JUB (gene)

Protein ajuba is a protein that in humans is encoded by the JUB gene.[5][6]

AJUBA
Identifiers
Aliases	AJUBA, JUB, ajuba LIM protein
External IDs	OMIM: 609066 MGI: 1341886 HomoloGene: 7789 GeneCards: AJUBA
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q11.2 Start 22,971,177 bp[1] End 22,982,551 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 C2 Start 54,567,472 bp[2] End 54,577,558 bp[2]
Gene ontology Molecular function • GO:0001106 transcription corepressor activity • chromatin binding • metal ion binding • actin filament binding • GO:0001948 protein binding • alpha-catenin binding Cellular component • cytoplasm • membrane • focal adhesion • intercellular junction • cell membrane • P-body • microtubule organizing center • cell junction • cytoskeleton • cell nucleus • lamellipodium • transcription factor complex • Golgi apparatus • cytosol • adherens junction Biological process • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules • regulation of cell migration • response to hypoxia • positive regulation of MAP kinase activity • positive regulation of protein complex assembly • GO:0043087, GO:0032313, GO:0032319, GO:0032314, GO:0043088 regulation of GTPase activity • wound healing, spreading of epidermal cells • positive regulation of kinase activity • positive regulation of cellular biosynthetic process • negative regulation of transcription from RNA polymerase II promoter • transcription, DNA-templated • positive regulation of gene silencing by miRNA • regulation of cellular response to hypoxia • cellular protein localization • glycerophospholipid biosynthetic process • focal adhesion assembly • cell adhesion • G2/M transition of mitotic cell cycle • gene silencing by miRNA • negative regulation of hippo signaling • positive regulation of I-kappaB kinase/NF-kappaB signaling • cell cycle • gene silencing by RNA • lamellipodium assembly • negative regulation of kinase activity • regulation of transcription, DNA-templated • cytoskeleton organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	84962	16475
Ensembl	ENSG00000129474	ENSMUSG00000022178
UniProt	Q96IF1	Q91XC0
RefSeq (mRNA)	NM_198086 NM_001289097 NM_032876	NM_010590
RefSeq (protein)	NP_001276026 NP_116265 NP_932352	NP_034720
Location (UCSC)	Chr 14: 22.97 – 22.98 Mb	Chr 14: 54.57 – 54.58 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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[7] and SLC1A2.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000129474 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022178 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Goyal RK, Lin P, Kanungo J, Payne AS, Muslin AJ, Longmore GD (Jun 1999). "Ajuba, a Novel LIM Protein, Interacts with Grb2, Augments Mitogen-Activated Protein Kinase Activity in Fibroblasts, and Promotes Meiotic Maturation of Xenopus Oocytes in a Grb2- and Ras-Dependent Manner". Mol Cell Biol. 19 (6): 4379–89. doi:10.1128/MCB.19.6.4379. PMC 104397. PMID 10330178.
6. "Entrez Gene: JUB jub, ajuba homolog (Xenopus laevis)".
7. Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (Jun 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.
8. Marie H, Billups D, Bedford FK, Dumoulin A, Goyal RK, Longmore GD, Moss SJ, Attwell D (Feb 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.

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. doi:10.1091/mbc.11.10.3299. PMC 14993. PMID 11029037.
• Marie H, Billups D, Bedford FK, Dumoulin A, Goyal RK, Longmore GD, Moss SJ, Attwell D (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, Epple H, Kittler JT, Meek L, Moss SJ, Troyanovsky S, Attwell D, Longmore GD, Braga VM (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.
• Hirota T, Kunitoku N, Sasayama T, Marumoto T, Zhang D, Nitta M, Hatakeyama K, Saya H (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.
• Pratt SJ, Epple H, Ward M, Feng Y, Braga VM, Longmore GD (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.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (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, Song C, Anderson RA, Longmore GD (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.
• 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.
• Abe Y, Ohsugi M, Haraguchi K, Fujimoto J, Yamamoto T (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, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (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.