MGP Database

MGP006192

UniProt Annotations

Entry Information
Gene Nameajuba LIM protein
Protein EntryAJUBA_HUMAN
UniProt IDQ96IF1
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96IF1-1; Sequence=Displayed; Name=2; IsoId=Q96IF1-2; Sequence=VSP_044227;
DomainLIM-2 and LIM-3 domains mediate the interaction with the N-terminal region of AURKA. The association between LATS2 and AJUBA required the second LIM domain of AJUBA.
DomainLIM region interacts with CTNNA1. The preLIM region binds directly actin filaments.
FunctionAdapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell- cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1- induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. {ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:15870274, ECO:0000269|PubMed:16413547, ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22286099}.
InteractionQ9NRM7:LATS2; NbExp=6; IntAct=EBI-949782, EBI-3506895; P31947:SFN; NbExp=2; IntAct=EBI-949782, EBI-476295;
Miscellaneous'Ajuba' means 'curiosity' in Urdu, an Indian dialect.
PtmPhosphorylated by LATS2 during mitosis. Phosphorylated by AURKA. {ECO:0000269|PubMed:18669648, ECO:0000269|PubMed:18691976, ECO:0000269|PubMed:20068231, ECO:0000269|PubMed:21406692}.
SimilarityBelongs to the zyxin/ajuba family. {ECO:0000305}.
SimilarityContains 3 LIM zinc-binding domains. {ECO:0000255|PROSITE-ProRule:PRU00125}.
Subcellular LocationCytoplasm, cytoskeleton. Cell membrane. Cell junction. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, P-body. Note=Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase. Preferentially co- localizes with cadherin-adhesive complexes at sites of cell-cell contacts. Colocalizes with GFI1 in the nucleus.
SubunitInteracts with GRB2, PIP5K1B and SLC1A2 (By similarity). Interacts with AURKA; the interaction occurs during mitosis and both proteins are phosphorylated as they form a complex. Interacts with CTNNA1 and with F-actin. Interacts with LATS2; the interaction occurs during mitosis and the complex regulates organization of the spindle apparatus through recruitment of TUBG to the centrosome. Forms a complex with SQSTM1, PRKCZ and TRAF6. Component of the GFI1-AJUBA-HDAC1 repressor complex. Interacts directly (via the LIM domains) with GFI1; the interaction results in the HDAC-dependent corepression of a subset of GFI1 target genes, and is independent of the GFI1 SNAG domain. Interacts with HDAC1, HDAC2 and HDAC3. Interacts with SNAI2/SLUG (via SNAG domain) and SCRT1 (via SNAG domain) (By similarity). Interacts with EIF4E, AGO1, AGO2, DCP2, DDX6, LATS1, LATS2, SAV1, EGLN2/PHD1 and EGLN3/PHD3. Interacts (via LIM domains) with isoform 1 and isoform 3 of VHL. Interacts (via LIM domains) with SNAI1 (via SNAG domain). {ECO:0000250, ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:15870274, ECO:0000269|PubMed:16413547, ECO:0000269|PubMed:17909014, ECO:0000269|PubMed:18331720, ECO:0000269|PubMed:18805794, ECO:0000269|PubMed:20303269, ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:22286099}.
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