- CAB39
Calcium binding protein 39, also known as CAB39, is a human
gene .cite web | title = Entrez Gene: CAB39 calcium binding protein 39| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51719| accessdate = ]The
protein encoded by this gene associates withSTK11 (Serine/Threonine Kinase 11) and STRAD (STE20-Related ADaptor protein).cite journal | author = Boudeau J, Baas AF, Deak M, Morrice NA, Kieloch A, Schutkowski M, Prescott AR, Clevers HC, Alessi DR | title = MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm | journal = EMBO J. | volume = 22 | issue = 19 | pages = 5102–14 | year = 2003 | month = October | pmid = 14517248 | pmc = 204473 | doi = 10.1093/emboj/cdg490 | url = | issn = ] CAB39 enhances formation of STK11/STRAD complexes and stimulates STK11 catalytic activity. CAB39 may function as a scaffolding component of the STK11/STRAD complex and regulates STK11 activity and cellular localization.References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Baas AF, Smit L, Clevers H |title=LKB1 tumor suppressor protein: PARtaker in cell polarity. |journal=Trends Cell Biol. |volume=14 |issue= 6 |pages= 312–9 |year= 2004 |pmid= 15183188 |doi= 10.1016/j.tcb.2004.04.001
*cite journal | author=Hawley SA, Davison M, Woods A, "et al." |title=Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27879–87 |year= 1996 |pmid= 8910387 |doi=
*cite journal | author=Lai CH, Chou CY, Ch'ang LY, "et al." |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703–13 |year= 2000 |pmid= 10810093 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Boudeau J, Baas AF, Deak M, "et al." |title=MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm. |journal=EMBO J. |volume=22 |issue= 19 |pages= 5102–14 |year= 2003 |pmid= 14517248 |doi= 10.1093/emboj/cdg490
*cite journal | author=Brajenovic M, Joberty G, Küster B, "et al." |title=Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network. |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12804–11 |year= 2004 |pmid= 14676191 |doi= 10.1074/jbc.M312171200
*cite journal | author=Milburn CC, Boudeau J, Deak M, "et al." |title=Crystal structure of MO25 alpha in complex with the C terminus of the pseudo kinase STE20-related adaptor. |journal=Nat. Struct. Mol. Biol. |volume=11 |issue= 2 |pages= 193–200 |year= 2004 |pmid= 14730349 |doi= 10.1038/nsmb716
*cite journal | author=Lizcano JM, Göransson O, Toth R, "et al." |title=LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. |journal=EMBO J. |volume=23 |issue= 4 |pages= 833–43 |year= 2005 |pmid= 14976552 |doi= 10.1038/sj.emboj.7600110
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Boudeau J, Scott JW, Resta N, "et al." |title=Analysis of the LKB1-STRAD-MO25 complex. |journal=J. Cell. Sci. |volume=117 |issue= Pt 26 |pages= 6365–75 |year= 2005 |pmid= 15561763 |doi= 10.1242/jcs.01571
*cite journal | author=Ewing RM, Chu P, Elisma F, "et al." |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134PBB_Controls
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