cAMP-dependent protein kinase catalytic subunit alpha

NamecAMP-dependent protein kinase catalytic subunit alpha
Synonyms2.7.11.11 PKA C-alpha PKACA
Gene NamePRKACA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0007218|cAMP-dependent protein kinase catalytic subunit alpha
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML
VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
Number of residues351
Molecular Weight40589.38
Theoretical pI9.22
GO Classification
Functions
    ATP binding
protein kinase A regulatory subunit binding
protein kinase binding
protein serine/threonine/tyrosine kinase activity
cAMP-dependent protein kinase activity
ubiquitin protein ligase binding
Processes
    G2/M transition of mitotic cell cycle
renal water homeostasis
cellular response to parathyroid hormone stimulus
protein phosphorylation
cellular response to glucose stimulus
mitotic cell cycle
regulation of protein processing
water transport
negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning
stimulatory C-type lectin receptor signaling pathway
sperm capacitation
organelle organization
regulation of proteasomal protein catabolic process
carbohydrate metabolic process
neural tube closure
positive regulation of cell cycle arrest
energy reserve metabolic process
regulation of osteoblast differentiation
signal transduction
glucose metabolic process
peptidyl-serine phosphorylation
regulation of insulin secretion
positive regulation of protein export from nucleus
activation of phospholipase C activity
regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
regulation of synaptic transmission, glutamatergic
cytosolic calcium ion homeostasis
regulation of heart rate
cell communication by electrical coupling involved in cardiac conduction
blood coagulation
activation of protein kinase A activity
positive regulation of cell proliferation
protein autophosphorylation
regulation of bicellular tight junction assembly
cellular response to epinephrine stimulus
epidermal growth factor receptor signaling pathway
intracellular signal transduction
calcium-mediated signaling using intracellular calcium source
gluconeogenesis
regulation of protein binding
innate immune response
regulation of cardiac muscle contraction
mesoderm formation
triglyceride catabolic process
negative regulation of meiotic cell cycle
transmembrane transport
peptidyl-threonine phosphorylation
fibroblast growth factor receptor signaling pathway
small molecule metabolic process
cellular response to glucagon stimulus
regulation of cellular respiration
neurotrophin TRK receptor signaling pathway
regulation of ryanodine-sensitive calcium-release channel activity
Components
    cytosol
calcium channel complex
extracellular exosome
mitochondrion
motile cilium
plasma membrane raft
nucleoplasm
perinuclear region of cytoplasm
nucleus
neuromuscular junction
nucleotide-activated protein kinase complex
neuron projection
cAMP-dependent protein kinase complex
centrosome
Golgi apparatus
ciliary base
sperm midpiece
General FunctionUbiquitin protein ligase binding
Specific FunctionPhosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.
Transmembrane Regions
GenBank Protein ID35479
UniProtKB IDP17612
UniProtKB Entry NameKAPCA_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0017217|cAMP-dependent protein kinase catalytic subunit alpha (PRKACA)
ATGTTCACCTTGGGATACCATGGGGCCGAGGAGTGGGCATCGGGCGAGACTTCCCTTGAA
CCAGCTCTGGAGCAATGCCCTTGCGATTGCCACGGAGAGGAACAGGGCCAGCTGGGGGCC
AAGGTGACAGCTGAGCCCCCCAAGGGCACCTGCTACCCGAGCCCCCGAGGCCTCCATCCC
AGGCCCGGCCTCCCCAGAGAAGGGGCCAGAGGAACAGCCAAATCCCAAGGCTATAAATAC
CTCGGCTGGCGTCGGCCCTGGCCATGGAATGTCGTGAAAGAATTCTTAGCCAAAGCCAAA
GAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCACTTGGATCAGTTT
GAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTGGTGAAACACAAG
GAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTGGTGAAACTGAAA
CAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAACTTTCCGTTCCTC
GTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTCATGGAGTACGTG
CCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGTGAGCCCCATGCC
CGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCGCTGGATCTCATC
TACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTACATTCAGGTGACA
GACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGCGGCACCCCTGAG
TACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTGGACTGGTGGGCC
CTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTCGCAGACCAGCCC
ATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCCCACTTCAGCTCT
GACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAGCGCTTTGGGAAC
CTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACAACTGACTGGATT
GCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAAGGCCCTGGGGAT
ACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATCAATGAGAAGTGT
GGCAAGGAGTTTTCTGAGTTTTAG
GenBank Gene IDX07767
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:9380
Chromosome Location19
Locus19p13.1
References
  1. Maldonado F, Hanks SK: A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha. Nucleic Acids Res. 1988 Aug 25;16(16):8189-90.[2843813 ]
  2. 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.[15489334 ]
  3. Reinton N, Orstavik S, Haugen TB, Jahnsen T, Tasken K, Skalhegg BS: A novel isoform of human cyclic 3',5'-adenosine monophosphate-dependent protein kinase, c alpha-s, localizes to sperm midpiece. Biol Reprod. 2000 Aug;63(2):607-11.[10906071 ]
  4. Agustin JT, Wilkerson CG, Witman GB: The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Calpha mRNA expressed specifically in spermatogenic cells. Mol Biol Cell. 2000 Sep;11(9):3031-44.[10982398 ]
  5. Desseyn JL, Burton KA, McKnight GS: Expression of a nonmyristylated variant of the catalytic subunit of protein kinase A during male germ-cell development. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6433-8.[10841548 ]
  6. Moore MJ, Kanter JR, Jones KC, Taylor SS: Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1. J Biol Chem. 2002 Dec 6;277(49):47878-84. Epub 2002 Oct 7.[12372837 ]
  7. Kohler K, Louvard D, Zahraoui A: Rab13 regulates PKA signaling during tight junction assembly. J Cell Biol. 2004 Apr 26;165(2):175-80. Epub 2004 Apr 19.[15096524 ]
  8. Guan H, Hou S, Ricciardi RP: DNA binding of repressor nuclear factor-kappaB p50/p50 depends on phosphorylation of Ser337 by the protein kinase A catalytic subunit. J Biol Chem. 2005 Mar 18;280(11):9957-62. Epub 2005 Jan 7.[15642694 ]
  9. D'Souza T, Agarwal R, Morin PJ: Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells. J Biol Chem. 2005 Jul 15;280(28):26233-40. Epub 2005 May 19.[15905176 ]
  10. Pasqualucci L, Kitaura Y, Gu H, Dalla-Favera R: PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells. Proc Natl Acad Sci U S A. 2006 Jan 10;103(2):395-400. Epub 2005 Dec 30.[16387847 ]
  11. Xiao B, Tian X, Xie W, Jones PP, Cai S, Wang X, Jiang D, Kong H, Zhang L, Chen K, Walsh MP, Cheng H, Chen SR: Functional consequence of protein kinase A-dependent phosphorylation of the cardiac ryanodine receptor: sensitization of store overload-induced Ca2+ release. J Biol Chem. 2007 Oct 12;282(41):30256-64. Epub 2007 Aug 10.[17693412 ]
  12. Ichikawa T, Horie-Inoue K, Ikeda K, Blumberg B, Inoue S: Vitamin K2 induces phosphorylation of protein kinase A and expression of novel target genes in osteoblastic cells. J Mol Endocrinol. 2007 Oct;39(4):239-47.[17909264 ]
  13. Xu H, Washington S, Verderame MF, Manni A: Activation of protein kinase A (PKA) signaling mitigates the antiproliferative and antiinvasive effects of alpha-difluoromethylornithine in breast cancer cells. Breast Cancer Res Treat. 2008 Jan;107(1):63-70. Epub 2007 Feb 27.[17333334 ]
  14. 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.[18691976 ]
  15. Shirakawa K, Takaori-Kondo A, Yokoyama M, Izumi T, Matsui M, Io K, Sato T, Sato H, Uchiyama T: Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif. Nat Struct Mol Biol. 2008 Nov;15(11):1184-91. doi: 10.1038/nsmb.1497. Epub 2008 Oct 5.[18836454 ]
  16. Masterson LR, Mascioni A, Traaseth NJ, Taylor SS, Veglia G: Allosteric cooperativity in protein kinase A. Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):506-11. doi: 10.1073/pnas.0709214104. Epub 2008 Jan 4.[18178622 ]
  17. Yan X, Walkiewicz M, Carlson J, Leiphon L, Grove B: Gravin dynamics regulates the subcellular distribution of PKA. Exp Cell Res. 2009 Apr 15;315(7):1247-59. doi: 10.1016/j.yexcr.2008.12.026. Epub 2009 Jan 13.[19210988 ]
  18. 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.[19369195 ]
  19. 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.[19690332 ]
  20. Wang W, Zhang X, Zheng J, Yang J: High glucose stimulates adipogenic and inhibits osteogenic differentiation in MG-63 cells through cAMP/protein kinase A/extracellular signal-regulated kinase pathway. Mol Cell Biochem. 2010 May;338(1-2):115-22. doi: 10.1007/s11010-009-0344-6. Epub 2009 Dec 1.[19949837 ]
  21. 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.[21269460 ]
  22. Ermisch M, Firla B, Steinhilber D: Protein kinase A activates and phosphorylates RORalpha4 in vitro and takes part in RORalpha activation by CaMK-IV. Biochem Biophys Res Commun. 2011 May 13;408(3):442-6. doi: 10.1016/j.bbrc.2011.04.046. Epub 2011 Apr 13.[21514275 ]
  23. Vetter MM, Zenn HM, Mendez E, van den Boom H, Herberg FW, Skalhegg BS: The testis-specific Calpha2 subunit of PKA is kinetically indistinguishable from the common Calpha1 subunit of PKA. BMC Biochem. 2011 Aug 3;12:40. doi: 10.1186/1471-2091-12-40.[21812984 ]
  24. Lignitto L, Carlucci A, Sepe M, Stefan E, Cuomo O, Nistico R, Scorziello A, Savoia C, Garbi C, Annunziato L, Feliciello A: Control of PKA stability and signalling by the RING ligase praja2. Nat Cell Biol. 2011 Apr;13(4):412-22. doi: 10.1038/ncb2209. Epub 2011 Mar 20.[21423175 ]
  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.[24275569 ]
  26. Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW: Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. Nat Commun. 2014 Sep 26;5:4919. doi: 10.1038/ncomms5919.[25255805 ]
  27. Goh G, Scholl UI, Healy JM, Choi M, Prasad ML, Nelson-Williams C, Kunstman JW, Korah R, Suttorp AC, Dietrich D, Haase M, Willenberg HS, Stalberg P, Hellman P, Akerstrom G, Bjorklund P, Carling T, Lifton RP: Recurrent activating mutation in PRKACA in cortisol-producing adrenal tumors. Nat Genet. 2014 Jun;46(6):613-7. doi: 10.1038/ng.2956. Epub 2014 Apr 20.[24747643 ]
  28. Broncel M, Serwa RA, Ciepla P, Krause E, Dallman MJ, Magee AI, Tate EW: Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development. Angew Chem Int Ed Engl. 2015 May 11;54(20):5948-51. doi: 10.1002/anie.201500342. Epub 2015 Mar 25.[25807930 ]
  29. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8.[25944712 ]
  30. Lin X, Murray JM, Rico AC, Wang MX, Chu DT, Zhou Y, Del Rosario M, Kaufman S, Ma S, Fang E, Crawford K, Jefferson AB: Discovery of 2-pyrimidyl-5-amidothiophenes as potent inhibitors for AKT: synthesis and SAR studies. Bioorg Med Chem Lett. 2006 Aug 15;16(16):4163-8. Epub 2006 Jun 9.[16765046 ]
  31. Zeng Q, Allen JG, Bourbeau MP, Wang X, Yao G, Tadesse S, Rider JT, Yuan CC, Hong FT, Lee MR, Zhang S, Lofgren JA, Freeman DJ, Yang S, Li C, Tominey E, Huang X, Hoffman D, Yamane HK, Fotsch C, Dominguez C, Hungate R, Zhang X: Azole-based inhibitors of AKT/PKB for the treatment of cancer. Bioorg Med Chem Lett. 2010 Mar 1;20(5):1559-64. doi: 10.1016/j.bmcl.2010.01.067. Epub 2010 Jan 21.[20137943 ]
  32. Freeman-Cook KD, Autry C, Borzillo G, Gordon D, Barbacci-Tobin E, Bernardo V, Briere D, Clark T, Corbett M, Jakubczak J, Kakar S, Knauth E, Lippa B, Luzzio MJ, Mansour M, Martinelli G, Marx M, Nelson K, Pandit J, Rajamohan F, Robinson S, Subramanyam C, Wei L, Wythes M, Morris J: Design of selective, ATP-competitive inhibitors of Akt. J Med Chem. 2010 Jun 24;53(12):4615-22. doi: 10.1021/jm1003842.[20481595 ]
  33. Pflug A, de Oliveira TM, Bossemeyer D, Engh RA: Mutants of protein kinase A that mimic the ATP-binding site of Aurora kinase. Biochem J. 2011 Nov 15;440(1):85-93. doi: 10.1042/BJ20110592.[21774789 ]
  34. Beuschlein F, Fassnacht M, Assie G, Calebiro D, Stratakis CA, Osswald A, Ronchi CL, Wieland T, Sbiera S, Faucz FR, Schaak K, Schmittfull A, Schwarzmayr T, Barreau O, Vezzosi D, Rizk-Rabin M, Zabel U, Szarek E, Salpea P, Forlino A, Vetro A, Zuffardi O, Kisker C, Diener S, Meitinger T, Lohse MJ, Reincke M, Bertherat J, Strom TM, Allolio B: Constitutive activation of PKA catalytic subunit in adrenal Cushing's syndrome. N Engl J Med. 2014 Mar 13;370(11):1019-28. doi: 10.1056/NEJMoa1310359. Epub 2014 Feb 26.[24571724 ]
  35. Cao Y, He M, Gao Z, Peng Y, Li Y, Li L, Zhou W, Li X, Zhong X, Lei Y, Su T, Wang H, Jiang Y, Yang L, Wei W, Yang X, Jiang X, Liu L, He J, Ye J, Wei Q, Li Y, Wang W, Wang J, Ning G: Activating hotspot L205R mutation in PRKACA and adrenal Cushing's syndrome. Science. 2014 May 23;344(6186):913-7. doi: 10.1126/science.1249480. Epub 2014 Apr 3.[24700472 ]
  36. Sato Y, Maekawa S, Ishii R, Sanada M, Morikawa T, Shiraishi Y, Yoshida K, Nagata Y, Sato-Otsubo A, Yoshizato T, Suzuki H, Shiozawa Y, Kataoka K, Kon A, Aoki K, Chiba K, Tanaka H, Kume H, Miyano S, Fukayama M, Nureki O, Homma Y, Ogawa S: Recurrent somatic mutations underlie corticotropin-independent Cushing's syndrome. Science. 2014 May 23;344(6186):917-20. doi: 10.1126/science.1252328.[24855271 ]
  37. 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.[14702039 ]
  38. Zhang F, Hu Y, Huang P, Toleman CA, Paterson AJ, Kudlow JE: Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J Biol Chem. 2007 Aug 3;282(31):22460-71. Epub 2007 Jun 12.[17565987 ]
  39. Gambaryan S, Kobsar A, Rukoyatkina N, Herterich S, Geiger J, Smolenski A, Lohmann SM, Walter U: Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex. J Biol Chem. 2010 Jun 11;285(24):18352-63. doi: 10.1074/jbc.M109.077602. Epub 2010 Mar 31.[20356841 ]
  40. Pflug A, Rogozina J, Lavogina D, Enkvist E, Uri A, Engh RA, Bossemeyer D: Diversity of bisubstrate binding modes of adenosine analogue-oligoarginine conjugates in protein kinase a and implications for protein substrate interactions. J Mol Biol. 2010 Oct 15;403(1):66-77. doi: 10.1016/j.jmb.2010.08.028. Epub 2010 Aug 21.[20732331 ]
  41. 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.[17344846 ]

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