JUB (gene)

Jub, ajuba homolog (Xenopus laevis)
Identifiers
Symbols	JUB; Ajuba; MGC15563
External IDs	OMIM: 609066 MGI: 1341886 HomoloGene: 7789 GeneCards: JUB Gene
Gene Ontology Molecular function • chromatin binding • zinc ion binding • alpha-catenin binding • metal ion binding • actin filament binding Cellular component • cytoplasmic mRNA processing body • nucleus • transcription factor complex • cytoplasm • microtubule organizing center • cytosol • cytoskeleton • plasma membrane • cell-cell junction • focal adhesion • lamellipodium Biological process • negative regulation of transcription from RNA polymerase II promoter • cell cycle • cell adhesion • calcium-dependent cell-cell adhesion • lamellipodium assembly • regulation of cell migration • positive regulation of cellular biosynthetic process • positive regulation of protein complex assembly • negative regulation of kinase activity • positive regulation of kinase activity • cellular protein localization • gene silencing by miRNA • wound healing, spreading of epidermal cells • regulation of GTPase activity • positive regulation of I-kappaB kinase/NF-kappaB cascade • positive regulation of MAP kinase activity • glycerophospholipid biosynthetic process • focal adhesion assembly Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	84962	16475
Ensembl	ENSG00000129474	ENSMUSG00000022178
UniProt	Q96IF1	n/a
RefSeq (mRNA)	NM_032876.4	NM_010590.5
RefSeq (protein)	NP_116265.1	NP_034720.2
Location (UCSC)	Chr 14: 23.44 – 23.45 Mb	Chr 14: 55.19 – 55.2 Mb
PubMed search	[1]	[2]

Protein ajuba is a protein that in humans is encoded by the JUB gene.

JUB proteins contribute to cell fate determination and regulate cell proliferation and differentiation. Plays an important role in regulation of the kinase activity of AURKA/Aurora-A for mitotic commitment.

Interactions

JUB (gene) has been shown to interact with Stratifin and SLC1A2.

Further reading

• Kanungo J, Pratt SJ, Marie H, Longmore GD (2000). "Ajuba, a Cytosolic LIM Protein, Shuttles into the Nucleus and Affects Embryonal Cell Proliferation and Fate Decisions". Mol. Biol. Cell 11 (10): 3299–313. PMC 14993. PMID 11029037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=14993. 
• Marie H, Billups D, Bedford FK, et al. (2002). "The amino terminus of the glial glutamate transporter GLT-1 interacts with the LIM protein Ajuba". Mol. Cell. Neurosci. 19 (2): 152–64. doi:10.1006/mcne.2001.1066. PMID 11860269. 
• Marie H, Pratt SJ, Betson M, et al. (2003). "The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin". J. Biol. Chem. 278 (2): 1220–8. doi:10.1074/jbc.M205391200. PMID 12417594. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Hirota T, Kunitoku N, Sasayama T, et al. (2003). "Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells". Cell 114 (5): 585–98. doi:10.1016/S0092-8674(03)00642-1. PMID 13678582. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Pratt SJ, Epple H, Ward M, et al. (2005). "The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration". J. Cell Biol. 168 (5): 813–24. doi:10.1083/jcb.200406083. PMC 2171823. PMID 15728191. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2171823. 
• Benzinger A, Muster N, Koch HB, et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465. 
• Kisseleva M, Feng Y, Ward M, et al. (2005). "The LIM Protein Ajuba Regulates Phosphatidylinositol 4,5-Bisphosphate Levels in Migrating Cells through an Interaction with and Activation of PIPKIα". Mol. Cell. Biol. 25 (10): 3956–66. doi:10.1128/MCB.25.10.3956-3966.2005. PMC 1087706. PMID 15870270. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1087706. 
• Feng Y, Longmore GD (2005). "The LIM Protein Ajuba Influences Interleukin-1-Induced NF-κB Activation by Affecting the Assembly and Activity of the Protein Kinase Cζ/p62/TRAF6 Signaling Complex". Mol. Cell. Biol. 25 (10): 4010–22. doi:10.1128/MCB.25.10.4010-4022.2005. PMC 1087715. PMID 15870274. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1087715. 
• Abe Y, Ohsugi M, Haraguchi K, et al. (2006). "LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis". FEBS Lett. 580 (3): 782–8. doi:10.1016/j.febslet.2005.12.096. PMID 16413547. 
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
• Alagaratnam S, Hardy JR, Lothe RA, Skotheim RI, Byrne JA (2008). "TPD52, a candidate gene from genomic studies, is overexpressed in testicular germ cell tumours". Mol. Cell Endocrinol. 306 (1–2): 75–80. doi:10.1016/j.mce.2008.10.043. PMID 19041365.