Serine/threonine-protein kinase N1

Details

Name
Serine/threonine-protein kinase N1
Synonyms
  • 2.7.11.13
  • PAK-1
  • PAK1
  • PKN
  • PRK1
  • PRKCL1
  • Protease-activated kinase 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
Gene Name
PKN1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0051918|Serine/threonine-protein kinase N1
MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLR
RATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTC
SATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDII
RMQLRRALQAGQLENQAAPDDTQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLS
AAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAF
STRLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSMGGPGTPDSRPPF
LSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFT
LELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPV
IERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGS
EARTTGDISVEKLNLGTDSDSSPQKSSRDPPSSPSSLSSPIQESTAPELPSETQETPGPA
LCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESL
MCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFY
SACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPE
FLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSA
EAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTD
VSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC
Number of residues
942
Molecular Weight
103930.995
Theoretical pI
Not Available
GO Classification
Functions
androgen receptor binding / ATP binding / chromatin binding / GTP-Rho binding / histone binding / histone deacetylase binding / histone kinase activity (H3-T11 specific) / ligand-dependent nuclear receptor transcription coactivator activity / protein kinase activity / protein kinase C activity / protein kinase C binding / protein serine/threonine kinase activity / Rac GTPase binding
Processes
activation of JUN kinase activity / B cell apoptotic process / B cell homeostasis / epithelial cell migration / histone H3-T11 phosphorylation / hyperosmotic response / negative regulation of B cell proliferation / negative regulation of protein kinase activity / peptidyl-serine phosphorylation / protein phosphorylation / regulation of cell motility / regulation of germinal center formation / regulation of immunoglobulin production / regulation of transcription by RNA polymerase II / renal system process / signal transduction / spleen development / transcription, DNA-templated
Components
cleavage furrow / cytoplasm / cytosol / endosome / midbody / nucleoplasm / nucleus / protein-containing complex
General 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.
Specific Function
Androgen receptor binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051919|Serine/threonine-protein kinase N1 (PKN1)
ATGGCCAGCGACGCCGTGCAGAGTGAGCCTCGCAGCTGGTCCCTGCTAGAGCAGCTGGGC
CTGGCCGGGGCAGACCTGGCGGCCCCCGGGGTACAGCAGCAGCTGGAGCTGGAGCGGGAG
CGGCTGCGGCGGGAAATCCGCAAGGAGCTGAAGCTGAAGGAGGGTGCTGAGAACCTGCGG
CGGGCCACCACTGACCTGGGCCGCAGCCTGGGCCCCGTAGAGCTGCTGCTGCGGGGCTCC
TCGCGCCGCCTCGACCTGCTGCACCAGCAGCTGCAGGAGCTGCACGCCCACGTGGTGCTT
CCCGACCCGGCGGCCACCCACGATGGCCCCCAGTCCCCTGGTGCGGGTGGCCCCACCTGC
TCGGCCACCAACCTGAGCCGCGTGGCGGGCCTGGAGAAGCAGTTGGCCATTGAGCTGAAG
GTGAAGCAGGGGGCGGAGAACATGATCCAGACCTACAGCAATGGCAGCACCAAGGACCGG
AAGCTGCTGCTGACAGCCCAGCAGATGTTGCAGGACAGTAAGACCAAGATTGACATCATC
CGCATGCAACTCCGCCGGGCGCTGCAGGCCGGCCAGCTGGAGAACCAGGCAGCCCCGGAT
GACACCCAAGGGAGTCCTGACCTGGGGGCTGTGGAGCTGCGCATCGAAGAGCTGCGGCAC
CACTTCCGAGTGGAGCACGCGGTGGCCGAGGGTGCCAAGAACGTACTGCGCCTGCTCAGC
GCTGCCAAGGCCCCGGACCGCAAGGCAGTCAGCGAGGCCCAGGAGAAATTGACAGAATCC
AACCAGAAGCTGGGGCTGCTGCGGGAGGCTCTGGAGCGGAGACTTGGGGAGCTGCCCGCC
GACCACCCCAAGGGGCGGCTGCTGCGAGAAGAGCTCGCTGCGGCCTCCTCCGCTGCCTTC
AGCACCCGCCTGGCCGGGCCCTTTCCCGCCACGCACTACAGCACCCTGTGCAAGCCCGCG
CCGCTCACAGGGACCCTGGAGGTACGAGTGGTGGGCTGCAGAGACCTCCCAGAGACCATC
CCGTGGAACCCTACCCCCTCAATGGGGGGACCTGGGACCCCAGACAGCCGCCCCCCCTTC
CTGAGCCGCCCAGCCCGGGGCCTTTACAGCCGAAGCGGAAGCCTCAGTGGCCGGAGCAGC
CTCAAAGCAGAAGCCGAGAACACCAGTGAAGTCAGCACTGTGCTTAAGCTGGATAACACA
GTGGTGGGGCAGACGTCTTGGAAGCCATGTGGCCCCAATGCCTGGGACCAGAGCTTCACT
CTGGAGCTGGAAAGGGCACGGGAACTGGAGTTGGCTGTGTTCTGGCGGGACCAGCGGGGC
CTGTGTGCCCTCAAATTCCTGAAGTTGGAGGATTTCTTGGACAATGAGAGGCATGAGGTG
CAGCTGGACATGGAACCCCAGGGCTGCCTGGTGGCTGAGGTCACCTTCCGCAACCCTGTC
ATTGAGAGGATTCCTCGGCTCCGACGGCAGAAGAAAATTTTCTCCAAGCAGCAAGGGAAG
GCGTTCCAGCGTGCTAGGCAGATGAACATCGATGTCGCCACGTGGGTGCGGCTGCTCCGG
AGGCTCATCCCCAATGCCACGGGCACAGGCACCTTTAGCCCTGGGGCTTCTCCAGGATCC
GAGGCCCGGACCACGGGTGACATATCGGTGGAGAAGCTGAACCTCGGCACTGACTCGGAC
AGCTCACCTCAGAAGAGCTCGCGGGATCCTCCTTCCAGCCCATCGAGCCTGAGCTCCCCC
ATCCAGGAATCCACTGCTCCCGAGCTGCCTTCGGAGACCCAGGAGACCCCAGGCCCCGCC
CTGTGCAGCCCTCTGAGGAAGTCACCTCTGACCCTCGAAGATTTCAAGTTCCTGGCGGTG
CTGGGCCGGGGTCATTTTGGGAAGGTGCTCCTCTCCGAATTCCGGCCCAGTGGGGAGCTG
TTCGCCATCAAGGCTCTGAAGAAAGGGGACATTGTGGCCCGAGACGAGGTGGAGAGCCTG
ATGTGTGAGAAGCGGATATTGGCGGCAGTGACCAGTGCGGGACACCCCTTCCTGGTGAAC
CTCTTCGGCTGTTTCCAGACACCGGAGCACGTGTGCTTCGTGATGGAGTACTCGGCCGGT
GGGGACCTGATGCTGCACATCCACAGCGACGTGTTCTCTGAGCCCCGTGCCATCTTTTAT
TCCGCCTGCGTGGTGCTGGGCCTACAGTTTCTTCACGAACACAAGATCGTCTACAGGGAC
CTGAAGTTGGACAATTTGCTCCTGGACACCGAGGGCTACGTCAAGATCGCAGACTTTGGC
CTCTGCAAGGAGGGGATGGGCTATGGGGACCGGACCAGCACATTCTGTGGGACCCCGGAG
TTCCTGGCCCCTGAGGTGCTGACGGACACGTCGTACACGCGAGCTGTGGACTGGTGGGGA
CTGGGTGTGCTGCTCTACGAGATGCTGGTTGGCGAGTCCCCATTCCCAGGGGATGATGAG
GAGGAGGTCTTCGACAGCATCGTCAACGACGAGGTTCGCTACCCCCGCTTCCTGTCGGCC
GAAGCCATCGGCATCATGAGAAGGCTGCTTCGGAGGAACCCAGAGCGGAGGCTGGGATCT
AGCGAGAGAGATGCAGAAGATGTGAAGAAACAGCCCTTCTTCAGGACTCTGGGCTGGGAA
GCCCTGTTGGCCCGGCGCCTGCCACCGCCCTTTGTGCCCACGCTGTCCGGCCGCACCGAC
GTCAGCAACTTCGACGAGGAGTTCACCGGGGAGGCCCCCACACTGAGCCCGCCCCGCGAC
GCGCGGCCCCTCACAGCCGCGGAGCAGGCAGCCTTCCTGGACTTCGACTTCGTGGCCGGG
GGCTGCTAG
Chromosome Location
19
Locus
19p13.12
External Identifiers
ResourceLink
UniProtKB IDQ16512
UniProtKB Entry NamePKN1_HUMAN
HGNC IDHGNC:9405
General References
  1. 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. 1994 Mar 15;199(2):897-904. [Article]
  2. Palmer RH, Ridden J, Parker PJ: Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. Eur J Biochem. 1995 Jan 15;227(1-2):344-51. [Article]
  3. 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, 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, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, 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 SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, 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 TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [Article]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Palmer RH, Ridden J, Parker PJ: Identification of multiple, novel, protein kinase C-related gene products. FEBS Lett. 1994 Dec 12;356(1):5-8. [Article]
  7. Palmer RH, Schonwasser DC, Rahman D, Pappin DJ, Herget T, Parker PJ: PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. FEBS Lett. 1996 Jan 15;378(3):281-5. [Article]
  8. 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. 1996 Apr 19;271(16):9816-22. [Article]
  9. 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. 1996 Feb 2;271(5249):645-8. [Article]
  10. 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. 1997 May 29;234(3):621-5. [Article]
  11. Mellor H, Flynn P, Nobes CD, Hall A, Parker PJ: PRK1 is targeted to endosomes by the small GTPase, RhoB. J Biol Chem. 1998 Feb 27;273(9):4811-4. [Article]
  12. 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. 1998 Sep 29;95(20):11566-71. [Article]
  13. Dong LQ, Landa LR, Wick MJ, 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. 2000 May 9;97(10):5089-94. [Article]
  14. 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. 2001 Mar 30;276(13):10025-31. Epub 2000 Dec 4. [Article]
  15. Metzger E, Muller JM, Ferrari S, Buettner R, Schule R: A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer. EMBO J. 2003 Jan 15;22(2):270-80. [Article]
  16. Haraga A, Miller SI: A Salmonella type III secretion effector interacts with the mammalian serine/threonine protein kinase PKN1. Cell Microbiol. 2006 May;8(5):837-46. [Article]
  17. Cottone G, Baldi A, Palescandolo E, Manente L, Penta R, Paggi MG, De Luca A: Pkn is a novel partner of cyclin T2a in muscle differentiation. J Cell Physiol. 2006 Apr;207(1):232-7. doi: 10.1002/jcp.20566. [Article]
  18. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [Article]
  19. Schmidt A, Durgan J, Magalhaes A, Hall A: Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis. EMBO J. 2007 Mar 21;26(6):1624-36. Epub 2007 Mar 1. [Article]
  20. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [Article]
  21. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, 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. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [Article]
  22. Metzger E, Yin N, Wissmann M, Kunowska N, Fischer K, Friedrichs N, Patnaik D, Higgins JM, Potier N, Scheidtmann KH, Buettner R, Schule R: Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation. Nat Cell Biol. 2008 Jan;10(1):53-60. Epub 2007 Dec 9. [Article]
  23. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  24. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  27. Harrison BC, Huynh K, Lundgaard GL, Helmke SM, Perryman MB, McKinsey TA: Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases. FEBS Lett. 2010 Mar 19;584(6):1103-10. doi: 10.1016/j.febslet.2010.02.057. Epub 2010 Feb 24. [Article]
  28. Metzger E, Imhof A, Patel D, Kahl P, Hoffmeyer K, Friedrichs N, Muller JM, 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. 2010 Apr 1;464(7289):792-6. doi: 10.1038/nature08839. Epub 2010 Mar 14. [Article]
  29. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  30. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  31. 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. 2011 Mar 11;286(10):7925-37. doi: 10.1074/jbc.M110.185645. Epub 2011 Jan 11. [Article]
  32. Lachmann S, Jevons A, De Rycker M, Casamassima A, Radtke S, Collazos A, Parker PJ: Regulatory domain selectivity in the cell-type specific PKN-dependence of cell migration. PLoS One. 2011;6(7):e21732. doi: 10.1371/journal.pone.0021732. Epub 2011 Jul 6. [Article]
  33. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  34. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, 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. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  35. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]
  36. 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. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  37. 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. 1999 Nov;4(5):793-803. [Article]
  38. 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. 1999 Jun 15;126(2):166-70. [Article]
  39. Owen D, Lowe PN, Nietlispach D, Brosnan CE, Chirgadze DY, Parker PJ, Blundell TL, Mott HR: Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1). J Biol Chem. 2003 Dec 12;278(50):50578-87. Epub 2003 Sep 26. [Article]
  40. Modha R, Campbell LJ, Nietlispach D, Buhecha HR, Owen D, Mott HR: The Rac1 polybasic region is required for interaction with its effector PRK1. J Biol Chem. 2008 Jan 18;283(3):1492-500. Epub 2007 Nov 15. [Article]
  41. Keszei AF, Tang X, McCormick C, Zeqiraj E, Rohde JR, 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. 2014 Feb;34(3):362-73. doi: 10.1128/MCB.01360-13. Epub 2013 Nov 18. [Article]
  42. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, 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 DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails