Ribosomal protein S6 kinase alpha-3

Details

Name
Ribosomal protein S6 kinase alpha-3
Synonyms
  • 2.7.11.1
  • 90 kDa ribosomal protein S6 kinase 3
  • Insulin-stimulated protein kinase 1
  • ISPK-1
  • ISPK1
  • MAP kinase-activated protein kinase 1b
  • MAPK-activated protein kinase 1b
  • MAPKAP kinase 1b
  • MAPKAPK-1b
  • MAPKAPK1B
  • p90-RSK 3
  • p90RSK3
  • pp90RSK2
  • Ribosomal S6 kinase 2
  • RSK-2
  • RSK2
  • S6K-alpha-3
Gene Name
RPS6KA3
Organism
Humans
Amino acid sequence
>lcl|BSEQ0008668|Ribosomal protein S6 kinase alpha-3
MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEVSIKEIAITHHVKEGH
EKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERD
ILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALA
LDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVV
NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLR
MLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPE
FTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTD
GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLK
DVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDL
KPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACD
IWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKML
HVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEP
VGRSTLAQRRGIKKITSTAL
Number of residues
740
Molecular Weight
83735.325
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / magnesium ion binding / protein kinase activity / protein serine/threonine kinase activity / ribosomal protein S6 kinase activity
Processes
axon guidance / cell cycle / central nervous system development / innate immune response / intracellular signal transduction / MyD88-dependent toll-like receptor signaling pathway / MyD88-independent toll-like receptor signaling pathway / negative regulation of apoptotic process / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / neurotrophin TRK receptor signaling pathway / positive regulation of cell differentiation / positive regulation of cell growth / positive regulation of transcription from RNA polymerase II promoter / protein phosphorylation / regulation of DNA-templated transcription in response to stress / regulation of translation in response to stress / response to lipopolysaccharide / signal transduction / skeletal system development / stress-activated MAPK cascade / synaptic transmission / toll-like receptor 10 signaling pathway / toll-like receptor 2 signaling pathway / toll-like receptor 3 signaling pathway / toll-like receptor 4 signaling pathway / toll-like receptor 5 signaling pathway / toll-like receptor 9 signaling pathway / toll-like receptor signaling pathway / toll-like receptor TLR1 / toll-like receptor TLR6 / TRIF-dependent toll-like receptor signaling pathway
Components
cytoplasm / cytosol / nucleoplasm
General Function
Ribosomal protein s6 kinase activity
Specific Function
Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0013342|Ribosomal protein S6 kinase alpha-3 (RPS6KA3)
ATGCCGCTGGCGCAGCTGGCGGACCCGTGGCAGAAGATGGCTGTGGAGAGCCCGTCCGAC
AGCGCTGAGAATGGACAGCAAATTATGGATGAACCTATGGGAGAGGAGGAGATTAACCCA
CAAACTGAAGAAGTCAGTATCAAAGAAATTGCAATCACACATCATGTAAAGGAAGGACAT
GAAAAGGCAGATCCTTCCCAGTTTGAACTTTTAAAAGTATTAGGGCAGGGATCATTTGGA
AAGGTTTTCTTAGTTAAAAAAATCTCAGGCTCTGATGCTAGGCAGCTTTATGCCATGAAG
GTATTGAAGAAGGCCACACTGAAAGTTCGAGACCGAGTTCGGACAAAAATGGAACGTGAT
ATCTTGGTAGAGGTTAATCATCCTTTTATTGTCAAGTTGCATTATGCTTTTCAAACTGAA
GGGAAGTTGTATCTTATTTTGGATTTTCTCAGGGGAGGAGATTTGTTTACACGCTTATCC
AAAGAGGTGATGTTCACAGAAGAAGATGTCAAATTCTACTTGGCTGAACTTGCACTTGCT
TTAGACCATCTACATAGCCTGGGAATAATTTATAGAGACTTAAAACCAGAAAATATACTT
CTTGATGAAGAAGGTCACATCAAGTTAACAGATTTCGGCCTAAGTAAAGAGTCTATTGAC
CATGAAAAGAAGGCATATTCTTTTTGTGGAACTGTGGAGTATATGGCTCCAGAAGTAGTT
AATCGTCGAGGTCATACTCAGAGTGCTGACTGGTGGTCTTTTGGTGTGTTAATGTTTGAA
ATGCTTACTGGTACACTCCCTTTCCAAGGAAAAGATCGAAAAGAAACAATGACTATGATT
CTTAAAGCCAAACTTGGAATGCCACAGTTTTTGAGTCCTGAAGCGCAGAGTCTTTTACGA
ATGCTTTTCAAGCGAAATCCTGCAAACAGATTAGGTGCAGGACCAGATGGAGTTGAAGAA
ATTAAAAGACATTCATTTTTCTCAACGATAGACTGGAATAAACTGTATAGAAGAGAAATT
CATCCGCCATTTAAACCTGCAACGGGCAGGCCTGAAGATACATTCTATTTTGATCCTGAG
TTTACTGCAAAAACTCCCAAAGATTCACCTGGCATTCCACCTAGTGCTAATGCACATCAG
CTTTTTCGGGGGTTTAGTTTTGTTGCTATTACCTCAGATGATGAAAGCCAAGCTATGCAG
ACAGTTGGTGTACATTCAATTGTTCAGCAGTTACACAGGAACAGTATTCAGTTTACTGAT
GGATATGAAGTAAAAGAAGATATTGGAGTTGGCTCCTACTCTGTTTGCAAGAGATGTATA
CATAAAGCTACAAACATGGAGTTTGCAGTGAAGATTATTGATAAAAGCAAGAGAGACCCA
ACAGAAGAAATTGAAATTCTTCTTCGTTATGGACAGCATCCAAACATTATCACTCTAAAG
GATGTATATGATGATGGAAAGTATGTGTATGTAGTAACAGAACTTATGAAAGGAGGTGAA
TTGCTGGATAAAATTCTTAGACAAAAATTTTTCTCTGAACGAGAGGCCAGTGCTGTCCTG
TTCACTATAACTAAAACCGTTGAATATCTTCACGCACAAGGGGTGGTTCATAGAGACTTG
AAACCTAGCAACATTCTTTATGTGGATGAATCTGGTAATCCGGAATCTATTCGAATTTGT
GATTTTGGCTTTGCAAAACAGCTGAGAGCGGAAAATGGTCTTCTCATGACTCCTTGTTAC
ACTGCAAATTTTGTTGCACCAGAGGTTTTAAAAAGACAAGGCTATGATGCTGCTTGTGAT
ATATGGAGTCTTGGTGTCCTACTCTATACAATGCTTACCGGTTACACTCCATTTGCAAAT
GGTCCTGATGATACACCAGAGGAAATATTGGCACGAATAGGTAGCGGAAAATTCTCACTC
AGTGGTGGTTACTGGAATTCTGTTTCAGACACAGCAAAGGACCTGGTGTCAAAGATGCTT
CATGTAGACCCTCATCAGAGACTGACTGCTGCTCTTGTGCTCAGACATCCTTGGATCGTC
CACTGGGACCAACTGCCACAATACCAACTAAACAGACAGGATGCACCACATCTAGTAAAG
GGTGCCATGGCAGCTACATATTCTGCTTTGAACCGTAATCAGTCACCAGTTTTGGAACCA
GTAGGCCGCTCTACTCTTGCTCAGCGGAGAGGTATTAAAAAAATCACCTCAACAGCCCTG
TGA
Chromosome Location
X
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP51812
UniProtKB Entry NameKS6A3_HUMAN
HGNC IDHGNC:10432
General References
  1. Bjorbaek C, Vik TA, Echwald SM, Yang PY, Vestergaard H, Wang JP, Webb GC, Richmond K, Hansen T, Erikson RL, et al.: Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene and analysis of coding regions and mRNA levels of the ISPK-1 and the protein phosphatase-1 genes in muscle from NIDDM patients. Diabetes. 1995 Jan;44(1):90-7. [PubMed:7813820]
  2. 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. [PubMed:14702039]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed:15772651]
  4. 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. [PubMed:15489334]
  5. Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M: Human rsk isoforms: cloning and characterization of tissue-specific expression. Am J Physiol. 1994 Feb;266(2 Pt 1):C351-9. [PubMed:8141249]
  6. Kitano T, Schwarz C, Nickel B, Paabo S: Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees. Mol Biol Evol. 2003 Aug;20(8):1281-9. Epub 2003 May 30. [PubMed:12777533]
  7. Sutherland C, Leighton IA, Cohen P: Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. Biochem J. 1993 Nov 15;296 ( Pt 1):15-9. [PubMed:8250835]
  8. De Cesare D, Jacquot S, Hanauer A, Sassone-Corsi P: Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene. Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12202-7. [PubMed:9770464]
  9. Sassone-Corsi P, Mizzen CA, Cheung P, Crosio C, Monaco L, Jacquot S, Hanauer A, Allis CD: Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3. Science. 1999 Aug 6;285(5429):886-91. [PubMed:10436156]
  10. Anjum R, Roux PP, Ballif BA, Gygi SP, Blenis J: The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling. Curr Biol. 2005 Oct 11;15(19):1762-7. [PubMed:16213824]
  11. Wingate AD, Campbell DG, Peggie M, Arthur JS: Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation. Biochem J. 2006 Feb 1;393(Pt 3):715-24. [PubMed:16223362]
  12. 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. [PubMed:16964243]
  13. Cho YY, Yao K, Bode AM, Bergen HR 3rd, Madden BJ, Oh SM, Ermakova S, Kang BS, Choi HS, Shim JH, Dong Z: RSK2 mediates muscle cell differentiation through regulation of NFAT3. J Biol Chem. 2007 Mar 16;282(11):8380-92. Epub 2007 Jan 9. [PubMed:17213202]
  14. Roux PP, Shahbazian D, Vu H, Holz MK, Cohen MS, Taunton J, Sonenberg N, Blenis J: RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation. J Biol Chem. 2007 May 11;282(19):14056-64. Epub 2007 Mar 14. [PubMed:17360704]
  15. Carriere A, Cargnello M, Julien LA, Gao H, Bonneil E, Thibault P, Roux PP: Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation. Curr Biol. 2008 Sep 9;18(17):1269-77. doi: 10.1016/j.cub.2008.07.078. Epub 2008 Aug 21. [PubMed:18722121]
  16. Carriere A, Ray H, Blenis J, Roux PP: The RSK factors of activating the Ras/MAPK signaling cascade. Front Biosci. 2008 May 1;13:4258-75. [PubMed:18508509]
  17. 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. [PubMed:18691976]
  18. Anjum R, Blenis J: The RSK family of kinases: emerging roles in cellular signalling. Nat Rev Mol Cell Biol. 2008 Oct;9(10):747-58. doi: 10.1038/nrm2509. [PubMed:18813292]
  19. 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. [PubMed:18669648]
  20. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195]
  21. 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. [PubMed:19690332]
  22. 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. [PubMed:20068231]
  23. 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. [PubMed:21269460]
  24. 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. [PubMed:21406692]
  25. 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. [PubMed:24275569]
  26. Trivier E, De Cesare D, Jacquot S, Pannetier S, Zackai E, Young I, Mandel JL, Sassone-Corsi P, Hanauer A: Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome. Nature. 1996 Dec 12;384(6609):567-70. [PubMed:8955270]
  27. Jacquot S, Merienne K, De Cesare D, Pannetier S, Mandel JL, Sassone-Corsi P, Hanauer A: Mutation analysis of the RSK2 gene in Coffin-Lowry patients: extensive allelic heterogeneity and a high rate of de novo mutations. Am J Hum Genet. 1998 Dec;63(6):1631-40. [PubMed:9837815]
  28. Abidi F, Jacquot S, Lassiter C, Trivier E, Hanauer A, Schwartz CE: Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS). Eur J Hum Genet. 1999 Jan;7(1):20-6. [PubMed:10094187]
  29. Manouvrier-Hanu S, Amiel J, Jacquot S, Merienne K, Moerman A, Coeslier A, Labarriere F, Vallee L, Croquette MF, Hanauer A: Unreported RSK2 missense mutation in two male sibs with an unusually mild form of Coffin-Lowry syndrome. J Med Genet. 1999 Oct;36(10):775-8. [PubMed:10528858]
  30. Merienne K, Jacquot S, Pannetier S, Zeniou M, Bankier A, Gecz J, Mandel JL, Mulley J, Sassone-Corsi P, Hanauer A: A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation. Nat Genet. 1999 May;22(1):13-4. [PubMed:10319851]
  31. Martinez-Garay I, Ballesta MJ, Oltra S, Orellana C, Palomeque A, Molto MD, Prieto F, Martinez F: Intronic L1 insertion and F268S, novel mutations in RPS6KA3 (RSK2) causing Coffin-Lowry syndrome. Clin Genet. 2003 Dec;64(6):491-6. [PubMed:14986828]
  32. Facher JJ, Regier EJ, Jacobs GH, Siwik E, Delaunoy JP, Robin NH: Cardiomyopathy in Coffin-Lowry syndrome. Am J Med Genet A. 2004 Jul 15;128A(2):176-8. [PubMed:15214012]
  33. Field M, Tarpey P, Boyle J, Edkins S, Goodship J, Luo Y, Moon J, Teague J, Stratton MR, Futreal PA, Wooster R, Raymond FL, Turner G: Mutations in the RSK2(RPS6KA3) gene cause Coffin-Lowry syndrome and nonsyndromic X-linked mental retardation. Clin Genet. 2006 Dec;70(6):509-15. [PubMed:17100996]
  34. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974]
  35. 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. [PubMed:17344846]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00945Acetylsalicylic acidapproved, vet_approvedunknowninhibitorDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails