*FIELD* CD
Alan F. Scott: 2/2/1996
*FIELD* ED
carol: 09/07/2012
joanna: 2/2/2009
mgross: 1/23/2007
carol: 11/29/2006
mgross: 11/29/2005
carol: 9/30/2003
terry: 3/7/2000
terry: 6/18/1998
dholmes: 6/1/1998
terry: 3/26/1996
mark: 2/2/1996
*RECORD*
*FIELD* NO
601032
*FIELD* TI
*601032 PROTEIN KINASE N1; PKN1
;;PROTEIN KINASE C-RELATED KINASE 1; PRK1;;
SERINE/THREONINE PROTEIN KINASE N; PKN;;
read morePKN-ALPHA;;
PROTEIN KINASE C-LIKE 1; PRKCL1;;
PAK1, RAT, HOMOLOG OF
*FIELD* TX
CLONING
Mukai and Ono (1994) isolated a cDNA for the protein kinase PRK1, which
they designated PKN, from a human hippocampus cDNA library. The putative
942-amino acid protein has leucine zipper-like sequences at its N
terminus and contains a domain with strong similarity to that of the
protein kinase C (PKC) family. Ubiquitous expression in human tissues
was shown. Antisera detected a 120-kD recombinantly expressed protein on
Western blots. The protein showed intrinsic protein kinase activity that
was abolished by a mutation in the predicted ATP binding site.
Palmer et al. (1994) used degenerate PCR to isolate 3 novel members of
the closely related PKC family, termed PRK1, PRK2 (602549), and PRK3
(610714). Palmer et al. (1995) cloned a full-length cDNA of PRK1 from a
human fetal brain library. Using Northern blot and RT-PCR analyses,
Palmer et al. (1995) detected expression of PRK1 in all tissues and cell
lines tested.
GENE FUNCTION
In a study of proteins that bind to the rho GTPase (see Ridley and Hall,
1992), Amano et al. (1996) discovered a protein that had partial amino
acid sequences identical to PKN. They found that rho binds directly to a
polybasic region of the N-terminal regulatory domain that precedes the
leucine zipper-like motif. The authors speculated that through this
activity, PKN may mediate the rho-dependent signaling pathway.
Metzger et al. (2003) found that androgen receptor (AR; 313700) and PRK1
interact in vitro and in vivo. Stimulation of the PRK1 signaling cascade
resulted in ligand-dependent superactivation of AR in human prostate
carcinoma cells, and PRK1 promoted a functional complex of AR with the
coactivator TIF2 (NCOA2; 601993). PRK1 signaling stimulated AR activity
in the presence of adrenal androgens and in the presence of an AR
antagonist. Metzger et al. (2003) concluded that AR is controlled by
PRK1 signaling as well as by ligand binding.
MAPPING
Bartsch et al. (1998) used fluorescence in situ hybridization to map the
PRKCL1 gene to 19p13.1-p12 and radiation hybrid mapping to localize the
gene in subband 19p12. By segregation analysis, they mapped the
corresponding mouse gene (Prkcl1) to chromosome 8.
*FIELD* RF
1. Amano, M.; Mukai, H.; Ono, Y.; Chihara, K.; Matsui, T.; Hamajima,
Y.; Okawa, K.; Iwamatsu, A.; Kaibuchi, K.: Identification of a putative
target for rho as the serine-threonine kinase protein kinase N. Science 271:
648-651, 1996.
2. Bartsch, J. W.; Mukai, H.; Takahashi, N.; Ronsiek, M.; Fuchs, S.;
Jockusch, H.; Ono, Y.: The protein kinase N (PKN) gene PRKCL1/Prkcl1
maps to human chromosome 19p12-p13.1 and mouse chromosome 8 with close
linkage to the myodystrophy (myd) mutation. Genomics 49: 129-132,
1998.
3. 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.
4. 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.
5. Palmer, R. H.; Ridden, J.; Parker, P. J.: Identification of multiple,
novel, protein kinase C-related gene products. FEBS Lett. 356: 5-8,
1994.
6. Palmer, R. H.; Ridden, J.; Parker, P. J.: Cloning and expressions
patterns of two members of a novel protein-kinase-C-related kinase
family. Europ. J. Biochem. 227: 344-351, 1995.
7. Ridley, A. J.; Hall, A.: The small GTP-binding protein rho regulates
the assembly of focal adhesions and actin stress fibers in response
to growth factors. Cell 70: 389-399, 1992.
*FIELD* CN
Patricia A. Hartz - updated: 11/29/2005
Carol A. Bocchini - updated: 6/18/1998
Jennifer P. Macke - updated: 6/1/1998
*FIELD* CD
Alan F. Scott: 2/2/1996
*FIELD* ED
carol: 09/07/2012
joanna: 2/2/2009
mgross: 1/23/2007
carol: 11/29/2006
mgross: 11/29/2005
carol: 9/30/2003
terry: 3/7/2000
terry: 6/18/1998
dholmes: 6/1/1998
terry: 3/26/1996
mark: 2/2/1996